data_11547 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 11547 _Entry.Title ; the pure alternative state of ubiquitin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2013-12-04 _Entry.Accession_date 2013-12-05 _Entry.Last_release_date 2014-02-04 _Entry.Original_release_date 2014-02-04 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1.1.61 _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 Soichiro Kitazawa . . . 11547 2 Tomoshi Kameda . . . 11547 3 Ayumi Kumo . . . 11547 4 Maho Utsumi . . . 11547 5 Nicola Baxter . . . 11547 6 Koichi Kato . . . 11547 7 Mike Williamson . P. . 11547 8 Ryo Kitahara . . . 11547 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' . 11547 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'alternatively folded state' . 11547 'high-pressure NMR' . 11547 ubiquitin . 11547 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 11547 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 337 11547 '15N chemical shifts' 79 11547 '1H chemical shifts' 564 11547 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 . . 2014-02-04 2013-12-04 original author . 11547 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2RSU 'alternatively folded state is 70% populated' 11547 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 11547 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 24401037 _Citation.Full_citation . _Citation.Title 'Close identity between the alternatively folded state N2 of ubiquitin and the conformation of the protein bound to ubiquitin-activating enzyme' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 53 _Citation.Journal_issue 3 _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 447 _Citation.Page_last 449 _Citation.Year 2014 _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 Soichiro Kitazawa . . . 11547 1 2 Tomoshi Kameda . . . 11547 1 3 Ayumi Kumo . . . 11547 1 4 Maho Utsumi . . . 11547 1 5 Nicola Baxter . . . 11547 1 6 Koichi Kato . . . 11547 1 7 Mike Williamson . P. . 11547 1 8 Ryo Kitahara . . . 11547 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 11547 _Assembly.ID 1 _Assembly.Name 'the pure alternative state of ubiquitin' _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 ubiquitin 1 $ubiquitin A . yes native no no . . . 11547 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 2RU6 . . . . 'Structure from this entry' . 11547 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_ubiquitin _Entity.Sf_category entity _Entity.Sf_framecode ubiquitin _Entity.Entry_ID 11547 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name ubiquitin _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 ; MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ NRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG ; _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 76 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state . _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 8562.888 _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 . . . . . 100.00 76 100.00 100.00 4.42e-46 . . . . 11547 1 2 no BMRB 15047 . denatured_ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 3 no BMRB 15410 . Ubi . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 4 no BMRB 15689 . UBB . . . . . 98.68 103 97.33 98.67 3.57e-43 . . . . 11547 1 5 no BMRB 15907 . Ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 6 no BMRB 16582 . Ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 7 no BMRB 16626 . Ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 8 no BMRB 16895 . UBB+1 . . . . . 98.68 103 97.33 98.67 3.57e-43 . . . . 11547 1 9 no BMRB 17181 . ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 10 no BMRB 17439 . ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 11 no BMRB 17769 . Ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 12 no BMRB 17919 . entity . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 13 no BMRB 18582 . ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 14 no BMRB 18583 . ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 15 no BMRB 18584 . ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 16 no BMRB 18610 . Ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 17 no BMRB 18611 . Ubiquitin_A_state . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 18 no BMRB 18737 . UBIQUITIN . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 19 no BMRB 19406 . entity . . . . . 100.00 152 98.68 98.68 3.20e-44 . . . . 11547 1 20 no BMRB 19412 . entity . . . . . 100.00 152 98.68 98.68 3.20e-44 . . . . 11547 1 21 no BMRB 25070 . Ubiquitin . . . . . 100.00 79 98.68 98.68 3.56e-45 . . . . 11547 1 22 no BMRB 25123 . Ubiquitin . . . . . 94.74 72 98.61 98.61 4.36e-42 . . . . 11547 1 23 no BMRB 26604 . Ubiquitin_(microcrystalline) . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 24 no BMRB 4245 . ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 25 no BMRB 4375 . Ubiquitin . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 26 no PDB 1AAR . "Structure Of A Diubiquitin Conjugate And A Model For Interaction With Ubiquitin Conjugating Enzyme (E2)" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 27 no PDB 1CMX . "Structural Basis For The Specificity Of Ubiquitin C- Terminal Hydrolases" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 28 no PDB 1D3Z . "Ubiquitin Nmr Structure" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 29 no PDB 1F9J . "Structure Of A New Crystal Form Of Tetraubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 30 no PDB 1FXT . "Structure Of A Conjugating Enzyme-Ubiquitin Thiolester Complex" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 31 no PDB 1G6J . "Structure Of Recombinant Human Ubiquitin In Aot Reverse Micelles" . . . . . 98.68 76 98.67 98.67 3.79e-44 . . . . 11547 1 32 no PDB 1GJZ . "Solution Structure Of A Dimeric N-Terminal Fragment Of Human Ubiquitin" . . . . . 67.11 53 98.04 98.04 1.44e-25 . . . . 11547 1 33 no PDB 1NBF . "Crystal Structure Of A Ubp-Family Deubiquitinating Enzyme In Isolation And In Complex With Ubiquitin Aldehyde" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 34 no PDB 1P3Q . "Mechanism Of Ubiquitin Recognition By The Cue Domain Of Vps9" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 35 no PDB 1Q5W . "Ubiquitin Recognition By Npl4 Zinc-Fingers" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 36 no PDB 1S1Q . "Tsg101(Uev) Domain In Complex With Ubiquitin" . . . . . 98.68 76 98.67 98.67 3.79e-44 . . . . 11547 1 37 no PDB 1TBE . "Structure Of Tetraubiquitin Shows How Multiubiquitin Chains Can Be Formed" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 38 no PDB 1UBI . "Synthetic Structural And Biological Studies Of The Ubiquitin System. Part 1" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 39 no PDB 1UBQ . "Structure Of Ubiquitin Refined At 1.8 Angstroms Resolution" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 40 no PDB 1UZX . "A Complex Of The Vps23 Uev With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 41 no PDB 1V80 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 42 no PDB 1V81 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 43 no PDB 1VX7 . "Cryo-em Structure Of The Plasmodium Falciparum 80s Ribosome Bound To The Anti-protozoan Drug Emetine, Large Subunit (protein On" . . . . . 100.00 128 97.37 98.68 1.06e-44 . . . . 11547 1 44 no PDB 1WR6 . "Crystal Structure Of Gga3 Gat Domain In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 45 no PDB 1WRD . "Crystal Structure Of Tom1 Gat Domain In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 46 no PDB 1XD3 . "Crystal Structure Of Uchl3-Ubvme Complex" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 47 no PDB 1XQQ . "Simultaneous Determination Of Protein Structure And Dynamics" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 48 no PDB 1YD8 . "Complex Of Human Gga3 Gat Domain And Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 49 no PDB 1YIW . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.62e-44 . . . . 11547 1 50 no PDB 1YX5 . "Solution Structure Of S5a Uim-1UBIQUITIN COMPLEX" . . . . . 100.00 98 98.68 98.68 1.64e-45 . . . . 11547 1 51 no PDB 1YX6 . "Solution Structure Of S5a Uim-2UBIQUITIN COMPLEX" . . . . . 100.00 98 98.68 98.68 1.64e-45 . . . . 11547 1 52 no PDB 1ZGU . "Solution Structure Of The Human Mms2-Ubiquitin Complex" . . . . . 100.00 76 97.37 98.68 8.73e-45 . . . . 11547 1 53 no PDB 2AYO . "Structure Of Usp14 Bound To Ubquitin Aldehyde" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 54 no PDB 2BGF . "Nmr Structure Of Lys48-Linked Di-Ubiquitin Using Chemical Shift Perturbation Data Together With Rdcs And 15n- Relaxation Data" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 55 no PDB 2C7M . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 56 no PDB 2C7N . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 57 no PDB 2D3G . "Double Sided Ubiquitin Binding Of Hrs-Uim" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 58 no PDB 2DEN . "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 59 no PDB 2DX5 . "The Complex Structure Between The Mouse Eap45-Glue Domain And Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 60 no PDB 2FCQ . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin With A Cubic Space Group" . . . . . 100.00 76 97.37 98.68 1.62e-44 . . . . 11547 1 61 no PDB 2FID . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 62 no PDB 2FIF . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 63 no PDB 2FUH . "Solution Structure Of The Ubch5cUB NON-Covalent Complex" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 64 no PDB 2G45 . "Co-Crystal Structure Of Znf Ubp Domain From The Deubiquitinating Enzyme Isopeptidase T (Isot) In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 65 no PDB 2GMI . Mms2UBC13~UBIQUITIN . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 66 no PDB 2HD5 . "Usp2 In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 67 no PDB 2HTH . "Structural Basis For Ubiquitin Recognition By The Human Eap45ESCRT-Ii Glue Domain" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 68 no PDB 2IBI . "Covalent Ubiquitin-Usp2 Complex" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 69 no PDB 2J7Q . "Crystal Structure Of The Ubiquitin-Specific Protease Encoded By Murine Cytomegalovirus Tegument Protein M48 In Complex With A U" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 70 no PDB 2JF5 . "Crystal Structure Of Lys63-Linked Di-Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 71 no PDB 2JRI . "Solution Structure Of The Josephin Domain Of Ataxin-3 In Complex With Ubiquitin Molecule." . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 72 no PDB 2JY6 . "Solution Structure Of The Complex Of Ubiquitin And Ubiquilin 1 Uba Domain" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 73 no PDB 2JZZ . "Solid-State Nmr Structure Of Microcrystalline Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 74 no PDB 2K25 . "Automated Nmr Structure Of The Ubb By Fapsy" . . . . . 98.68 103 97.33 98.67 3.57e-43 . . . . 11547 1 75 no PDB 2K39 . "Recognition Dynamics Up To Microseconds Revealed From Rdc Derived Ubiquitin Ensemble In Solution" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 76 no PDB 2K6D . "Cin85 Sh3-C Domain In Complex With Ubiquitin" . . . . . 98.68 76 98.67 98.67 2.08e-44 . . . . 11547 1 77 no PDB 2K8B . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Cis Isomer In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 78 no PDB 2K8C . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Trans Isomer In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 79 no PDB 2KDE . "Nmr Structure Of Major S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 80 no PDB 2KDF . "Nmr Structure Of Minor S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 81 no PDB 2KHW . "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" . . . . . 100.00 79 98.68 98.68 3.56e-45 . . . . 11547 1 82 no PDB 2KJH . "Nmr Based Structural Model Of The Ubch8-Ubiquitin Complex" . . . . . 98.68 76 98.67 98.67 2.08e-44 . . . . 11547 1 83 no PDB 2KLG . "Pere Nmr Structure Of Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 84 no PDB 2KN5 . "A Correspondence Between Solution-State Dynamics Of An Individual Protein And The Sequence And Conformational Diversity Of Its " . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 85 no PDB 2KOX . "Nmr Residual Dipolar Couplings Identify Long Range Correlated Motions In The Backbone Of The Protein Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 86 no PDB 2KTF . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 87 no PDB 2KWU . "Solution Structure Of Ubm2 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 88 no PDB 2KWV . "Solution Structure Of Ubm1 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 89 no PDB 2KX0 . "The Solution Structure Of Ubb+1, Frameshift Mutant Of Ubiquitin B" . . . . . 98.68 103 97.33 98.67 3.57e-43 . . . . 11547 1 90 no PDB 2L0F . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 (P692a Mutant) In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 91 no PDB 2L0T . "Solution Structure Of The Complex Of Ubiquitin And The Vhs Domain Of Stam2" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 92 no PDB 2L3Z . "Proton-Detected 4d Dream Solid-State Nmr Structure Of Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 93 no PDB 2LD9 . "Backbone Structure Of Ubiquitin Determined Using Backbone Amide Noes And Backbone N-H And N-C Rdcs" . . . . . 100.00 77 98.68 98.68 4.23e-45 . . . . 11547 1 94 no PDB 2LJ5 . "Description Of The Structural Fluctuations Of Proteins From Structure- Based Calculations Of Residual Dipolar Couplings" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 95 no PDB 2LVO . "Structure Of The Gp78cue Domain Bound To Monubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 96 no PDB 2LVP . "Gp78cue Domain Bound To The Distal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 97 no PDB 2LVQ . "Gp78cue Domain Bound To The Proximal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 98 no PDB 2LZ6 . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 99 no PDB 2MBB . "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" . . . . . 100.00 78 98.68 98.68 3.04e-45 . . . . 11547 1 100 no PDB 2MBH . "Nmr Structure Of Eklf(22-40)/ubiquitin Complex" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 101 no PDB 2MBO . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 0 Mm Nacl" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 102 no PDB 2MBQ . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 150 Mm Nacl" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 103 no PDB 2MCN . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 104 no PDB 2MJ5 . "Structure Of The Uba Domain Of Human Nbr1 In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 105 no PDB 2MJB . "Solution Nmr Structure Of Ubiquitin Refined Against Dipolar Couplings In 4 Media" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 106 no PDB 2MOR . "A Tensor-free Method For The Structural And Dynamical Refinement Of Proteins Using Residual Dipolar Couplings" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 107 no PDB 2MRE . "Nmr Structure Of The Rad18-ubz/ubiquitin Complex" . . . . . 100.00 79 98.68 98.68 3.56e-45 . . . . 11547 1 108 no PDB 2MRO . "Structure Of The Complex Of Ubiquitin And The Uba Domain From Dna- Damage-inducible 1 Protein (ddi1)" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 109 no PDB 2MSG . "Solid-state Nmr Structure Of Ubiquitin" . . . . . 94.74 72 98.61 98.61 4.36e-42 . . . . 11547 1 110 no PDB 2MUR . "Solution Structure Of The Human Faap20 Ubz-ubiquitin Complex" . . . . . 100.00 78 98.68 98.68 3.04e-45 . . . . 11547 1 111 no PDB 2MWS . "Structure Of The Complex Of Ubiquitin And The Ubiquitin-like (ubl) Domain Of Ddi1" . . . . . 100.00 76 97.37 97.37 2.15e-44 . . . . 11547 1 112 no PDB 2N2K . "Ensemble Structure Of The Closed State Of Lys63-linked Diubiquitin In The Absence Of A Ligand" . . . . . 93.42 71 98.59 98.59 3.65e-41 . . . . 11547 1 113 no PDB 2NR2 . "The Mumo (Minimal Under-Restraining Minimal Over- Restraining) Method For The Determination Of Native States Ensembles Of Prote" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 114 no PDB 2O6V . "Crystal Structure And Solution Nmr Studies Of Lys48-Linked Tetraubiquitin At Neutral Ph" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 115 no PDB 2OJR . "Structure Of Ubiquitin Solved By Sad Using The Lanthanide- Binding Tag" . . . . . 100.00 111 98.68 98.68 1.89e-44 . . . . 11547 1 116 no PDB 2OOB . "Crystal Structure Of The Uba Domain From Cbl-B Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 117 no PDB 2PE9 . "Nmr Based Structure Of The Open Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Tenso" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 118 no PDB 2PEA . "Nmr Based Structure Of The Closed Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Ten" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 119 no PDB 2QHO . "Crystal Structure Of The Uba Domain From Edd Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 120 no PDB 2RR9 . "The Solution Structure Of The K63-Ub2:tuims Complex" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 121 no PDB 2RSU . "Alternative Structure Of Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.42e-46 . . . . 11547 1 122 no PDB 2RU6 . "The Pure Alternative State Of Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.42e-46 . . . . 11547 1 123 no PDB 2W9N . "Crystal Structure Of Linear Di-Ubiquitin" . . . . . 98.68 152 98.67 98.67 3.05e-43 . . . . 11547 1 124 no PDB 2WDT . "Crystal Structure Of Plasmodium Falciparum Uchl3 In Complex With The Suicide Inhibitor Ubvme" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 125 no PDB 2WWZ . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P212121" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 126 no PDB 2WX0 . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P21" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 127 no PDB 2WX1 . "Tab2 Nzf Domain In Complex With Lys63-Linked Tri-Ubiquitin, P212121" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 128 no PDB 2XBB . "Nedd4 Hect:ub Complex" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 129 no PDB 2XEW . "Crystal Structure Of K11-Linked Diubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 130 no PDB 2XK5 . "Crystal Structure Of K6-Linked Diubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 131 no PDB 2Y5B . "Structure Of Usp21 In Complex With Linear Diubiquitin-Aldehyde" . . . . . 98.68 152 98.67 98.67 2.23e-43 . . . . 11547 1 132 no PDB 2Z59 . "Complex Structures Of Mouse Rpn13 (22-130aa) And Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 133 no PDB 2ZCC . "Ubiquitin Crystallized Under High Pressure" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 134 no PDB 2ZNV . "Crystal Structure Of Human Amsh-Lp Dub Domain In Complex With Lys63-Linked Ubiquitin Dimer" . . . . . 100.00 77 98.68 98.68 3.88e-45 . . . . 11547 1 135 no PDB 2ZVN . "Nemo Cozi Domain Incomplex With Diubiquitin In P212121 Space Group" . . . . . 100.00 154 98.68 98.68 3.14e-44 . . . . 11547 1 136 no PDB 2ZVO . "Nemo Cozi Domain In Complex With Diubiquitin In C2 Space Group" . . . . . 100.00 154 98.68 98.68 3.14e-44 . . . . 11547 1 137 no PDB 3A1Q . "Crystal Structure Of The Mouse Rap80 Uims In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 100.00 77 98.68 98.68 3.88e-45 . . . . 11547 1 138 no PDB 3A33 . "Ubch5b~ubiquitin Conjugate" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 139 no PDB 3A9J . "Crystal Structure Of The Mouse Tab2-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 100.00 77 98.68 98.68 3.88e-45 . . . . 11547 1 140 no PDB 3A9K . "Crystal Structure Of The Mouse Tab3-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 100.00 77 98.68 98.68 3.88e-45 . . . . 11547 1 141 no PDB 3AI5 . "Crystal Structure Of Yeast Enhanced Green Fluorescent Protein- Ubiquitin Fusion Protein" . . . . . 97.37 307 98.65 98.65 1.10e-40 . . . . 11547 1 142 no PDB 3ALB . "Cyclic Lys48-Linked Tetraubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 143 no PDB 3AUL . "Crystal Structure Of Wild-Type Lys48-Linked Diubiquitin In An Open Conformation" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 144 no PDB 3AXC . "Crystal Structure Of Linear Diubiquitin" . . . . . 100.00 154 98.68 98.68 3.14e-44 . . . . 11547 1 145 no PDB 3B08 . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 100.00 152 98.68 98.68 3.20e-44 . . . . 11547 1 146 no PDB 3B0A . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 100.00 152 98.68 98.68 3.20e-44 . . . . 11547 1 147 no PDB 3BY4 . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 148 no PDB 3C0R . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 149 no PDB 3DVG . "Crystal Structure Of K63-Specific Fab Apu.3a8 Bound To K63-Linked Di- Ubiquitin" . . . . . 100.00 80 98.68 98.68 4.75e-45 . . . . 11547 1 150 no PDB 3DVN . "Crystal Structure Of K63-specific Fab Apu2.16 Bound To K63-linked Di- Ubiquitin" . . . . . 100.00 80 98.68 98.68 4.75e-45 . . . . 11547 1 151 no PDB 3EEC . "X-Ray Structure Of Human Ubiquitin Cd(Ii) Adduct" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 152 no PDB 3EFU . "X-Ray Structure Of Human Ubiquitin-Hg(Ii) Adduct" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 153 no PDB 3EHV . "X-Ray Structure Of Human Ubiquitin Zn(Ii) Adduct" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 154 no PDB 3H1U . "Structure Of Ubiquitin In Complex With Cd Ions" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 155 no PDB 3H7P . "Crystal Structure Of K63-Linked Di-Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 156 no PDB 3H7S . "Crystal Structures Of K63-Linked Di- And Tri-Ubiquitin Reveal A Highly Extended Chain Architecture" . . . . . 100.00 76 97.37 97.37 1.50e-42 . . . . 11547 1 157 no PDB 3HM3 . "The Structure And Conformation Of Lys-63 Linked Tetra-Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 158 no PDB 3I3T . "Crystal Structure Of Covalent Ubiquitin-usp21 Complex" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 159 no PDB 3IFW . "Crystal Structure Of The S18y Variant Of Ubiquitin Carboxy T Hydrolase L1 Bound To Ubiquitin Vinylmethylester." . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 160 no PDB 3IHP . "Covalent Ubiquitin-Usp5 Complex" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 161 no PDB 3JSV . "Crystal Structure Of Mouse Nemo Cozi In Complex With Lys63- Linked Di-Ubiquitin" . . . . . 100.00 77 98.68 98.68 3.88e-45 . . . . 11547 1 162 no PDB 3JVZ . E2~ubiquitin-Hect . . . . . 100.00 81 98.68 98.68 3.68e-45 . . . . 11547 1 163 no PDB 3JW0 . E2~ubiquitin-Hect . . . . . 100.00 81 98.68 98.68 3.68e-45 . . . . 11547 1 164 no PDB 3K9O . "The Crystal Structure Of E2-25k And Ubb+1 Complex" . . . . . 98.68 96 98.67 98.67 6.80e-44 . . . . 11547 1 165 no PDB 3K9P . "The Crystal Structure Of E2-25k And Ubiquitin Complex" . . . . . 100.00 79 98.68 98.68 3.56e-45 . . . . 11547 1 166 no PDB 3KVF . "Crystal Structure Of The I93m Mutant Of Ubiquitin Carboxy Te Hydrolase L1 Bound To Ubiquitin Vinylmethylester" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 167 no PDB 3KW5 . "Crystal Structure Of Ubiquitin Carboxy Terminal Hydrolase L1 Ubiquitin Vinylmethylester" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 168 no PDB 3LDZ . "Crystal Structure Of Human Stam1 Vhs Domain In Complex With Ubiquitin" . . . . . 96.05 73 98.63 98.63 1.05e-42 . . . . 11547 1 169 no PDB 3M3J . "A New Crystal Form Of Lys48-Linked Diubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 170 no PDB 3MHS . "Structure Of The Saga Ubp8SGF11SUS1SGF73 DUB MODULE BOUND Ubiquitin Aldehyde" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 171 no PDB 3MTN . "Usp21 In Complex With A Ubiquitin-based, Usp21-specific Inhibitor" . . . . . 88.16 85 97.01 97.01 8.27e-37 . . . . 11547 1 172 no PDB 3N30 . "Crystal Structure Of Cubic Zn3-Hub (Human Ubiquitin) Adduct" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 173 no PDB 3N32 . "The Crystal Structure Of Human Ubiquitin Adduct With Zeise's Salt" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 174 no PDB 3NHE . "High Resolution Structure (1.26a) Of Usp2a In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 175 no PDB 3NOB . "Structure Of K11-linked Di-ubiquitin" . . . . . 100.00 78 98.68 98.68 3.04e-45 . . . . 11547 1 176 no PDB 3NS8 . "Crystal Structure Of An Open Conformation Of Lys48-Linked Diubiquitin At Ph 7.5" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 177 no PDB 3O65 . "Crystal Structure Of A Josephin-Ubiquitin Complex: Evolutionary Restraints On Ataxin-3 Deubiquitinating Activity" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 178 no PDB 3OFI . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 179 no PDB 3OJ3 . "Crystal Structure Of The A20 Znf4 And Ubiquitin Complex" . . . . . 100.00 79 98.68 98.68 3.56e-45 . . . . 11547 1 180 no PDB 3OJ4 . "Crystal Structure Of The A20 Znf4, Ubiquitin And Ubch5a Complex" . . . . . 100.00 79 98.68 98.68 3.56e-45 . . . . 11547 1 181 no PDB 3ONS . "Crystal Structure Of Human Ubiquitin In A New Crystal Form" . . . . . 94.74 72 98.61 98.61 4.36e-42 . . . . 11547 1 182 no PDB 3PHD . "Crystal Structure Of Human Hdac6 In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 183 no PDB 3PHW . "Otu Domain Of Crimean Congo Hemorrhagic Fever Virus In Complex With Ubiquitin" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 184 no PDB 3PRM . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 185 no PDB 3PRP . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 186 no PDB 3PT2 . "Structure Of A Viral Otu Domain Protease Bound To Ubiquitin" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 187 no PDB 3PTF . "X-Ray Structure Of The Non-Covalent Complex Between Ubch5a And Ubiquitin" . . . . . 100.00 79 98.68 98.68 3.56e-45 . . . . 11547 1 188 no PDB 3Q3F . "Engineering Domain-Swapped Binding Interfaces By Mutually Exclusive Folding: Insertion Of Ubiquitin Into Position 103 Of Barnas" . . . . . 98.68 189 98.67 98.67 3.79e-43 . . . . 11547 1 189 no PDB 3RUL . "New Strategy To Analyze Structures Of Glycopeptide-Target Complexes" . . . . . 98.68 79 98.67 98.67 2.21e-44 . . . . 11547 1 190 no PDB 3TBL . "Structure Of Mono-ubiquitinated Pcna: Implications For Dna Polymerase Switching And Okazaki Fragment Maturation" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 191 no PDB 3TMP . "The Catalytic Domain Of Human Deubiquitinase Duba In Complex With Ubiquitin Aldehyde" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 192 no PDB 3U30 . "Crystal Structure Of A Linear-Specific Ubiquitin Fab Bound To Linear Ubiquitin" . . . . . 100.00 172 98.68 98.68 3.73e-44 . . . . 11547 1 193 no PDB 3UGB . "Ubch5c~ubiquitin Conjugate" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 194 no PDB 3VDZ . "Tailoring Encodable Lanthanide-Binding Tags As Mri Contrast Agents: Xq-Dse3-Ubiquitin At 2.4 Angstroms" . . . . . 100.00 111 98.68 98.68 9.01e-45 . . . . 11547 1 195 no PDB 3VFK . "The Structure Of Monodechloro-teicoplanin In Complex With Its Ligand, Using Ubiquitin As A Ligand Carrier" . . . . . 98.68 79 98.67 98.67 2.21e-44 . . . . 11547 1 196 no PDB 3VHT . "Crystal Structure Of Gfp-Wrnip1 Ubz Domain Fusion Protein In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 197 no PDB 3VUW . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form I" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 198 no PDB 3VUX . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form Ii" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 199 no PDB 3VUY . "Crystal Structure Of A20 Zf7 In Complex With Linear Tetraubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 200 no PDB 3WWQ . "Crystal Structure Of Faap20 Ubz Domain In Complex With Lys63-linked Diubiquitin" . . . . . 100.00 77 98.68 98.68 3.88e-45 . . . . 11547 1 201 no PDB 3WXE . "Crystal Structure Of Cyld Usp Domain (c596s) In Complex With Met1- Linked Diubiquitin" . . . . . 94.74 148 98.61 98.61 4.19e-41 . . . . 11547 1 202 no PDB 3WXF . "Crystal Structure Of Cyld Usp Domain (c596s E674q) In Complex With Met1-linked Diubiquitin" . . . . . 94.74 148 98.61 98.61 4.19e-41 . . . . 11547 1 203 no PDB 3WXG . "Crystal Structure Of Cyld Usp Domain (c596a) In Complex With Lys63- Linked Diubiquitin" . . . . . 94.74 72 98.61 98.61 4.36e-42 . . . . 11547 1 204 no PDB 3ZLZ . "Lys6-linked Tri-ubiquitin" . . . . . 100.00 76 97.37 98.68 8.73e-45 . . . . 11547 1 205 no PDB 3ZNH . "Crimean Congo Hemorrhagic Fever Virus Otu Domain In Complex With Ubiquitin-propargyl." . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 206 no PDB 3ZNI . "Structure Of Phosphotyr363-cbl-b - Ubch5b-ub - Zap-70 Peptide Complex" . . . . . 100.00 81 98.68 98.68 3.68e-45 . . . . 11547 1 207 no PDB 3ZNZ . "Crystal Structure Of Otulin Otu Domain (c129a) In Complex With Met1-di Ubiquitin" . . . . . 100.00 152 98.68 98.68 3.20e-44 . . . . 11547 1 208 no PDB 4AP4 . "Rnf4 - Ubch5a - Ubiquitin Heterotrimeric Complex" . . . . . 100.00 80 98.68 98.68 3.78e-45 . . . . 11547 1 209 no PDB 4AUQ . "Structure Of Birc7-Ubch5b-Ub Complex." . . . . . 100.00 81 98.68 98.68 3.68e-45 . . . . 11547 1 210 no PDB 4BBN . "Nedd4 Hect-ub:ub Complex" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 211 no PDB 4BOS . "Structure Of Otud2 Otu Domain In Complex With Ubiquitin K11- Linked Peptide" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 212 no PDB 4BOZ . "Structure Of Otud2 Otu Domain In Complex With K11-linked Di Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 213 no PDB 4BVU . "Structure Of Shigella Effector Ospg In Complex With Host Ubch5c-ubiquitin Conjugate" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 214 no PDB 4CXC . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 215 no PDB 4CXD . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 216 no PDB 4D5L . "Cryo-em Structures Of Ribosomal 80s Complexes With Termination Factors And Cricket Paralysis Virus Ires Reveal The Ires In The " . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 217 no PDB 4D61 . "Cryo-em Structures Of Ribosomal 80s Complexes With Termination Factors And Cricket Paralysis Virus Ires Reveal The Ires In The " . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 218 no PDB 4DDG . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 219 no PDB 4DDI . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 220 no PDB 4DHJ . "The Structure Of A Ceotub1 Ubiquitin Aldehyde Ubc13~ub Complex" . . . . . 98.68 76 98.67 98.67 2.08e-44 . . . . 11547 1 221 no PDB 4DHZ . "The Structure Of HCEOTUB1-Ubiquitin Aldehyde-Ubc13~ub" . . . . . 98.68 76 98.67 98.67 2.08e-44 . . . . 11547 1 222 no PDB 4FJV . "Crystal Structure Of Human Otubain2 And Ubiquitin Complex" . . . . . 100.00 86 98.68 98.68 6.07e-45 . . . . 11547 1 223 no PDB 4HXD . "Diversity Of Ubiquitin And Isg15 Specificity Amongst Nairoviruses Viral Ovarian Tumor Domain Proteases" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 224 no PDB 4I6N . "Crystal Structure Of Trichinella Spiralis Uch37 Catalytic Domain Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 97.37 75 98.65 98.65 2.56e-43 . . . . 11547 1 225 no PDB 4IG7 . "Crystal Structure Of Trichinella Spiralis Uch37 Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 226 no PDB 4IUM . "Equine Arteritis Virus Papain-like Protease 2 (plp2) Covalently Bound To Ubiquitin" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 227 no PDB 4JIO . "Bro1 V Domain And Ubiquitin" . . . . . 100.00 76 97.37 97.37 2.43e-44 . . . . 11547 1 228 no PDB 4JQW . "Crystal Structure Of A Complex Of Nod1 Card And Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 229 no PDB 4K1R . "Crystal Structure Of Schizosaccharomyces Pombe Sst2 Catalytic Domain And Ubiquitin" . . . . . 100.00 81 98.68 98.68 6.63e-45 . . . . 11547 1 230 no PDB 4K7S . "Crystal Structure Of Zn2-hub (human Ubiquitin) Adduct From A Solution 35 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 231 no PDB 4K7U . "Crystal Structure Of Zn2.3-hub (human Ubiquitin) Adduct From A Solution 70 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 232 no PDB 4K7W . "Crystal Structure Of Zn3-hub(human Ubiquitin) Adduct From A Solution 100 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 233 no PDB 4KSK . "Gumby/fam105b In Complex With Ubiquitin" . . . . . 100.00 80 98.68 98.68 3.78e-45 . . . . 11547 1 234 no PDB 4KSL . "Gumby/fam105b In Complex With Linear Di-ubiquitin" . . . . . 100.00 156 98.68 98.68 3.44e-44 . . . . 11547 1 235 no PDB 4KZX . "Rabbit 40s Ribosomal Subunit In Complex With Eif1." . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 236 no PDB 4KZY . "Rabbit 40s Ribosomal Subunit In Complex With Eif1 And Eif1a." . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 237 no PDB 4KZZ . "Rabbit 40s Ribosomal Subunit In Complex With Mrna, Initiator Trna And Eif1a" . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 238 no PDB 4LCD . "Structure Of An Rsp5xubxsna3 Complex: Mechanism Of Ubiquitin Ligation And Lysine Prioritization By A Hect E3" . . . . . 97.37 83 98.65 98.65 1.11e-43 . . . . 11547 1 239 no PDB 4LDT . "The Structure Of H/ceotub1-ubiquitin Aldehyde-ubch5b~ub" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 240 no PDB 4LJO . "Structure Of An Active Ligase (hoip)/ubiquitin Transfer Complex" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 241 no PDB 4LJP . "Structure Of An Active Ligase (hoip-h889a)/ubiquitin Transfer Complex" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 242 no PDB 4M0W . "Crystal Structure Of Sars-cov Papain-like Protease C112s Mutant In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 243 no PDB 4MDK . "Cdc34-ubiquitin-cc0651 Complex" . . . . . 100.00 80 98.68 98.68 3.78e-45 . . . . 11547 1 244 no PDB 4MM3 . "Crystal Structure Of Sars-cov Papain-like Protease Plpro In Complex With Ubiquitin Aldehyde" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 245 no PDB 4MSM . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 E286a Mutant Bound To Ubiquitin" . . . . . 100.00 81 98.68 98.68 6.63e-45 . . . . 11547 1 246 no PDB 4MSQ . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 Catalytic Domain Bound To Ubiquitin" . . . . . 100.00 81 98.68 98.68 6.63e-45 . . . . 11547 1 247 no PDB 4NQK . "Structure Of An Ubiquitin Complex" . . . . . 100.00 79 98.68 98.68 6.34e-45 . . . . 11547 1 248 no PDB 4NQL . "The Crystal Structure Of The Dub Domain Of Amsh Orthologue, Sst2 From S. Pombe, In Complex With Lysine 63-linked Diubiquitin" . . . . . 100.00 77 98.68 98.68 3.88e-45 . . . . 11547 1 249 no PDB 4P4H . "Caught-in-action Signaling Complex Of Rig-i 2card Domain And Mavs Card Domain" . . . . . 100.00 79 98.68 98.68 6.34e-45 . . . . 11547 1 250 no PDB 4PIG . "Crystal Structure Of The Ubiquitin K11s Mutant" . . . . . 100.00 76 97.37 97.37 1.69e-44 . . . . 11547 1 251 no PDB 4PIH . "X-ray Crystal Structure Of The K33s Mutant Of Ubiquitin" . . . . . 100.00 76 97.37 97.37 1.69e-44 . . . . 11547 1 252 no PDB 4PQT . "Insights Into The Mechanism Of Deubiquitination By Jamm Deubiquitinases From Co-crystal Structures Of Enzyme With Substrate And" . . . . . 100.00 81 98.68 98.68 6.63e-45 . . . . 11547 1 253 no PDB 4R62 . "Structure Of Rad6~ub" . . . . . 100.00 78 98.68 98.68 3.54e-45 . . . . 11547 1 254 no PDB 4RF0 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 255 no PDB 4RF1 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 98.68 75 98.67 98.67 2.05e-44 . . . . 11547 1 256 no PDB 4S1Z . "Crystal Structure Of Trabid Nzf1 In Complex With K29 Linked Di- Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 257 no PDB 4S22 . "Crystal Structure Of K29 Linked Di-ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 258 no PDB 4UEL . "Uch-l5 In Complex With Ubiquitin-propargyl Bound To The Rpn13 Deubad Domain" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 259 no PDB 4UF6 . "Uch-l5 In Complex With Ubiquitin-propargyl Bound To An Activating Fragment Of Ino80g" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 260 no PDB 4UN2 . "Crystal Structure Of The Uba Domain Of Dsk2 In Complex With Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 261 no PDB 4UPX . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 262 no PDB 4UQ1 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 263 no PDB 4UQ4 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 264 no PDB 4UQ5 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 265 no PDB 4V3K . "Rnf38-ubch5b-ub Complex" . . . . . 100.00 81 98.68 98.68 3.68e-45 . . . . 11547 1 266 no PDB 4V3L . "Rnf38-ub-ubch5b-ub Complex" . . . . . 100.00 81 98.68 98.68 3.68e-45 . . . . 11547 1 267 no PDB 4W20 . "Structure Of The Mammalian 60s Ribosomal Subunit (this Entry Contains The Large Ribosomal Proteins)" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 268 no PDB 4W22 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 269 no PDB 4W23 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Small Ribosomal Subunit)" . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 270 no PDB 4W25 . "Structure Of The Idle Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 271 no PDB 4W27 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 272 no PDB 4W28 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Small Ribosomal Subunit)" . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 273 no PDB 4WHV . Rnf8/ubc13c87k~ub . . . . . 100.00 83 98.68 98.68 8.34e-45 . . . . 11547 1 274 no PDB 4WLR . "Crystal Structure Of Much37-hrpn13 Ctd-hub Complex" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 275 no PDB 4WUR . "The Crystal Structure Of The Mers-cov Papain-like Protease (c111s) With Human Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 276 no PDB 4WZP . "Ser65 Phosphorylated Ubiquitin, Major Conformation" . . . . . 100.00 76 97.37 97.37 2.37e-44 . . . . 11547 1 277 no PDB 4XKL . "Crystal Structure Of Ndp52 Zf2 In Complex With Mono-ubiquitin" . . . . . 100.00 80 98.68 98.68 5.53e-45 . . . . 11547 1 278 no PDB 4XOF . "Observing The Overall Rocking Motion Of A Protein In A Crystal - Orthorhombic Ubiquitin Crystals Without Zinc." . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 279 no PDB 4XOK . "Observing The Overall Rocking Motion Of A Protein In A Crystal." . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 280 no PDB 4XOL . "Observing The Overall Rocking Motion Of A Protein In A Crystal - Cubic Ubiquitin Crystals." . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 281 no PDB 4XYZ . "Crystal Structure Of K33 Linked Di-ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 282 no PDB 4Y1H . "Crystal Structure Of K33 Linked Tri-ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 283 no PDB 4Z9S . "Non-covalent Assembly Of Monoubiquitin That Mimics K11 Poly-ubiquitin" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 284 no PDB 4ZFR . "Catalytic Domain Of Sst2 F403a Mutant Bound To Ubiquitin" . . . . . 100.00 81 98.68 98.68 6.63e-45 . . . . 11547 1 285 no PDB 4ZFT . "Catalytic Domain Of Sst2 F403w Mutant Bound To Ubiquitin" . . . . . 100.00 81 98.68 98.68 6.63e-45 . . . . 11547 1 286 no PDB 5A5B . "Structure Of The 26s Proteasome-ubp6 Complex" . . . . . 98.68 76 98.67 98.67 2.11e-44 . . . . 11547 1 287 no PDB 5AF4 . "Structure Of Lys33-linked Diub" . . . . . 100.00 76 97.37 98.68 8.73e-45 . . . . 11547 1 288 no PDB 5AF5 . "Structure Of Lys33-linked Triub S.g. P 212121" . . . . . 96.05 73 97.26 98.63 2.71e-42 . . . . 11547 1 289 no PDB 5AF6 . "Structure Of Lys33-linked Diub Bound To Trabid Nzf1" . . . . . 100.00 76 97.37 98.68 8.73e-45 . . . . 11547 1 290 no PDB 5AIT . "A Complex Of Of Rnf4-ring Domain, Ubev2, Ubc13-ub (isopeptide Crosslink)" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 291 no PDB 5AIU . "A Complex Of Rnf4-ring Domain, Ubc13-ub (isopeptide Crosslink)" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 292 no PDB 5CAW . "Structure Of Pediculus Humanus Parkin Bound To Phospho-ubiquitin" . . . . . 98.68 76 97.33 97.33 1.45e-43 . . . . 11547 1 293 no DBJ BAA03983 . "polyubiquitin [Rattus norvegicus]" . . . . . 100.00 305 98.68 98.68 1.68e-42 . . . . 11547 1 294 no DBJ BAA09860 . "polyubiquitin [Homo sapiens]" . . . . . 100.00 611 97.37 97.37 6.30e-40 . . . . 11547 1 295 no DBJ BAA11842 . "ubiquitin [Cavia porcellus]" . . . . . 100.00 311 98.68 98.68 1.84e-42 . . . . 11547 1 296 no DBJ BAA11843 . "ubiquitin extention protein [Cavia porcellus]" . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 297 no DBJ BAA23486 . "polyubiquitin [Homo sapiens]" . . . . . 100.00 609 97.37 97.37 3.35e-40 . . . . 11547 1 298 no EMBL CAA25706 . "unnamed protein product [Saccharomyces cerevisiae]" . . . . . 50.00 191 97.37 97.37 2.23e-15 . . . . 11547 1 299 no EMBL CAA26488 . "unnamed protein product [Gallus gallus]" . . . . . 100.00 157 97.37 97.37 1.96e-43 . . . . 11547 1 300 no EMBL CAA28495 . "ubiquitin [Homo sapiens]" . . . . . 100.00 229 98.68 98.68 2.63e-43 . . . . 11547 1 301 no EMBL CAA30815 . "unnamed protein product [Cricetulus sp.]" . . . . . 93.42 223 98.59 98.59 2.47e-39 . . . . 11547 1 302 no EMBL CAA35999 . "ubiquitin [Mus musculus]" . . . . . 100.00 305 98.68 98.68 1.68e-42 . . . . 11547 1 303 no GB AAA28997 . "ubiquitin [Drosophila melanogaster]" . . . . . 100.00 231 98.68 98.68 2.41e-43 . . . . 11547 1 304 no GB AAA28998 . "ubiquitin-hybrid protein precursor [Drosophila melanogaster]" . . . . . 100.00 156 98.68 98.68 8.59e-45 . . . . 11547 1 305 no GB AAA28999 . "ubiquitin, partial [Drosophila melanogaster]" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 306 no GB AAA29000 . "ubiquitin, partial [Drosophila melanogaster]" . . . . . 100.00 76 97.37 97.37 1.79e-44 . . . . 11547 1 307 no GB AAA29001 . "ubiquitin, partial [Drosophila melanogaster]" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 308 no PIR I50437 . "polyubiquitin 4 - chicken [Gallus gallus]" . . . . . 100.00 305 98.68 98.68 1.68e-42 . . . . 11547 1 309 no PIR I51568 . "polyubiquitin - African clawed frog (fragment)" . . . . . 100.00 167 98.68 98.68 4.42e-44 . . . . 11547 1 310 no PIR I65237 . "ubiquitin / ribosomal protein L40, cytosolic [validated] - rat" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 311 no PIR S13928 . "ubiquitin precursor - chicken [Gallus gallus]" . . . . . 100.00 229 98.68 98.68 2.63e-43 . . . . 11547 1 312 no PIR S21083 . "polyubiquitin 5 - Chinese hamster" . . . . . 100.00 381 98.68 98.68 7.54e-42 . . . . 11547 1 313 no PRF 0412265A . ubiquitin . . . . . 98.68 75 97.33 97.33 9.61e-44 . . . . 11547 1 314 no PRF 1101405A . "ubiquitin precursor" . . . . . 50.00 191 97.37 97.37 2.14e-15 . . . . 11547 1 315 no PRF 1212243A . "ubiquitin S1" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 316 no PRF 1212243B . "ubiquitin S5" . . . . . 92.11 77 97.14 97.14 5.59e-40 . . . . 11547 1 317 no PRF 1212243C . "ubiquitin S3" . . . . . 100.00 76 98.68 98.68 3.54e-45 . . . . 11547 1 318 no REF NP_001005123 . "ubiquitin-60S ribosomal protein L40 [Xenopus (Silurana) tropicalis]" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 319 no REF NP_001006688 . "ubiquitin C [Xenopus (Silurana) tropicalis]" . . . . . 100.00 609 98.68 98.68 5.95e-41 . . . . 11547 1 320 no REF NP_001009117 . "polyubiquitin-B [Pan troglodytes]" . . . . . 100.00 229 98.68 98.68 2.63e-43 . . . . 11547 1 321 no REF NP_001009202 . "polyubiquitin-B [Ovis aries]" . . . . . 100.00 305 97.37 98.68 3.04e-42 . . . . 11547 1 322 no REF NP_001009286 . "ubiquitin-60S ribosomal protein L40 [Ovis aries]" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 323 no SP P0C273 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 324 no SP P0C275 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 325 no SP P0C276 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 1 326 no SP P0CG47 . "RecName: Full=Polyubiquitin-B; Contains: RecName: Full=Ubiquitin; Flags: Precursor" . . . . . 100.00 229 98.68 98.68 2.63e-43 . . . . 11547 1 327 no SP P0CG48 . "RecName: Full=Polyubiquitin-C; Contains: RecName: Full=Ubiquitin; Flags: Precursor" . . . . . 100.00 685 98.68 98.68 9.23e-41 . . . . 11547 1 328 no TPE CEL68433 . "TPA: ubiquitin / ribosomal protein CEP52 fusion protein, putative [Neospora caninum Liverpool]" . . . . . 100.00 129 97.37 98.68 1.10e-44 . . . . 11547 1 329 no TPE CEL70397 . "TPA: Ubiquitin, related [Neospora caninum Liverpool]" . . . . . 100.00 535 97.37 98.68 1.44e-40 . . . . 11547 1 330 no TPE CEL75964 . "TPA: ubiquitin / ribosomal protein CEP52 fusion protein, putative [Toxoplasma gondii VEG]" . . . . . 100.00 129 97.37 98.68 1.10e-44 . . . . 11547 1 331 no TPE CEL78064 . "TPA: polyubiquitin, putative [Toxoplasma gondii VEG]" . . . . . 100.00 307 97.37 98.68 6.36e-42 . . . . 11547 1 332 no TPG DAA18802 . "TPA: polyubiquitin [Bos taurus]" . . . . . 100.00 305 98.68 98.68 1.61e-42 . . . . 11547 1 333 no TPG DAA20663 . "TPA: ubiquitin C [Bos taurus]" . . . . . 98.68 314 97.33 98.67 5.94e-41 . . . . 11547 1 334 no TPG DAA20672 . "TPA: ubiquitin B-like [Bos taurus]" . . . . . 100.00 77 97.37 97.37 2.61e-44 . . . . 11547 1 335 no TPG DAA24675 . "TPA: 40S ribosomal protein S27a [Bos taurus]" . . . . . 100.00 156 98.68 98.68 5.81e-45 . . . . 11547 1 336 no TPG DAA28295 . "TPA: ubiquitin and ribosomal protein L40 [Bos taurus]" . . . . . 100.00 128 98.68 98.68 3.14e-45 . . . . 11547 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 1 MET . 11547 1 2 2 GLN . 11547 1 3 3 ILE . 11547 1 4 4 PHE . 11547 1 5 5 VAL . 11547 1 6 6 LYS . 11547 1 7 7 THR . 11547 1 8 8 LEU . 11547 1 9 9 THR . 11547 1 10 10 GLY . 11547 1 11 11 LYS . 11547 1 12 12 THR . 11547 1 13 13 ILE . 11547 1 14 14 THR . 11547 1 15 15 LEU . 11547 1 16 16 GLU . 11547 1 17 17 VAL . 11547 1 18 18 GLU . 11547 1 19 19 PRO . 11547 1 20 20 SER . 11547 1 21 21 ASP . 11547 1 22 22 THR . 11547 1 23 23 ILE . 11547 1 24 24 GLU . 11547 1 25 25 ASN . 11547 1 26 26 VAL . 11547 1 27 27 LYS . 11547 1 28 28 ALA . 11547 1 29 29 LYS . 11547 1 30 30 ILE . 11547 1 31 31 GLN . 11547 1 32 32 ASP . 11547 1 33 33 LYS . 11547 1 34 34 GLU . 11547 1 35 35 GLY . 11547 1 36 36 ILE . 11547 1 37 37 PRO . 11547 1 38 38 PRO . 11547 1 39 39 ASP . 11547 1 40 40 GLN . 11547 1 41 41 ASN . 11547 1 42 42 ARG . 11547 1 43 43 LEU . 11547 1 44 44 ILE . 11547 1 45 45 PHE . 11547 1 46 46 ALA . 11547 1 47 47 GLY . 11547 1 48 48 LYS . 11547 1 49 49 GLN . 11547 1 50 50 LEU . 11547 1 51 51 GLU . 11547 1 52 52 ASP . 11547 1 53 53 GLY . 11547 1 54 54 ARG . 11547 1 55 55 THR . 11547 1 56 56 LEU . 11547 1 57 57 SER . 11547 1 58 58 ASP . 11547 1 59 59 TYR . 11547 1 60 60 ASN . 11547 1 61 61 ILE . 11547 1 62 62 GLN . 11547 1 63 63 LYS . 11547 1 64 64 GLU . 11547 1 65 65 SER . 11547 1 66 66 THR . 11547 1 67 67 LEU . 11547 1 68 68 HIS . 11547 1 69 69 LEU . 11547 1 70 70 VAL . 11547 1 71 71 LEU . 11547 1 72 72 ARG . 11547 1 73 73 LEU . 11547 1 74 74 ARG . 11547 1 75 75 GLY . 11547 1 76 76 GLY . 11547 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 11547 1 . GLN 2 2 11547 1 . ILE 3 3 11547 1 . PHE 4 4 11547 1 . VAL 5 5 11547 1 . LYS 6 6 11547 1 . THR 7 7 11547 1 . LEU 8 8 11547 1 . THR 9 9 11547 1 . GLY 10 10 11547 1 . LYS 11 11 11547 1 . THR 12 12 11547 1 . ILE 13 13 11547 1 . THR 14 14 11547 1 . LEU 15 15 11547 1 . GLU 16 16 11547 1 . VAL 17 17 11547 1 . GLU 18 18 11547 1 . PRO 19 19 11547 1 . SER 20 20 11547 1 . ASP 21 21 11547 1 . THR 22 22 11547 1 . ILE 23 23 11547 1 . GLU 24 24 11547 1 . ASN 25 25 11547 1 . VAL 26 26 11547 1 . LYS 27 27 11547 1 . ALA 28 28 11547 1 . LYS 29 29 11547 1 . ILE 30 30 11547 1 . GLN 31 31 11547 1 . ASP 32 32 11547 1 . LYS 33 33 11547 1 . GLU 34 34 11547 1 . GLY 35 35 11547 1 . ILE 36 36 11547 1 . PRO 37 37 11547 1 . PRO 38 38 11547 1 . ASP 39 39 11547 1 . GLN 40 40 11547 1 . ASN 41 41 11547 1 . ARG 42 42 11547 1 . LEU 43 43 11547 1 . ILE 44 44 11547 1 . PHE 45 45 11547 1 . ALA 46 46 11547 1 . GLY 47 47 11547 1 . LYS 48 48 11547 1 . GLN 49 49 11547 1 . LEU 50 50 11547 1 . GLU 51 51 11547 1 . ASP 52 52 11547 1 . GLY 53 53 11547 1 . ARG 54 54 11547 1 . THR 55 55 11547 1 . LEU 56 56 11547 1 . SER 57 57 11547 1 . ASP 58 58 11547 1 . TYR 59 59 11547 1 . ASN 60 60 11547 1 . ILE 61 61 11547 1 . GLN 62 62 11547 1 . LYS 63 63 11547 1 . GLU 64 64 11547 1 . SER 65 65 11547 1 . THR 66 66 11547 1 . LEU 67 67 11547 1 . HIS 68 68 11547 1 . LEU 69 69 11547 1 . VAL 70 70 11547 1 . LEU 71 71 11547 1 . ARG 72 72 11547 1 . LEU 73 73 11547 1 . ARG 74 74 11547 1 . GLY 75 75 11547 1 . GLY 76 76 11547 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 11547 _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 $ubiquitin . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 11547 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 11547 _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 $ubiquitin . 'recombinant technology' 'Escherichia coli' 'E. coli' . 562 Escherichia coli . . . . . . . . . . . . . . . . pCGN . . . . . . 11547 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 11547 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '88% H2O/12% 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 ubiquitin '[U-100% 13C; U-100% 15N]' . . 1 $ubiquitin . protein 2 . . mM . . . . 11547 1 2 Tris(hydroxymethyl)aminomethane '[U-100% 2H]' . . . . . buffer 20 . . mM . . . . 11547 1 3 DSS 'natural abundance' . . . . . . 0.2 . . mM . . . . 11547 1 4 H2O . . . . . . solvent 88 . . % . . . . 11547 1 5 D2O . . . . . . solvent 12 . . % . . . . 11547 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 11547 _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' 20 . mM 11547 1 pH 7.2 . pH 11547 1 pressure 2500 . bar 11547 1 temperature 298 . K 11547 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 11547 _Software.ID 1 _Software.Name CYANA _Software.Version 3.93 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 11547 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 11547 1 stop_ save_ save_AMBER _Software.Sf_category software _Software.Sf_framecode AMBER _Software.Entry_ID 11547 _Software.ID 2 _Software.Name AMBER _Software.Version 11 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman' . . 11547 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 11547 2 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 11547 _Software.ID 3 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 11547 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 11547 3 stop_ save_ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 11547 _Software.ID 4 _Software.Name NMRView _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Johnson, One Moon Scientific' . . 11547 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak picking' 11547 4 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 11547 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 11547 _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 Avance . 800 . . . 11547 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 11547 _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 . . . . . . . . . . . . . . . . 11547 1 2 '2D 1H-13C HSQC aliphatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11547 1 3 '2D 1H-13C HSQC aromatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11547 1 4 '2D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11547 1 5 '3D 1H-13C/15N simultaneous evolutio NOESY HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11547 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 11547 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details 'DSS (4,4-dimethyl-4-silapentane-1-sulfonic acid)' 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 internal indirect 0.25144952 . . . . . . . . . 11547 1 H 1 DSS 'methyl protons' . . . . ppm 0 internal direct 1 . . . . . . . . . 11547 1 N 15 DSS 'methyl protons' . . . . ppm 0 internal indirect 0.10132905 . . . . . . . . . 11547 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 11547 _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' 1 $sample_1 isotropic 11547 1 2 '2D 1H-13C HSQC aliphatic' 1 $sample_1 isotropic 11547 1 3 '2D 1H-13C HSQC aromatic' 1 $sample_1 isotropic 11547 1 4 '2D HNCO' 1 $sample_1 isotropic 11547 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 MET HA H 1 4.195 0.030 . 1 . . . A 1 MET HA . 11547 1 2 . 1 1 1 1 MET HB2 H 1 1.982 0.030 . 1 . . . A 1 MET HB2 . 11547 1 3 . 1 1 1 1 MET HB3 H 1 1.982 0.030 . 1 . . . A 1 MET HB3 . 11547 1 4 . 1 1 1 1 MET HG2 H 1 2.421 0.030 . 1 . . . A 1 MET HG2 . 11547 1 5 . 1 1 1 1 MET HG3 H 1 2.421 0.030 . 1 . . . A 1 MET HG3 . 11547 1 6 . 1 1 1 1 MET C C 13 170.441 0.300 . 1 . . . A 1 MET C . 11547 1 7 . 1 1 1 1 MET CA C 13 54.503 0.300 . 1 . . . A 1 MET CA . 11547 1 8 . 1 1 1 1 MET CB C 13 30.926 0.300 . 1 . . . A 1 MET CB . 11547 1 9 . 1 1 1 1 MET CG C 13 31.116 0.300 . 1 . . . A 1 MET CG . 11547 1 10 . 1 1 2 2 GLN H H 1 8.951 0.030 . 1 . . . A 2 GLN H . 11547 1 11 . 1 1 2 2 GLN HA H 1 5.265 0.030 . 1 . . . A 2 GLN HA . 11547 1 12 . 1 1 2 2 GLN HB2 H 1 1.710 0.030 . 2 . . . A 2 GLN HB2 . 11547 1 13 . 1 1 2 2 GLN HB3 H 1 1.835 0.030 . 2 . . . A 2 GLN HB3 . 11547 1 14 . 1 1 2 2 GLN HG2 H 1 1.839 0.030 . 2 . . . A 2 GLN HG2 . 11547 1 15 . 1 1 2 2 GLN HG3 H 1 2.156 0.030 . 2 . . . A 2 GLN HG3 . 11547 1 16 . 1 1 2 2 GLN HE21 H 1 6.727 0.030 . 2 . . . A 2 GLN HE21 . 11547 1 17 . 1 1 2 2 GLN HE22 H 1 7.780 0.030 . 2 . . . A 2 GLN HE22 . 11547 1 18 . 1 1 2 2 GLN C C 13 175.973 0.300 . 1 . . . A 2 GLN C . 11547 1 19 . 1 1 2 2 GLN CA C 13 54.899 0.300 . 1 . . . A 2 GLN CA . 11547 1 20 . 1 1 2 2 GLN CB C 13 30.706 0.300 . 1 . . . A 2 GLN CB . 11547 1 21 . 1 1 2 2 GLN CG C 13 34.660 0.300 . 1 . . . A 2 GLN CG . 11547 1 22 . 1 1 2 2 GLN N N 15 124.610 0.300 . 1 . . . A 2 GLN N . 11547 1 23 . 1 1 2 2 GLN NE2 N 15 114.473 0.300 . 1 . . . A 2 GLN NE2 . 11547 1 24 . 1 1 3 3 ILE H H 1 8.369 0.030 . 1 . . . A 3 ILE H . 11547 1 25 . 1 1 3 3 ILE HA H 1 4.151 0.030 . 1 . . . A 3 ILE HA . 11547 1 26 . 1 1 3 3 ILE HB H 1 1.790 0.030 . 1 . . . A 3 ILE HB . 11547 1 27 . 1 1 3 3 ILE HG12 H 1 0.821 0.030 . 2 . . . A 3 ILE HG12 . 11547 1 28 . 1 1 3 3 ILE HG13 H 1 0.992 0.030 . 2 . . . A 3 ILE HG13 . 11547 1 29 . 1 1 3 3 ILE HG21 H 1 0.596 0.030 . 1 . . . A 3 ILE HG21 . 11547 1 30 . 1 1 3 3 ILE HG22 H 1 0.596 0.030 . 1 . . . A 3 ILE HG22 . 11547 1 31 . 1 1 3 3 ILE HG23 H 1 0.596 0.030 . 1 . . . A 3 ILE HG23 . 11547 1 32 . 1 1 3 3 ILE HD11 H 1 0.582 0.030 . 1 . . . A 3 ILE HD11 . 11547 1 33 . 1 1 3 3 ILE HD12 H 1 0.582 0.030 . 1 . . . A 3 ILE HD12 . 11547 1 34 . 1 1 3 3 ILE HD13 H 1 0.582 0.030 . 1 . . . A 3 ILE HD13 . 11547 1 35 . 1 1 3 3 ILE C C 13 172.456 0.300 . 1 . . . A 3 ILE C . 11547 1 36 . 1 1 3 3 ILE CA C 13 59.697 0.300 . 1 . . . A 3 ILE CA . 11547 1 37 . 1 1 3 3 ILE CB C 13 42.037 0.300 . 1 . . . A 3 ILE CB . 11547 1 38 . 1 1 3 3 ILE CG1 C 13 24.983 0.300 . 1 . . . A 3 ILE CG1 . 11547 1 39 . 1 1 3 3 ILE CG2 C 13 18.101 0.300 . 1 . . . A 3 ILE CG2 . 11547 1 40 . 1 1 3 3 ILE CD1 C 13 14.841 0.300 . 1 . . . A 3 ILE CD1 . 11547 1 41 . 1 1 3 3 ILE N N 15 116.594 0.300 . 1 . . . A 3 ILE N . 11547 1 42 . 1 1 4 4 PHE H H 1 8.839 0.030 . 1 . . . A 4 PHE H . 11547 1 43 . 1 1 4 4 PHE HA H 1 5.704 0.030 . 1 . . . A 4 PHE HA . 11547 1 44 . 1 1 4 4 PHE HB2 H 1 3.042 0.030 . 2 . . . A 4 PHE HB2 . 11547 1 45 . 1 1 4 4 PHE HB3 H 1 2.842 0.030 . 2 . . . A 4 PHE HB3 . 11547 1 46 . 1 1 4 4 PHE HD1 H 1 7.054 0.030 . 1 . . . A 4 PHE HD1 . 11547 1 47 . 1 1 4 4 PHE HD2 H 1 7.054 0.030 . 1 . . . A 4 PHE HD2 . 11547 1 48 . 1 1 4 4 PHE HE1 H 1 7.253 0.030 . 1 . . . A 4 PHE HE1 . 11547 1 49 . 1 1 4 4 PHE HE2 H 1 7.253 0.030 . 1 . . . A 4 PHE HE2 . 11547 1 50 . 1 1 4 4 PHE HZ H 1 7.262 0.030 . 1 . . . A 4 PHE HZ . 11547 1 51 . 1 1 4 4 PHE C C 13 175.640 0.300 . 1 . . . A 4 PHE C . 11547 1 52 . 1 1 4 4 PHE CA C 13 55.044 0.300 . 1 . . . A 4 PHE CA . 11547 1 53 . 1 1 4 4 PHE CB C 13 41.236 0.300 . 1 . . . A 4 PHE CB . 11547 1 54 . 1 1 4 4 PHE CD1 C 13 132.381 0.300 . 1 . . . A 4 PHE CD1 . 11547 1 55 . 1 1 4 4 PHE CD2 C 13 132.381 0.300 . 1 . . . A 4 PHE CD2 . 11547 1 56 . 1 1 4 4 PHE CE1 C 13 131.368 0.300 . 1 . . . A 4 PHE CE1 . 11547 1 57 . 1 1 4 4 PHE CE2 C 13 131.368 0.300 . 1 . . . A 4 PHE CE2 . 11547 1 58 . 1 1 4 4 PHE CZ C 13 129.896 0.300 . 1 . . . A 4 PHE CZ . 11547 1 59 . 1 1 4 4 PHE N N 15 119.549 0.300 . 1 . . . A 4 PHE N . 11547 1 60 . 1 1 5 5 VAL H H 1 9.295 0.030 . 1 . . . A 5 VAL H . 11547 1 61 . 1 1 5 5 VAL HB H 1 1.760 0.030 . 1 . . . A 5 VAL HB . 11547 1 62 . 1 1 5 5 VAL HG11 H 1 0.628 0.030 . 2 . . . A 5 VAL HG11 . 11547 1 63 . 1 1 5 5 VAL HG12 H 1 0.628 0.030 . 2 . . . A 5 VAL HG12 . 11547 1 64 . 1 1 5 5 VAL HG13 H 1 0.628 0.030 . 2 . . . A 5 VAL HG13 . 11547 1 65 . 1 1 5 5 VAL HG21 H 1 0.685 0.030 . 2 . . . A 5 VAL HG21 . 11547 1 66 . 1 1 5 5 VAL HG22 H 1 0.685 0.030 . 2 . . . A 5 VAL HG22 . 11547 1 67 . 1 1 5 5 VAL HG23 H 1 0.685 0.030 . 2 . . . A 5 VAL HG23 . 11547 1 68 . 1 1 5 5 VAL C C 13 174.952 0.300 . 1 . . . A 5 VAL C . 11547 1 69 . 1 1 5 5 VAL CB C 13 34.948 0.300 . 1 . . . A 5 VAL CB . 11547 1 70 . 1 1 5 5 VAL CG1 C 13 21.977 0.300 . 2 . . . A 5 VAL CG1 . 11547 1 71 . 1 1 5 5 VAL CG2 C 13 21.215 0.300 . 2 . . . A 5 VAL CG2 . 11547 1 72 . 1 1 5 5 VAL N N 15 120.994 0.300 . 1 . . . A 5 VAL N . 11547 1 73 . 1 1 6 6 LYS H H 1 8.986 0.030 . 1 . . . A 6 LYS H . 11547 1 74 . 1 1 6 6 LYS HA H 1 5.068 0.030 . 1 . . . A 6 LYS HA . 11547 1 75 . 1 1 6 6 LYS HB2 H 1 1.689 0.030 . 2 . . . A 6 LYS HB2 . 11547 1 76 . 1 1 6 6 LYS HB3 H 1 1.416 0.030 . 2 . . . A 6 LYS HB3 . 11547 1 77 . 1 1 6 6 LYS HG2 H 1 1.222 0.030 . 2 . . . A 6 LYS HG2 . 11547 1 78 . 1 1 6 6 LYS HG3 H 1 1.377 0.030 . 2 . . . A 6 LYS HG3 . 11547 1 79 . 1 1 6 6 LYS HD2 H 1 1.529 0.030 . 1 . . . A 6 LYS HD2 . 11547 1 80 . 1 1 6 6 LYS HD3 H 1 1.529 0.030 . 1 . . . A 6 LYS HD3 . 11547 1 81 . 1 1 6 6 LYS HE2 H 1 2.886 0.030 . 1 . . . A 6 LYS HE2 . 11547 1 82 . 1 1 6 6 LYS HE3 H 1 2.886 0.030 . 1 . . . A 6 LYS HE3 . 11547 1 83 . 1 1 6 6 LYS C C 13 177.064 0.300 . 1 . . . A 6 LYS C . 11547 1 84 . 1 1 6 6 LYS CA C 13 54.920 0.300 . 1 . . . A 6 LYS CA . 11547 1 85 . 1 1 6 6 LYS CB C 13 32.861 0.300 . 1 . . . A 6 LYS CB . 11547 1 86 . 1 1 6 6 LYS CG C 13 24.836 0.300 . 1 . . . A 6 LYS CG . 11547 1 87 . 1 1 6 6 LYS CD C 13 28.904 0.300 . 1 . . . A 6 LYS CD . 11547 1 88 . 1 1 6 6 LYS CE C 13 41.974 0.300 . 1 . . . A 6 LYS CE . 11547 1 89 . 1 1 6 6 LYS N N 15 129.582 0.300 . 1 . . . A 6 LYS N . 11547 1 90 . 1 1 7 7 THR H H 1 8.959 0.030 . 1 . . . A 7 THR H . 11547 1 91 . 1 1 7 7 THR HA H 1 4.700 0.030 . 1 . . . A 7 THR HA . 11547 1 92 . 1 1 7 7 THR HB H 1 4.746 0.030 . 1 . . . A 7 THR HB . 11547 1 93 . 1 1 7 7 THR HG21 H 1 1.140 0.030 . 1 . . . A 7 THR HG21 . 11547 1 94 . 1 1 7 7 THR HG22 H 1 1.140 0.030 . 1 . . . A 7 THR HG22 . 11547 1 95 . 1 1 7 7 THR HG23 H 1 1.140 0.030 . 1 . . . A 7 THR HG23 . 11547 1 96 . 1 1 7 7 THR C C 13 176.583 0.300 . 1 . . . A 7 THR C . 11547 1 97 . 1 1 7 7 THR CA C 13 60.831 0.300 . 1 . . . A 7 THR CA . 11547 1 98 . 1 1 7 7 THR CB C 13 70.050 0.300 . 1 . . . A 7 THR CB . 11547 1 99 . 1 1 7 7 THR CG2 C 13 22.021 0.300 . 1 . . . A 7 THR CG2 . 11547 1 100 . 1 1 7 7 THR N N 15 117.890 0.300 . 1 . . . A 7 THR N . 11547 1 101 . 1 1 8 8 LEU H H 1 9.102 0.030 . 1 . . . A 8 LEU H . 11547 1 102 . 1 1 8 8 LEU HA H 1 4.298 0.030 . 1 . . . A 8 LEU HA . 11547 1 103 . 1 1 8 8 LEU HB2 H 1 1.901 0.030 . 2 . . . A 8 LEU HB2 . 11547 1 104 . 1 1 8 8 LEU HB3 H 1 1.711 0.030 . 2 . . . A 8 LEU HB3 . 11547 1 105 . 1 1 8 8 LEU HD11 H 1 0.990 0.030 . 2 . . . A 8 LEU HD11 . 11547 1 106 . 1 1 8 8 LEU HD12 H 1 0.990 0.030 . 2 . . . A 8 LEU HD12 . 11547 1 107 . 1 1 8 8 LEU HD13 H 1 0.990 0.030 . 2 . . . A 8 LEU HD13 . 11547 1 108 . 1 1 8 8 LEU HD21 H 1 0.952 0.030 . 2 . . . A 8 LEU HD21 . 11547 1 109 . 1 1 8 8 LEU HD22 H 1 0.952 0.030 . 2 . . . A 8 LEU HD22 . 11547 1 110 . 1 1 8 8 LEU HD23 H 1 0.952 0.030 . 2 . . . A 8 LEU HD23 . 11547 1 111 . 1 1 8 8 LEU C C 13 179.033 0.300 . 1 . . . A 8 LEU C . 11547 1 112 . 1 1 8 8 LEU CA C 13 57.476 0.300 . 1 . . . A 8 LEU CA . 11547 1 113 . 1 1 8 8 LEU CB C 13 41.509 0.300 . 1 . . . A 8 LEU CB . 11547 1 114 . 1 1 8 8 LEU CD1 C 13 26.045 0.300 . 2 . . . A 8 LEU CD1 . 11547 1 115 . 1 1 8 8 LEU CD2 C 13 24.157 0.300 . 2 . . . A 8 LEU CD2 . 11547 1 116 . 1 1 8 8 LEU N N 15 121.837 0.300 . 1 . . . A 8 LEU N . 11547 1 117 . 1 1 9 9 THR H H 1 7.725 0.030 . 1 . . . A 9 THR H . 11547 1 118 . 1 1 9 9 THR HA H 1 4.469 0.030 . 1 . . . A 9 THR HA . 11547 1 119 . 1 1 9 9 THR HB H 1 4.554 0.030 . 1 . . . A 9 THR HB . 11547 1 120 . 1 1 9 9 THR HG21 H 1 1.261 0.030 . 1 . . . A 9 THR HG21 . 11547 1 121 . 1 1 9 9 THR HG22 H 1 1.261 0.030 . 1 . . . A 9 THR HG22 . 11547 1 122 . 1 1 9 9 THR HG23 H 1 1.261 0.030 . 1 . . . A 9 THR HG23 . 11547 1 123 . 1 1 9 9 THR C C 13 175.711 0.300 . 1 . . . A 9 THR C . 11547 1 124 . 1 1 9 9 THR CA C 13 61.523 0.300 . 1 . . . A 9 THR CA . 11547 1 125 . 1 1 9 9 THR CB C 13 69.140 0.300 . 1 . . . A 9 THR CB . 11547 1 126 . 1 1 9 9 THR CG2 C 13 22.168 0.300 . 1 . . . A 9 THR CG2 . 11547 1 127 . 1 1 9 9 THR N N 15 133.650 0.300 . 1 . . . A 9 THR N . 11547 1 128 . 1 1 10 10 GLY H H 1 7.856 0.030 . 1 . . . A 10 GLY H . 11547 1 129 . 1 1 10 10 GLY HA2 H 1 4.357 0.030 . 2 . . . A 10 GLY HA2 . 11547 1 130 . 1 1 10 10 GLY HA3 H 1 3.634 0.030 . 2 . . . A 10 GLY HA3 . 11547 1 131 . 1 1 10 10 GLY C C 13 173.986 0.300 . 1 . . . A 10 GLY C . 11547 1 132 . 1 1 10 10 GLY CA C 13 45.541 0.300 . 1 . . . A 10 GLY CA . 11547 1 133 . 1 1 10 10 GLY N N 15 110.658 0.300 . 1 . . . A 10 GLY N . 11547 1 134 . 1 1 11 11 LYS H H 1 7.288 0.030 . 1 . . . A 11 LYS H . 11547 1 135 . 1 1 11 11 LYS HA H 1 4.356 0.030 . 1 . . . A 11 LYS HA . 11547 1 136 . 1 1 11 11 LYS HB2 H 1 1.687 0.030 . 1 . . . A 11 LYS HB2 . 11547 1 137 . 1 1 11 11 LYS HB3 H 1 1.687 0.030 . 1 . . . A 11 LYS HB3 . 11547 1 138 . 1 1 11 11 LYS HG2 H 1 1.197 0.030 . 2 . . . A 11 LYS HG2 . 11547 1 139 . 1 1 11 11 LYS HG3 H 1 1.358 0.030 . 2 . . . A 11 LYS HG3 . 11547 1 140 . 1 1 11 11 LYS HD2 H 1 1.596 0.030 . 1 . . . A 11 LYS HD2 . 11547 1 141 . 1 1 11 11 LYS HD3 H 1 1.596 0.030 . 1 . . . A 11 LYS HD3 . 11547 1 142 . 1 1 11 11 LYS HE2 H 1 2.930 0.030 . 1 . . . A 11 LYS HE2 . 11547 1 143 . 1 1 11 11 LYS HE3 H 1 2.930 0.030 . 1 . . . A 11 LYS HE3 . 11547 1 144 . 1 1 11 11 LYS C C 13 175.940 0.300 . 1 . . . A 11 LYS C . 11547 1 145 . 1 1 11 11 LYS CA C 13 55.888 0.300 . 1 . . . A 11 LYS CA . 11547 1 146 . 1 1 11 11 LYS CB C 13 33.605 0.300 . 1 . . . A 11 LYS CB . 11547 1 147 . 1 1 11 11 LYS CG C 13 24.869 0.300 . 1 . . . A 11 LYS CG . 11547 1 148 . 1 1 11 11 LYS CD C 13 29.251 0.300 . 1 . . . A 11 LYS CD . 11547 1 149 . 1 1 11 11 LYS CE C 13 42.047 0.300 . 1 . . . A 11 LYS CE . 11547 1 150 . 1 1 11 11 LYS N N 15 122.621 0.300 . 1 . . . A 11 LYS N . 11547 1 151 . 1 1 12 12 THR H H 1 8.914 0.030 . 1 . . . A 12 THR H . 11547 1 152 . 1 1 12 12 THR HA H 1 4.986 0.030 . 1 . . . A 12 THR HA . 11547 1 153 . 1 1 12 12 THR HB H 1 3.949 0.030 . 1 . . . A 12 THR HB . 11547 1 154 . 1 1 12 12 THR HG21 H 1 1.068 0.030 . 1 . . . A 12 THR HG21 . 11547 1 155 . 1 1 12 12 THR HG22 H 1 1.068 0.030 . 1 . . . A 12 THR HG22 . 11547 1 156 . 1 1 12 12 THR HG23 H 1 1.068 0.030 . 1 . . . A 12 THR HG23 . 11547 1 157 . 1 1 12 12 THR C C 13 174.494 0.300 . 1 . . . A 12 THR C . 11547 1 158 . 1 1 12 12 THR CA C 13 62.594 0.300 . 1 . . . A 12 THR CA . 11547 1 159 . 1 1 12 12 THR CB C 13 69.128 0.300 . 1 . . . A 12 THR CB . 11547 1 160 . 1 1 12 12 THR CG2 C 13 22.586 0.300 . 1 . . . A 12 THR CG2 . 11547 1 161 . 1 1 12 12 THR N N 15 122.289 0.300 . 1 . . . A 12 THR N . 11547 1 162 . 1 1 13 13 ILE H H 1 9.504 0.030 . 1 . . . A 13 ILE H . 11547 1 163 . 1 1 13 13 ILE HA H 1 4.588 0.030 . 1 . . . A 13 ILE HA . 11547 1 164 . 1 1 13 13 ILE HB H 1 1.914 0.030 . 1 . . . A 13 ILE HB . 11547 1 165 . 1 1 13 13 ILE HG12 H 1 1.217 0.030 . 2 . . . A 13 ILE HG12 . 11547 1 166 . 1 1 13 13 ILE HG13 H 1 1.391 0.030 . 2 . . . A 13 ILE HG13 . 11547 1 167 . 1 1 13 13 ILE HG21 H 1 0.867 0.030 . 1 . . . A 13 ILE HG21 . 11547 1 168 . 1 1 13 13 ILE HG22 H 1 0.867 0.030 . 1 . . . A 13 ILE HG22 . 11547 1 169 . 1 1 13 13 ILE HG23 H 1 0.867 0.030 . 1 . . . A 13 ILE HG23 . 11547 1 170 . 1 1 13 13 ILE HD11 H 1 0.738 0.030 . 1 . . . A 13 ILE HD11 . 11547 1 171 . 1 1 13 13 ILE HD12 H 1 0.738 0.030 . 1 . . . A 13 ILE HD12 . 11547 1 172 . 1 1 13 13 ILE HD13 H 1 0.738 0.030 . 1 . . . A 13 ILE HD13 . 11547 1 173 . 1 1 13 13 ILE C C 13 175.171 0.300 . 1 . . . A 13 ILE C . 11547 1 174 . 1 1 13 13 ILE CA C 13 59.491 0.300 . 1 . . . A 13 ILE CA . 11547 1 175 . 1 1 13 13 ILE CB C 13 40.149 0.300 . 1 . . . A 13 ILE CB . 11547 1 176 . 1 1 13 13 ILE CG1 C 13 26.720 0.300 . 1 . . . A 13 ILE CG1 . 11547 1 177 . 1 1 13 13 ILE CG2 C 13 18.435 0.300 . 1 . . . A 13 ILE CG2 . 11547 1 178 . 1 1 13 13 ILE CD1 C 13 15.148 0.300 . 1 . . . A 13 ILE CD1 . 11547 1 179 . 1 1 13 13 ILE N N 15 128.039 0.300 . 1 . . . A 13 ILE N . 11547 1 180 . 1 1 14 14 THR H H 1 8.886 0.030 . 1 . . . A 14 THR H . 11547 1 181 . 1 1 14 14 THR HA H 1 4.968 0.030 . 1 . . . A 14 THR HA . 11547 1 182 . 1 1 14 14 THR HB H 1 4.032 0.030 . 1 . . . A 14 THR HB . 11547 1 183 . 1 1 14 14 THR HG21 H 1 1.119 0.030 . 1 . . . A 14 THR HG21 . 11547 1 184 . 1 1 14 14 THR HG22 H 1 1.119 0.030 . 1 . . . A 14 THR HG22 . 11547 1 185 . 1 1 14 14 THR HG23 H 1 1.119 0.030 . 1 . . . A 14 THR HG23 . 11547 1 186 . 1 1 14 14 THR C C 13 173.604 0.300 . 1 . . . A 14 THR C . 11547 1 187 . 1 1 14 14 THR CA C 13 61.647 0.300 . 1 . . . A 14 THR CA . 11547 1 188 . 1 1 14 14 THR CB C 13 69.612 0.300 . 1 . . . A 14 THR CB . 11547 1 189 . 1 1 14 14 THR CG2 C 13 22.315 0.300 . 1 . . . A 14 THR CG2 . 11547 1 190 . 1 1 14 14 THR N N 15 121.506 0.300 . 1 . . . A 14 THR N . 11547 1 191 . 1 1 15 15 LEU H H 1 8.914 0.030 . 1 . . . A 15 LEU H . 11547 1 192 . 1 1 15 15 LEU HA H 1 4.699 0.030 . 1 . . . A 15 LEU HA . 11547 1 193 . 1 1 15 15 LEU HB2 H 1 1.262 0.030 . 1 . . . A 15 LEU HB2 . 11547 1 194 . 1 1 15 15 LEU HB3 H 1 1.262 0.030 . 1 . . . A 15 LEU HB3 . 11547 1 195 . 1 1 15 15 LEU HG H 1 1.382 0.030 . 1 . . . A 15 LEU HG . 11547 1 196 . 1 1 15 15 LEU HD11 H 1 0.699 0.030 . 2 . . . A 15 LEU HD11 . 11547 1 197 . 1 1 15 15 LEU HD12 H 1 0.699 0.030 . 2 . . . A 15 LEU HD12 . 11547 1 198 . 1 1 15 15 LEU HD13 H 1 0.699 0.030 . 2 . . . A 15 LEU HD13 . 11547 1 199 . 1 1 15 15 LEU HD21 H 1 0.720 0.030 . 2 . . . A 15 LEU HD21 . 11547 1 200 . 1 1 15 15 LEU HD22 H 1 0.720 0.030 . 2 . . . A 15 LEU HD22 . 11547 1 201 . 1 1 15 15 LEU HD23 H 1 0.720 0.030 . 2 . . . A 15 LEU HD23 . 11547 1 202 . 1 1 15 15 LEU C C 13 174.571 0.300 . 1 . . . A 15 LEU C . 11547 1 203 . 1 1 15 15 LEU CA C 13 52.955 0.300 . 1 . . . A 15 LEU CA . 11547 1 204 . 1 1 15 15 LEU CB C 13 46.976 0.300 . 1 . . . A 15 LEU CB . 11547 1 205 . 1 1 15 15 LEU CG C 13 26.927 0.300 . 1 . . . A 15 LEU CG . 11547 1 206 . 1 1 15 15 LEU CD1 C 13 27.294 0.300 . 2 . . . A 15 LEU CD1 . 11547 1 207 . 1 1 15 15 LEU CD2 C 13 25.083 0.300 . 2 . . . A 15 LEU CD2 . 11547 1 208 . 1 1 15 15 LEU N N 15 126.749 0.300 . 1 . . . A 15 LEU N . 11547 1 209 . 1 1 16 16 GLU H H 1 8.250 0.030 . 1 . . . A 16 GLU H . 11547 1 210 . 1 1 16 16 GLU HB2 H 1 1.906 0.030 . 2 . . . A 16 GLU HB2 . 11547 1 211 . 1 1 16 16 GLU HB3 H 1 1.808 0.030 . 2 . . . A 16 GLU HB3 . 11547 1 212 . 1 1 16 16 GLU HG2 H 1 2.103 0.030 . 2 . . . A 16 GLU HG2 . 11547 1 213 . 1 1 16 16 GLU HG3 H 1 2.267 0.030 . 2 . . . A 16 GLU HG3 . 11547 1 214 . 1 1 16 16 GLU C C 13 175.735 0.300 . 1 . . . A 16 GLU C . 11547 1 215 . 1 1 16 16 GLU CB C 13 29.578 0.300 . 1 . . . A 16 GLU CB . 11547 1 216 . 1 1 16 16 GLU CG C 13 35.569 0.300 . 1 . . . A 16 GLU CG . 11547 1 217 . 1 1 16 16 GLU N N 15 124.067 0.300 . 1 . . . A 16 GLU N . 11547 1 218 . 1 1 17 17 VAL H H 1 9.016 0.030 . 1 . . . A 17 VAL H . 11547 1 219 . 1 1 17 17 VAL HA H 1 4.651 0.030 . 1 . . . A 17 VAL HA . 11547 1 220 . 1 1 17 17 VAL HB H 1 2.280 0.030 . 1 . . . A 17 VAL HB . 11547 1 221 . 1 1 17 17 VAL HG11 H 1 0.695 0.030 . 2 . . . A 17 VAL HG11 . 11547 1 222 . 1 1 17 17 VAL HG12 H 1 0.695 0.030 . 2 . . . A 17 VAL HG12 . 11547 1 223 . 1 1 17 17 VAL HG13 H 1 0.695 0.030 . 2 . . . A 17 VAL HG13 . 11547 1 224 . 1 1 17 17 VAL HG21 H 1 0.394 0.030 . 2 . . . A 17 VAL HG21 . 11547 1 225 . 1 1 17 17 VAL HG22 H 1 0.394 0.030 . 2 . . . A 17 VAL HG22 . 11547 1 226 . 1 1 17 17 VAL HG23 H 1 0.394 0.030 . 2 . . . A 17 VAL HG23 . 11547 1 227 . 1 1 17 17 VAL C C 13 173.990 0.300 . 1 . . . A 17 VAL C . 11547 1 228 . 1 1 17 17 VAL CA C 13 58.592 0.300 . 1 . . . A 17 VAL CA . 11547 1 229 . 1 1 17 17 VAL CB C 13 36.448 0.300 . 1 . . . A 17 VAL CB . 11547 1 230 . 1 1 17 17 VAL CG1 C 13 22.638 0.300 . 2 . . . A 17 VAL CG1 . 11547 1 231 . 1 1 17 17 VAL CG2 C 13 20.208 0.300 . 2 . . . A 17 VAL CG2 . 11547 1 232 . 1 1 17 17 VAL N N 15 119.125 0.300 . 1 . . . A 17 VAL N . 11547 1 233 . 1 1 18 18 GLU H H 1 8.503 0.030 . 1 . . . A 18 GLU H . 11547 1 234 . 1 1 18 18 GLU HA H 1 5.036 0.030 . 1 . . . A 18 GLU HA . 11547 1 235 . 1 1 18 18 GLU HB2 H 1 1.585 0.030 . 2 . . . A 18 GLU HB2 . 11547 1 236 . 1 1 18 18 GLU HB3 H 1 2.127 0.030 . 2 . . . A 18 GLU HB3 . 11547 1 237 . 1 1 18 18 GLU HG2 H 1 2.201 0.030 . 2 . . . A 18 GLU HG2 . 11547 1 238 . 1 1 18 18 GLU HG3 H 1 2.355 0.030 . 2 . . . A 18 GLU HG3 . 11547 1 239 . 1 1 18 18 GLU CA C 13 52.694 0.300 . 1 . . . A 18 GLU CA . 11547 1 240 . 1 1 18 18 GLU CB C 13 30.901 0.300 . 1 . . . A 18 GLU CB . 11547 1 241 . 1 1 18 18 GLU CG C 13 35.367 0.300 . 1 . . . A 18 GLU CG . 11547 1 242 . 1 1 18 18 GLU N N 15 120.060 0.300 . 1 . . . A 18 GLU N . 11547 1 243 . 1 1 19 19 PRO HA H 1 4.117 0.030 . 1 . . . A 19 PRO HA . 11547 1 244 . 1 1 19 19 PRO HB2 H 1 2.437 0.030 . 1 . . . A 19 PRO HB2 . 11547 1 245 . 1 1 19 19 PRO HB3 H 1 2.437 0.030 . 1 . . . A 19 PRO HB3 . 11547 1 246 . 1 1 19 19 PRO HG2 H 1 2.210 0.030 . 2 . . . A 19 PRO HG2 . 11547 1 247 . 1 1 19 19 PRO HG3 H 1 2.058 0.030 . 2 . . . A 19 PRO HG3 . 11547 1 248 . 1 1 19 19 PRO HD2 H 1 3.984 0.030 . 2 . . . A 19 PRO HD2 . 11547 1 249 . 1 1 19 19 PRO HD3 H 1 3.781 0.030 . 2 . . . A 19 PRO HD3 . 11547 1 250 . 1 1 19 19 PRO C C 13 175.530 0.300 . 1 . . . A 19 PRO C . 11547 1 251 . 1 1 19 19 PRO CA C 13 65.222 0.300 . 1 . . . A 19 PRO CA . 11547 1 252 . 1 1 19 19 PRO CB C 13 32.001 0.300 . 1 . . . A 19 PRO CB . 11547 1 253 . 1 1 19 19 PRO CG C 13 28.228 0.300 . 1 . . . A 19 PRO CG . 11547 1 254 . 1 1 19 19 PRO CD C 13 50.613 0.300 . 1 . . . A 19 PRO CD . 11547 1 255 . 1 1 20 20 SER H H 1 7.219 0.030 . 1 . . . A 20 SER H . 11547 1 256 . 1 1 20 20 SER HA H 1 4.359 0.030 . 1 . . . A 20 SER HA . 11547 1 257 . 1 1 20 20 SER HB2 H 1 4.137 0.030 . 2 . . . A 20 SER HB2 . 11547 1 258 . 1 1 20 20 SER HB3 H 1 3.798 0.030 . 2 . . . A 20 SER HB3 . 11547 1 259 . 1 1 20 20 SER C C 13 174.666 0.300 . 1 . . . A 20 SER C . 11547 1 260 . 1 1 20 20 SER CA C 13 57.541 0.300 . 1 . . . A 20 SER CA . 11547 1 261 . 1 1 20 20 SER CB C 13 63.479 0.300 . 1 . . . A 20 SER CB . 11547 1 262 . 1 1 20 20 SER N N 15 131.028 0.300 . 1 . . . A 20 SER N . 11547 1 263 . 1 1 21 21 ASP H H 1 8.169 0.030 . 1 . . . A 21 ASP H . 11547 1 264 . 1 1 21 21 ASP HA H 1 4.620 0.030 . 1 . . . A 21 ASP HA . 11547 1 265 . 1 1 21 21 ASP HB2 H 1 2.866 0.030 . 2 . . . A 21 ASP HB2 . 11547 1 266 . 1 1 21 21 ASP HB3 H 1 2.522 0.030 . 2 . . . A 21 ASP HB3 . 11547 1 267 . 1 1 21 21 ASP C C 13 176.411 0.300 . 1 . . . A 21 ASP C . 11547 1 268 . 1 1 21 21 ASP CA C 13 55.454 0.300 . 1 . . . A 21 ASP CA . 11547 1 269 . 1 1 21 21 ASP CB C 13 40.888 0.300 . 1 . . . A 21 ASP CB . 11547 1 270 . 1 1 21 21 ASP N N 15 125.423 0.300 . 1 . . . A 21 ASP N . 11547 1 271 . 1 1 22 22 THR H H 1 8.238 0.030 . 1 . . . A 22 THR H . 11547 1 272 . 1 1 22 22 THR HA H 1 4.839 0.030 . 1 . . . A 22 THR HA . 11547 1 273 . 1 1 22 22 THR HB H 1 4.862 0.030 . 1 . . . A 22 THR HB . 11547 1 274 . 1 1 22 22 THR HG21 H 1 1.275 0.030 . 1 . . . A 22 THR HG21 . 11547 1 275 . 1 1 22 22 THR HG22 H 1 1.275 0.030 . 1 . . . A 22 THR HG22 . 11547 1 276 . 1 1 22 22 THR HG23 H 1 1.275 0.030 . 1 . . . A 22 THR HG23 . 11547 1 277 . 1 1 22 22 THR C C 13 176.254 0.300 . 1 . . . A 22 THR C . 11547 1 278 . 1 1 22 22 THR CB C 13 70.888 0.300 . 1 . . . A 22 THR CB . 11547 1 279 . 1 1 22 22 THR CG2 C 13 22.620 0.300 . 1 . . . A 22 THR CG2 . 11547 1 280 . 1 1 22 22 THR N N 15 110.899 0.300 . 1 . . . A 22 THR N . 11547 1 281 . 1 1 23 23 ILE H H 1 8.829 0.030 . 1 . . . A 23 ILE H . 11547 1 282 . 1 1 23 23 ILE HA H 1 3.571 0.030 . 1 . . . A 23 ILE HA . 11547 1 283 . 1 1 23 23 ILE HB H 1 2.604 0.030 . 1 . . . A 23 ILE HB . 11547 1 284 . 1 1 23 23 ILE HG12 H 1 1.828 0.030 . 2 . . . A 23 ILE HG12 . 11547 1 285 . 1 1 23 23 ILE HG13 H 1 1.194 0.030 . 2 . . . A 23 ILE HG13 . 11547 1 286 . 1 1 23 23 ILE HG21 H 1 0.817 0.030 . 1 . . . A 23 ILE HG21 . 11547 1 287 . 1 1 23 23 ILE HG22 H 1 0.817 0.030 . 1 . . . A 23 ILE HG22 . 11547 1 288 . 1 1 23 23 ILE HG23 H 1 0.817 0.030 . 1 . . . A 23 ILE HG23 . 11547 1 289 . 1 1 23 23 ILE HD11 H 1 0.550 0.030 . 1 . . . A 23 ILE HD11 . 11547 1 290 . 1 1 23 23 ILE HD12 H 1 0.550 0.030 . 1 . . . A 23 ILE HD12 . 11547 1 291 . 1 1 23 23 ILE HD13 H 1 0.550 0.030 . 1 . . . A 23 ILE HD13 . 11547 1 292 . 1 1 23 23 ILE C C 13 179.100 0.300 . 1 . . . A 23 ILE C . 11547 1 293 . 1 1 23 23 ILE CA C 13 62.316 0.300 . 1 . . . A 23 ILE CA . 11547 1 294 . 1 1 23 23 ILE CB C 13 34.227 0.300 . 1 . . . A 23 ILE CB . 11547 1 295 . 1 1 23 23 ILE CG1 C 13 28.094 0.300 . 1 . . . A 23 ILE CG1 . 11547 1 296 . 1 1 23 23 ILE CG2 C 13 19.237 0.300 . 1 . . . A 23 ILE CG2 . 11547 1 297 . 1 1 23 23 ILE CD1 C 13 9.960 0.300 . 1 . . . A 23 ILE CD1 . 11547 1 298 . 1 1 23 23 ILE N N 15 123.555 0.300 . 1 . . . A 23 ILE N . 11547 1 299 . 1 1 24 24 GLU H H 1 9.609 0.030 . 1 . . . A 24 GLU H . 11547 1 300 . 1 1 24 24 GLU HA H 1 3.885 0.030 . 1 . . . A 24 GLU HA . 11547 1 301 . 1 1 24 24 GLU HB2 H 1 2.039 0.030 . 1 . . . A 24 GLU HB2 . 11547 1 302 . 1 1 24 24 GLU HB3 H 1 2.039 0.030 . 1 . . . A 24 GLU HB3 . 11547 1 303 . 1 1 24 24 GLU HG2 H 1 2.285 0.030 . 1 . . . A 24 GLU HG2 . 11547 1 304 . 1 1 24 24 GLU HG3 H 1 2.285 0.030 . 1 . . . A 24 GLU HG3 . 11547 1 305 . 1 1 24 24 GLU C C 13 178.852 0.300 . 1 . . . A 24 GLU C . 11547 1 306 . 1 1 24 24 GLU CA C 13 59.965 0.300 . 1 . . . A 24 GLU CA . 11547 1 307 . 1 1 24 24 GLU CB C 13 29.229 0.300 . 1 . . . A 24 GLU CB . 11547 1 308 . 1 1 24 24 GLU CG C 13 35.647 0.300 . 1 . . . A 24 GLU CG . 11547 1 309 . 1 1 24 24 GLU N N 15 122.124 0.300 . 1 . . . A 24 GLU N . 11547 1 310 . 1 1 25 25 ASN H H 1 8.075 0.030 . 1 . . . A 25 ASN H . 11547 1 311 . 1 1 25 25 ASN HA H 1 4.481 0.030 . 1 . . . A 25 ASN HA . 11547 1 312 . 1 1 25 25 ASN HB2 H 1 2.951 0.030 . 2 . . . A 25 ASN HB2 . 11547 1 313 . 1 1 25 25 ASN HB3 H 1 3.161 0.030 . 2 . . . A 25 ASN HB3 . 11547 1 314 . 1 1 25 25 ASN HD21 H 1 6.971 0.030 . 2 . . . A 25 ASN HD21 . 11547 1 315 . 1 1 25 25 ASN HD22 H 1 7.750 0.030 . 2 . . . A 25 ASN HD22 . 11547 1 316 . 1 1 25 25 ASN C C 13 178.438 0.300 . 1 . . . A 25 ASN C . 11547 1 317 . 1 1 25 25 ASN CA C 13 56.209 0.300 . 1 . . . A 25 ASN CA . 11547 1 318 . 1 1 25 25 ASN CB C 13 38.799 0.300 . 1 . . . A 25 ASN CB . 11547 1 319 . 1 1 25 25 ASN N N 15 122.741 0.300 . 1 . . . A 25 ASN N . 11547 1 320 . 1 1 25 25 ASN ND2 N 15 112.558 0.300 . 1 . . . A 25 ASN ND2 . 11547 1 321 . 1 1 26 26 VAL H H 1 8.405 0.030 . 1 . . . A 26 VAL H . 11547 1 322 . 1 1 26 26 VAL HA H 1 3.395 0.030 . 1 . . . A 26 VAL HA . 11547 1 323 . 1 1 26 26 VAL HB H 1 2.259 0.030 . 1 . . . A 26 VAL HB . 11547 1 324 . 1 1 26 26 VAL HG11 H 1 0.665 0.030 . 2 . . . A 26 VAL HG11 . 11547 1 325 . 1 1 26 26 VAL HG12 H 1 0.665 0.030 . 2 . . . A 26 VAL HG12 . 11547 1 326 . 1 1 26 26 VAL HG13 H 1 0.665 0.030 . 2 . . . A 26 VAL HG13 . 11547 1 327 . 1 1 26 26 VAL HG21 H 1 1.000 0.030 . 2 . . . A 26 VAL HG21 . 11547 1 328 . 1 1 26 26 VAL HG22 H 1 1.000 0.030 . 2 . . . A 26 VAL HG22 . 11547 1 329 . 1 1 26 26 VAL HG23 H 1 1.000 0.030 . 2 . . . A 26 VAL HG23 . 11547 1 330 . 1 1 26 26 VAL C C 13 178.202 0.300 . 1 . . . A 26 VAL C . 11547 1 331 . 1 1 26 26 VAL CA C 13 67.384 0.300 . 1 . . . A 26 VAL CA . 11547 1 332 . 1 1 26 26 VAL CB C 13 30.860 0.300 . 1 . . . A 26 VAL CB . 11547 1 333 . 1 1 26 26 VAL CG1 C 13 22.157 0.300 . 2 . . . A 26 VAL CG1 . 11547 1 334 . 1 1 26 26 VAL CG2 C 13 23.796 0.300 . 2 . . . A 26 VAL CG2 . 11547 1 335 . 1 1 26 26 VAL N N 15 122.982 0.300 . 1 . . . A 26 VAL N . 11547 1 336 . 1 1 27 27 LYS H H 1 8.671 0.030 . 1 . . . A 27 LYS H . 11547 1 337 . 1 1 27 27 LYS HA H 1 3.817 0.030 . 1 . . . A 27 LYS HA . 11547 1 338 . 1 1 27 27 LYS HB2 H 1 2.008 0.030 . 2 . . . A 27 LYS HB2 . 11547 1 339 . 1 1 27 27 LYS HB3 H 1 1.750 0.030 . 2 . . . A 27 LYS HB3 . 11547 1 340 . 1 1 27 27 LYS HG2 H 1 1.205 0.030 . 2 . . . A 27 LYS HG2 . 11547 1 341 . 1 1 27 27 LYS HG3 H 1 1.676 0.030 . 2 . . . A 27 LYS HG3 . 11547 1 342 . 1 1 27 27 LYS HD2 H 1 1.708 0.030 . 2 . . . A 27 LYS HD2 . 11547 1 343 . 1 1 27 27 LYS HD3 H 1 1.579 0.030 . 2 . . . A 27 LYS HD3 . 11547 1 344 . 1 1 27 27 LYS HE2 H 1 2.772 0.030 . 1 . . . A 27 LYS HE2 . 11547 1 345 . 1 1 27 27 LYS HE3 H 1 2.772 0.030 . 1 . . . A 27 LYS HE3 . 11547 1 346 . 1 1 27 27 LYS C C 13 179.553 0.300 . 1 . . . A 27 LYS C . 11547 1 347 . 1 1 27 27 LYS CA C 13 60.573 0.300 . 1 . . . A 27 LYS CA . 11547 1 348 . 1 1 27 27 LYS CB C 13 31.990 0.300 . 1 . . . A 27 LYS CB . 11547 1 349 . 1 1 27 27 LYS CG C 13 26.556 0.300 . 1 . . . A 27 LYS CG . 11547 1 350 . 1 1 27 27 LYS CD C 13 29.817 0.300 . 1 . . . A 27 LYS CD . 11547 1 351 . 1 1 27 27 LYS CE C 13 41.676 0.300 . 1 . . . A 27 LYS CE . 11547 1 352 . 1 1 27 27 LYS N N 15 119.439 0.300 . 1 . . . A 27 LYS N . 11547 1 353 . 1 1 28 28 ALA H H 1 8.197 0.030 . 1 . . . A 28 ALA H . 11547 1 354 . 1 1 28 28 ALA HA H 1 4.198 0.030 . 1 . . . A 28 ALA HA . 11547 1 355 . 1 1 28 28 ALA HB1 H 1 1.617 0.030 . 1 . . . A 28 ALA HB1 . 11547 1 356 . 1 1 28 28 ALA HB2 H 1 1.617 0.030 . 1 . . . A 28 ALA HB2 . 11547 1 357 . 1 1 28 28 ALA HB3 H 1 1.617 0.030 . 1 . . . A 28 ALA HB3 . 11547 1 358 . 1 1 28 28 ALA C C 13 179.552 0.300 . 1 . . . A 28 ALA C . 11547 1 359 . 1 1 28 28 ALA CA C 13 55.258 0.300 . 1 . . . A 28 ALA CA . 11547 1 360 . 1 1 28 28 ALA CB C 13 18.194 0.300 . 1 . . . A 28 ALA CB . 11547 1 361 . 1 1 28 28 ALA N N 15 125.755 0.300 . 1 . . . A 28 ALA N . 11547 1 362 . 1 1 29 29 LYS H H 1 8.010 0.030 . 1 . . . A 29 LYS H . 11547 1 363 . 1 1 29 29 LYS HA H 1 4.180 0.030 . 1 . . . A 29 LYS HA . 11547 1 364 . 1 1 29 29 LYS HB2 H 1 2.115 0.030 . 2 . . . A 29 LYS HB2 . 11547 1 365 . 1 1 29 29 LYS HB3 H 1 1.925 0.030 . 2 . . . A 29 LYS HB3 . 11547 1 366 . 1 1 29 29 LYS HG2 H 1 1.553 0.030 . 2 . . . A 29 LYS HG2 . 11547 1 367 . 1 1 29 29 LYS HG3 H 1 1.724 0.030 . 2 . . . A 29 LYS HG3 . 11547 1 368 . 1 1 29 29 LYS HD2 H 1 1.462 0.030 . 2 . . . A 29 LYS HD2 . 11547 1 369 . 1 1 29 29 LYS HD3 H 1 1.780 0.030 . 2 . . . A 29 LYS HD3 . 11547 1 370 . 1 1 29 29 LYS HE2 H 1 3.012 0.030 . 2 . . . A 29 LYS HE2 . 11547 1 371 . 1 1 29 29 LYS HE3 H 1 3.145 0.030 . 2 . . . A 29 LYS HE3 . 11547 1 372 . 1 1 29 29 LYS C C 13 180.324 0.300 . 1 . . . A 29 LYS C . 11547 1 373 . 1 1 29 29 LYS CA C 13 59.518 0.300 . 1 . . . A 29 LYS CA . 11547 1 374 . 1 1 29 29 LYS CB C 13 33.279 0.300 . 1 . . . A 29 LYS CB . 11547 1 375 . 1 1 29 29 LYS CG C 13 26.272 0.300 . 1 . . . A 29 LYS CG . 11547 1 376 . 1 1 29 29 LYS CD C 13 30.169 0.300 . 1 . . . A 29 LYS CD . 11547 1 377 . 1 1 29 29 LYS CE C 13 42.385 0.300 . 1 . . . A 29 LYS CE . 11547 1 378 . 1 1 29 29 LYS N N 15 121.385 0.300 . 1 . . . A 29 LYS N . 11547 1 379 . 1 1 30 30 ILE H H 1 8.177 0.030 . 1 . . . A 30 ILE H . 11547 1 380 . 1 1 30 30 ILE HA H 1 3.498 0.030 . 1 . . . A 30 ILE HA . 11547 1 381 . 1 1 30 30 ILE HB H 1 2.092 0.030 . 1 . . . A 30 ILE HB . 11547 1 382 . 1 1 30 30 ILE HG12 H 1 0.795 0.030 . 2 . . . A 30 ILE HG12 . 11547 1 383 . 1 1 30 30 ILE HG13 H 1 1.999 0.030 . 2 . . . A 30 ILE HG13 . 11547 1 384 . 1 1 30 30 ILE HG21 H 1 0.834 0.030 . 1 . . . A 30 ILE HG21 . 11547 1 385 . 1 1 30 30 ILE HG22 H 1 0.834 0.030 . 1 . . . A 30 ILE HG22 . 11547 1 386 . 1 1 30 30 ILE HG23 H 1 0.834 0.030 . 1 . . . A 30 ILE HG23 . 11547 1 387 . 1 1 30 30 ILE HD11 H 1 0.847 0.030 . 1 . . . A 30 ILE HD11 . 11547 1 388 . 1 1 30 30 ILE HD12 H 1 0.847 0.030 . 1 . . . A 30 ILE HD12 . 11547 1 389 . 1 1 30 30 ILE HD13 H 1 0.847 0.030 . 1 . . . A 30 ILE HD13 . 11547 1 390 . 1 1 30 30 ILE C C 13 177.645 0.300 . 1 . . . A 30 ILE C . 11547 1 391 . 1 1 30 30 ILE CA C 13 65.362 0.300 . 1 . . . A 30 ILE CA . 11547 1 392 . 1 1 30 30 ILE CB C 13 37.665 0.300 . 1 . . . A 30 ILE CB . 11547 1 393 . 1 1 30 30 ILE CG1 C 13 29.746 0.300 . 1 . . . A 30 ILE CG1 . 11547 1 394 . 1 1 30 30 ILE CG2 C 13 18.743 0.300 . 1 . . . A 30 ILE CG2 . 11547 1 395 . 1 1 30 30 ILE CD1 C 13 16.631 0.300 . 1 . . . A 30 ILE CD1 . 11547 1 396 . 1 1 30 30 ILE N N 15 121.536 0.300 . 1 . . . A 30 ILE N . 11547 1 397 . 1 1 31 31 GLN H H 1 8.140 0.030 . 1 . . . A 31 GLN H . 11547 1 398 . 1 1 31 31 GLN HA H 1 3.904 0.030 . 1 . . . A 31 GLN HA . 11547 1 399 . 1 1 31 31 GLN HB2 H 1 2.415 0.030 . 2 . . . A 31 GLN HB2 . 11547 1 400 . 1 1 31 31 GLN HB3 H 1 2.069 0.030 . 2 . . . A 31 GLN HB3 . 11547 1 401 . 1 1 31 31 GLN HG2 H 1 2.120 0.030 . 2 . . . A 31 GLN HG2 . 11547 1 402 . 1 1 31 31 GLN HG3 H 1 2.371 0.030 . 2 . . . A 31 GLN HG3 . 11547 1 403 . 1 1 31 31 GLN HE21 H 1 7.643 0.030 . 2 . . . A 31 GLN HE21 . 11547 1 404 . 1 1 31 31 GLN HE22 H 1 7.009 0.030 . 2 . . . A 31 GLN HE22 . 11547 1 405 . 1 1 31 31 GLN C C 13 178.693 0.300 . 1 . . . A 31 GLN C . 11547 1 406 . 1 1 31 31 GLN CA C 13 59.464 0.300 . 1 . . . A 31 GLN CA . 11547 1 407 . 1 1 31 31 GLN CB C 13 28.011 0.300 . 1 . . . A 31 GLN CB . 11547 1 408 . 1 1 31 31 GLN CG C 13 34.198 0.300 . 1 . . . A 31 GLN CG . 11547 1 409 . 1 1 31 31 GLN N N 15 123.133 0.300 . 1 . . . A 31 GLN N . 11547 1 410 . 1 1 31 31 GLN NE2 N 15 112.897 0.300 . 1 . . . A 31 GLN NE2 . 11547 1 411 . 1 1 32 32 ASP H H 1 8.295 0.030 . 1 . . . A 32 ASP H . 11547 1 412 . 1 1 32 32 ASP HA H 1 4.353 0.030 . 1 . . . A 32 ASP HA . 11547 1 413 . 1 1 32 32 ASP HB2 H 1 2.809 0.030 . 2 . . . A 32 ASP HB2 . 11547 1 414 . 1 1 32 32 ASP HB3 H 1 2.779 0.030 . 2 . . . A 32 ASP HB3 . 11547 1 415 . 1 1 32 32 ASP C C 13 177.578 0.300 . 1 . . . A 32 ASP C . 11547 1 416 . 1 1 32 32 ASP CA C 13 57.006 0.300 . 1 . . . A 32 ASP CA . 11547 1 417 . 1 1 32 32 ASP CB C 13 41.167 0.300 . 1 . . . A 32 ASP CB . 11547 1 418 . 1 1 32 32 ASP N N 15 121.024 0.300 . 1 . . . A 32 ASP N . 11547 1 419 . 1 1 33 33 LYS H H 1 7.716 0.030 . 1 . . . A 33 LYS H . 11547 1 420 . 1 1 33 33 LYS HA H 1 4.270 0.030 . 1 . . . A 33 LYS HA . 11547 1 421 . 1 1 33 33 LYS HB2 H 1 1.951 0.030 . 2 . . . A 33 LYS HB2 . 11547 1 422 . 1 1 33 33 LYS HB3 H 1 1.887 0.030 . 2 . . . A 33 LYS HB3 . 11547 1 423 . 1 1 33 33 LYS HG2 H 1 1.595 0.030 . 1 . . . A 33 LYS HG2 . 11547 1 424 . 1 1 33 33 LYS HG3 H 1 1.595 0.030 . 1 . . . A 33 LYS HG3 . 11547 1 425 . 1 1 33 33 LYS HD2 H 1 1.722 0.030 . 1 . . . A 33 LYS HD2 . 11547 1 426 . 1 1 33 33 LYS HD3 H 1 1.722 0.030 . 1 . . . A 33 LYS HD3 . 11547 1 427 . 1 1 33 33 LYS HE2 H 1 3.141 0.030 . 1 . . . A 33 LYS HE2 . 11547 1 428 . 1 1 33 33 LYS HE3 H 1 3.141 0.030 . 1 . . . A 33 LYS HE3 . 11547 1 429 . 1 1 33 33 LYS C C 13 177.907 0.300 . 1 . . . A 33 LYS C . 11547 1 430 . 1 1 33 33 LYS CA C 13 58.030 0.300 . 1 . . . A 33 LYS CA . 11547 1 431 . 1 1 33 33 LYS CB C 13 33.622 0.300 . 1 . . . A 33 LYS CB . 11547 1 432 . 1 1 33 33 LYS CG C 13 24.990 0.300 . 1 . . . A 33 LYS CG . 11547 1 433 . 1 1 33 33 LYS CD C 13 28.961 0.300 . 1 . . . A 33 LYS CD . 11547 1 434 . 1 1 33 33 LYS CE C 13 42.117 0.300 . 1 . . . A 33 LYS CE . 11547 1 435 . 1 1 33 33 LYS N N 15 117.769 0.300 . 1 . . . A 33 LYS N . 11547 1 436 . 1 1 34 34 GLU H H 1 8.438 0.030 . 1 . . . A 34 GLU H . 11547 1 437 . 1 1 34 34 GLU HA H 1 4.585 0.030 . 1 . . . A 34 GLU HA . 11547 1 438 . 1 1 34 34 GLU HB2 H 1 1.763 0.030 . 2 . . . A 34 GLU HB2 . 11547 1 439 . 1 1 34 34 GLU HB3 H 1 2.219 0.030 . 2 . . . A 34 GLU HB3 . 11547 1 440 . 1 1 34 34 GLU HG2 H 1 2.261 0.030 . 2 . . . A 34 GLU HG2 . 11547 1 441 . 1 1 34 34 GLU HG3 H 1 2.115 0.030 . 2 . . . A 34 GLU HG3 . 11547 1 442 . 1 1 34 34 GLU C C 13 177.397 0.300 . 1 . . . A 34 GLU C . 11547 1 443 . 1 1 34 34 GLU CA C 13 55.243 0.300 . 1 . . . A 34 GLU CA . 11547 1 444 . 1 1 34 34 GLU CB C 13 33.282 0.300 . 1 . . . A 34 GLU CB . 11547 1 445 . 1 1 34 34 GLU CG C 13 36.848 0.300 . 1 . . . A 34 GLU CG . 11547 1 446 . 1 1 34 34 GLU N N 15 115.660 0.300 . 1 . . . A 34 GLU N . 11547 1 447 . 1 1 35 35 GLY H H 1 8.479 0.030 . 1 . . . A 35 GLY H . 11547 1 448 . 1 1 35 35 GLY HA2 H 1 3.962 0.030 . 2 . . . A 35 GLY HA2 . 11547 1 449 . 1 1 35 35 GLY HA3 H 1 4.101 0.030 . 2 . . . A 35 GLY HA3 . 11547 1 450 . 1 1 35 35 GLY C C 13 174.167 0.300 . 1 . . . A 35 GLY C . 11547 1 451 . 1 1 35 35 GLY CA C 13 46.227 0.300 . 1 . . . A 35 GLY CA . 11547 1 452 . 1 1 35 35 GLY N N 15 111.261 0.300 . 1 . . . A 35 GLY N . 11547 1 453 . 1 1 36 36 ILE H H 1 6.697 0.030 . 1 . . . A 36 ILE H . 11547 1 454 . 1 1 36 36 ILE HA H 1 4.370 0.030 . 1 . . . A 36 ILE HA . 11547 1 455 . 1 1 36 36 ILE HB H 1 1.505 0.030 . 1 . . . A 36 ILE HB . 11547 1 456 . 1 1 36 36 ILE HG12 H 1 1.382 0.030 . 2 . . . A 36 ILE HG12 . 11547 1 457 . 1 1 36 36 ILE HG13 H 1 1.101 0.030 . 2 . . . A 36 ILE HG13 . 11547 1 458 . 1 1 36 36 ILE HG21 H 1 0.856 0.030 . 1 . . . A 36 ILE HG21 . 11547 1 459 . 1 1 36 36 ILE HG22 H 1 0.856 0.030 . 1 . . . A 36 ILE HG22 . 11547 1 460 . 1 1 36 36 ILE HG23 H 1 0.856 0.030 . 1 . . . A 36 ILE HG23 . 11547 1 461 . 1 1 36 36 ILE HD11 H 1 0.802 0.030 . 1 . . . A 36 ILE HD11 . 11547 1 462 . 1 1 36 36 ILE HD12 H 1 0.802 0.030 . 1 . . . A 36 ILE HD12 . 11547 1 463 . 1 1 36 36 ILE HD13 H 1 0.802 0.030 . 1 . . . A 36 ILE HD13 . 11547 1 464 . 1 1 36 36 ILE CA C 13 58.484 0.300 . 1 . . . A 36 ILE CA . 11547 1 465 . 1 1 36 36 ILE CB C 13 39.854 0.300 . 1 . . . A 36 ILE CB . 11547 1 466 . 1 1 36 36 ILE CG1 C 13 27.467 0.300 . 1 . . . A 36 ILE CG1 . 11547 1 467 . 1 1 36 36 ILE CG2 C 13 17.620 0.300 . 1 . . . A 36 ILE CG2 . 11547 1 468 . 1 1 36 36 ILE CD1 C 13 14.026 0.300 . 1 . . . A 36 ILE CD1 . 11547 1 469 . 1 1 36 36 ILE N N 15 122.380 0.300 . 1 . . . A 36 ILE N . 11547 1 470 . 1 1 37 37 PRO HA H 1 4.689 0.030 . 1 . . . A 37 PRO HA . 11547 1 471 . 1 1 37 37 PRO HB2 H 1 1.957 0.030 . 2 . . . A 37 PRO HB2 . 11547 1 472 . 1 1 37 37 PRO HB3 H 1 2.360 0.030 . 2 . . . A 37 PRO HB3 . 11547 1 473 . 1 1 37 37 PRO HG2 H 1 2.079 0.030 . 1 . . . A 37 PRO HG2 . 11547 1 474 . 1 1 37 37 PRO HG3 H 1 2.079 0.030 . 1 . . . A 37 PRO HG3 . 11547 1 475 . 1 1 37 37 PRO HD2 H 1 3.605 0.030 . 2 . . . A 37 PRO HD2 . 11547 1 476 . 1 1 37 37 PRO HD3 H 1 4.103 0.030 . 2 . . . A 37 PRO HD3 . 11547 1 477 . 1 1 37 37 PRO CA C 13 61.132 0.300 . 1 . . . A 37 PRO CA . 11547 1 478 . 1 1 37 37 PRO CB C 13 31.927 0.300 . 1 . . . A 37 PRO CB . 11547 1 479 . 1 1 37 37 PRO CG C 13 27.551 0.300 . 1 . . . A 37 PRO CG . 11547 1 480 . 1 1 37 37 PRO CD C 13 51.471 0.300 . 1 . . . A 37 PRO CD . 11547 1 481 . 1 1 38 38 PRO HA H 1 4.371 0.030 . 1 . . . A 38 PRO HA . 11547 1 482 . 1 1 38 38 PRO HB2 H 1 2.232 0.030 . 2 . . . A 38 PRO HB2 . 11547 1 483 . 1 1 38 38 PRO HB3 H 1 2.038 0.030 . 2 . . . A 38 PRO HB3 . 11547 1 484 . 1 1 38 38 PRO HG2 H 1 2.078 0.030 . 2 . . . A 38 PRO HG2 . 11547 1 485 . 1 1 38 38 PRO HG3 H 1 1.861 0.030 . 2 . . . A 38 PRO HG3 . 11547 1 486 . 1 1 38 38 PRO HD2 H 1 3.824 0.030 . 2 . . . A 38 PRO HD2 . 11547 1 487 . 1 1 38 38 PRO HD3 H 1 3.776 0.030 . 2 . . . A 38 PRO HD3 . 11547 1 488 . 1 1 38 38 PRO C C 13 177.783 0.300 . 1 . . . A 38 PRO C . 11547 1 489 . 1 1 38 38 PRO CA C 13 64.817 0.300 . 1 . . . A 38 PRO CA . 11547 1 490 . 1 1 38 38 PRO CB C 13 32.940 0.300 . 1 . . . A 38 PRO CB . 11547 1 491 . 1 1 38 38 PRO CG C 13 27.547 0.300 . 1 . . . A 38 PRO CG . 11547 1 492 . 1 1 38 38 PRO CD C 13 51.543 0.300 . 1 . . . A 38 PRO CD . 11547 1 493 . 1 1 39 39 ASP H H 1 8.385 0.030 . 1 . . . A 39 ASP H . 11547 1 494 . 1 1 39 39 ASP HA H 1 4.487 0.030 . 1 . . . A 39 ASP HA . 11547 1 495 . 1 1 39 39 ASP HB2 H 1 2.697 0.030 . 2 . . . A 39 ASP HB2 . 11547 1 496 . 1 1 39 39 ASP HB3 H 1 2.732 0.030 . 2 . . . A 39 ASP HB3 . 11547 1 497 . 1 1 39 39 ASP C C 13 176.850 0.300 . 1 . . . A 39 ASP C . 11547 1 498 . 1 1 39 39 ASP CA C 13 54.986 0.300 . 1 . . . A 39 ASP CA . 11547 1 499 . 1 1 39 39 ASP CB C 13 40.430 0.300 . 1 . . . A 39 ASP CB . 11547 1 500 . 1 1 39 39 ASP N N 15 115.118 0.300 . 1 . . . A 39 ASP N . 11547 1 501 . 1 1 40 40 GLN H H 1 7.651 0.030 . 1 . . . A 40 GLN H . 11547 1 502 . 1 1 40 40 GLN HA H 1 4.337 0.030 . 1 . . . A 40 GLN HA . 11547 1 503 . 1 1 40 40 GLN HB2 H 1 1.880 0.030 . 2 . . . A 40 GLN HB2 . 11547 1 504 . 1 1 40 40 GLN HB3 H 1 2.234 0.030 . 2 . . . A 40 GLN HB3 . 11547 1 505 . 1 1 40 40 GLN HG2 H 1 2.327 0.030 . 2 . . . A 40 GLN HG2 . 11547 1 506 . 1 1 40 40 GLN HG3 H 1 2.388 0.030 . 2 . . . A 40 GLN HG3 . 11547 1 507 . 1 1 40 40 GLN HE21 H 1 7.724 0.030 . 2 . . . A 40 GLN HE21 . 11547 1 508 . 1 1 40 40 GLN HE22 H 1 6.978 0.030 . 2 . . . A 40 GLN HE22 . 11547 1 509 . 1 1 40 40 GLN C C 13 175.654 0.300 . 1 . . . A 40 GLN C . 11547 1 510 . 1 1 40 40 GLN CA C 13 56.073 0.300 . 1 . . . A 40 GLN CA . 11547 1 511 . 1 1 40 40 GLN CB C 13 29.913 0.300 . 1 . . . A 40 GLN CB . 11547 1 512 . 1 1 40 40 GLN CG C 13 34.157 0.300 . 1 . . . A 40 GLN CG . 11547 1 513 . 1 1 40 40 GLN N N 15 117.890 0.300 . 1 . . . A 40 GLN N . 11547 1 514 . 1 1 40 40 GLN NE2 N 15 114.607 0.300 . 1 . . . A 40 GLN NE2 . 11547 1 515 . 1 1 41 41 ASN H H 1 7.720 0.030 . 1 . . . A 41 ASN H . 11547 1 516 . 1 1 41 41 ASN HA H 1 5.286 0.030 . 1 . . . A 41 ASN HA . 11547 1 517 . 1 1 41 41 ASN HB2 H 1 2.624 0.030 . 2 . . . A 41 ASN HB2 . 11547 1 518 . 1 1 41 41 ASN HB3 H 1 2.578 0.030 . 2 . . . A 41 ASN HB3 . 11547 1 519 . 1 1 41 41 ASN HD21 H 1 6.607 0.030 . 2 . . . A 41 ASN HD21 . 11547 1 520 . 1 1 41 41 ASN HD22 H 1 7.340 0.030 . 2 . . . A 41 ASN HD22 . 11547 1 521 . 1 1 41 41 ASN C C 13 173.961 0.300 . 1 . . . A 41 ASN C . 11547 1 522 . 1 1 41 41 ASN CA C 13 52.755 0.300 . 1 . . . A 41 ASN CA . 11547 1 523 . 1 1 41 41 ASN CB C 13 43.102 0.300 . 1 . . . A 41 ASN CB . 11547 1 524 . 1 1 41 41 ASN N N 15 117.016 0.300 . 1 . . . A 41 ASN N . 11547 1 525 . 1 1 41 41 ASN ND2 N 15 113.939 0.300 . 1 . . . A 41 ASN ND2 . 11547 1 526 . 1 1 42 42 ARG H H 1 9.134 0.030 . 1 . . . A 42 ARG H . 11547 1 527 . 1 1 42 42 ARG HA H 1 4.542 0.030 . 1 . . . A 42 ARG HA . 11547 1 528 . 1 1 42 42 ARG HB2 H 1 1.660 0.030 . 1 . . . A 42 ARG HB2 . 11547 1 529 . 1 1 42 42 ARG HB3 H 1 1.660 0.030 . 1 . . . A 42 ARG HB3 . 11547 1 530 . 1 1 42 42 ARG HG2 H 1 1.439 0.030 . 1 . . . A 42 ARG HG2 . 11547 1 531 . 1 1 42 42 ARG HG3 H 1 1.439 0.030 . 1 . . . A 42 ARG HG3 . 11547 1 532 . 1 1 42 42 ARG HD2 H 1 3.112 0.030 . 1 . . . A 42 ARG HD2 . 11547 1 533 . 1 1 42 42 ARG HD3 H 1 3.112 0.030 . 1 . . . A 42 ARG HD3 . 11547 1 534 . 1 1 42 42 ARG C C 13 173.913 0.300 . 1 . . . A 42 ARG C . 11547 1 535 . 1 1 42 42 ARG CA C 13 54.225 0.300 . 1 . . . A 42 ARG CA . 11547 1 536 . 1 1 42 42 ARG CB C 13 32.812 0.300 . 1 . . . A 42 ARG CB . 11547 1 537 . 1 1 42 42 ARG CG C 13 26.945 0.300 . 1 . . . A 42 ARG CG . 11547 1 538 . 1 1 42 42 ARG CD C 13 43.626 0.300 . 1 . . . A 42 ARG CD . 11547 1 539 . 1 1 42 42 ARG N N 15 120.060 0.300 . 1 . . . A 42 ARG N . 11547 1 540 . 1 1 43 43 LEU H H 1 8.951 0.030 . 1 . . . A 43 LEU H . 11547 1 541 . 1 1 43 43 LEU HA H 1 5.232 0.030 . 1 . . . A 43 LEU HA . 11547 1 542 . 1 1 43 43 LEU HB2 H 1 1.415 0.030 . 2 . . . A 43 LEU HB2 . 11547 1 543 . 1 1 43 43 LEU HB3 H 1 1.341 0.030 . 2 . . . A 43 LEU HB3 . 11547 1 544 . 1 1 43 43 LEU HG H 1 1.567 0.030 . 1 . . . A 43 LEU HG . 11547 1 545 . 1 1 43 43 LEU HD11 H 1 0.719 0.030 . 2 . . . A 43 LEU HD11 . 11547 1 546 . 1 1 43 43 LEU HD12 H 1 0.719 0.030 . 2 . . . A 43 LEU HD12 . 11547 1 547 . 1 1 43 43 LEU HD13 H 1 0.719 0.030 . 2 . . . A 43 LEU HD13 . 11547 1 548 . 1 1 43 43 LEU HD21 H 1 0.753 0.030 . 2 . . . A 43 LEU HD21 . 11547 1 549 . 1 1 43 43 LEU HD22 H 1 0.753 0.030 . 2 . . . A 43 LEU HD22 . 11547 1 550 . 1 1 43 43 LEU HD23 H 1 0.753 0.030 . 2 . . . A 43 LEU HD23 . 11547 1 551 . 1 1 43 43 LEU C C 13 175.133 0.300 . 1 . . . A 43 LEU C . 11547 1 552 . 1 1 43 43 LEU CA C 13 53.504 0.300 . 1 . . . A 43 LEU CA . 11547 1 553 . 1 1 43 43 LEU CB C 13 45.485 0.300 . 1 . . . A 43 LEU CB . 11547 1 554 . 1 1 43 43 LEU CG C 13 27.043 0.300 . 1 . . . A 43 LEU CG . 11547 1 555 . 1 1 43 43 LEU CD1 C 13 26.055 0.300 . 2 . . . A 43 LEU CD1 . 11547 1 556 . 1 1 43 43 LEU CD2 C 13 26.250 0.300 . 2 . . . A 43 LEU CD2 . 11547 1 557 . 1 1 43 43 LEU N N 15 123.736 0.300 . 1 . . . A 43 LEU N . 11547 1 558 . 1 1 44 44 ILE H H 1 9.143 0.030 . 1 . . . A 44 ILE H . 11547 1 559 . 1 1 44 44 ILE HA H 1 4.929 0.030 . 1 . . . A 44 ILE HA . 11547 1 560 . 1 1 44 44 ILE HB H 1 1.670 0.030 . 1 . . . A 44 ILE HB . 11547 1 561 . 1 1 44 44 ILE HG12 H 1 1.296 0.030 . 2 . . . A 44 ILE HG12 . 11547 1 562 . 1 1 44 44 ILE HG13 H 1 1.220 0.030 . 2 . . . A 44 ILE HG13 . 11547 1 563 . 1 1 44 44 ILE HG21 H 1 0.641 0.030 . 1 . . . A 44 ILE HG21 . 11547 1 564 . 1 1 44 44 ILE HG22 H 1 0.641 0.030 . 1 . . . A 44 ILE HG22 . 11547 1 565 . 1 1 44 44 ILE HG23 H 1 0.641 0.030 . 1 . . . A 44 ILE HG23 . 11547 1 566 . 1 1 44 44 ILE HD11 H 1 0.623 0.030 . 1 . . . A 44 ILE HD11 . 11547 1 567 . 1 1 44 44 ILE HD12 H 1 0.623 0.030 . 1 . . . A 44 ILE HD12 . 11547 1 568 . 1 1 44 44 ILE HD13 H 1 0.623 0.030 . 1 . . . A 44 ILE HD13 . 11547 1 569 . 1 1 44 44 ILE C C 13 176.044 0.300 . 1 . . . A 44 ILE C . 11547 1 570 . 1 1 44 44 ILE CB C 13 40.565 0.300 . 1 . . . A 44 ILE CB . 11547 1 571 . 1 1 44 44 ILE CG1 C 13 27.520 0.300 . 1 . . . A 44 ILE CG1 . 11547 1 572 . 1 1 44 44 ILE CG2 C 13 17.861 0.300 . 1 . . . A 44 ILE CG2 . 11547 1 573 . 1 1 44 44 ILE CD1 C 13 12.663 0.300 . 1 . . . A 44 ILE CD1 . 11547 1 574 . 1 1 44 44 ILE N N 15 122.229 0.300 . 1 . . . A 44 ILE N . 11547 1 575 . 1 1 45 45 PHE H H 1 8.654 0.030 . 1 . . . A 45 PHE H . 11547 1 576 . 1 1 45 45 PHE HA H 1 5.245 0.030 . 1 . . . A 45 PHE HA . 11547 1 577 . 1 1 45 45 PHE HB2 H 1 3.057 0.030 . 2 . . . A 45 PHE HB2 . 11547 1 578 . 1 1 45 45 PHE HB3 H 1 2.816 0.030 . 2 . . . A 45 PHE HB3 . 11547 1 579 . 1 1 45 45 PHE HD1 H 1 7.354 0.030 . 1 . . . A 45 PHE HD1 . 11547 1 580 . 1 1 45 45 PHE HD2 H 1 7.354 0.030 . 1 . . . A 45 PHE HD2 . 11547 1 581 . 1 1 45 45 PHE HE1 H 1 7.552 0.030 . 1 . . . A 45 PHE HE1 . 11547 1 582 . 1 1 45 45 PHE HE2 H 1 7.552 0.030 . 1 . . . A 45 PHE HE2 . 11547 1 583 . 1 1 45 45 PHE HZ H 1 7.497 0.030 . 1 . . . A 45 PHE HZ . 11547 1 584 . 1 1 45 45 PHE C C 13 174.899 0.300 . 1 . . . A 45 PHE C . 11547 1 585 . 1 1 45 45 PHE CA C 13 56.196 0.300 . 1 . . . A 45 PHE CA . 11547 1 586 . 1 1 45 45 PHE CB C 13 43.722 0.300 . 1 . . . A 45 PHE CB . 11547 1 587 . 1 1 45 45 PHE CD1 C 13 132.218 0.300 . 1 . . . A 45 PHE CD1 . 11547 1 588 . 1 1 45 45 PHE CD2 C 13 132.218 0.300 . 1 . . . A 45 PHE CD2 . 11547 1 589 . 1 1 45 45 PHE CE1 C 13 132.381 0.300 . 1 . . . A 45 PHE CE1 . 11547 1 590 . 1 1 45 45 PHE CE2 C 13 132.381 0.300 . 1 . . . A 45 PHE CE2 . 11547 1 591 . 1 1 45 45 PHE CZ C 13 130.354 0.300 . 1 . . . A 45 PHE CZ . 11547 1 592 . 1 1 45 45 PHE N N 15 123.344 0.300 . 1 . . . A 45 PHE N . 11547 1 593 . 1 1 46 46 ALA H H 1 9.285 0.030 . 1 . . . A 46 ALA H . 11547 1 594 . 1 1 46 46 ALA HA H 1 3.742 0.030 . 1 . . . A 46 ALA HA . 11547 1 595 . 1 1 46 46 ALA HB1 H 1 0.827 0.030 . 1 . . . A 46 ALA HB1 . 11547 1 596 . 1 1 46 46 ALA HB2 H 1 0.827 0.030 . 1 . . . A 46 ALA HB2 . 11547 1 597 . 1 1 46 46 ALA HB3 H 1 0.827 0.030 . 1 . . . A 46 ALA HB3 . 11547 1 598 . 1 1 46 46 ALA C C 13 177.550 0.300 . 1 . . . A 46 ALA C . 11547 1 599 . 1 1 46 46 ALA CA C 13 52.490 0.300 . 1 . . . A 46 ALA CA . 11547 1 600 . 1 1 46 46 ALA CB C 13 16.892 0.300 . 1 . . . A 46 ALA CB . 11547 1 601 . 1 1 46 46 ALA N N 15 109.724 0.300 . 1 . . . A 46 ALA N . 11547 1 602 . 1 1 47 47 GLY H H 1 8.266 0.030 . 1 . . . A 47 GLY H . 11547 1 603 . 1 1 47 47 GLY HA2 H 1 3.478 0.030 . 2 . . . A 47 GLY HA2 . 11547 1 604 . 1 1 47 47 GLY HA3 H 1 4.108 0.030 . 2 . . . A 47 GLY HA3 . 11547 1 605 . 1 1 47 47 GLY C C 13 173.866 0.300 . 1 . . . A 47 GLY C . 11547 1 606 . 1 1 47 47 GLY CA C 13 45.541 0.300 . 1 . . . A 47 GLY CA . 11547 1 607 . 1 1 47 47 GLY N N 15 130.275 0.300 . 1 . . . A 47 GLY N . 11547 1 608 . 1 1 48 48 LYS H H 1 7.973 0.030 . 1 . . . A 48 LYS H . 11547 1 609 . 1 1 48 48 LYS HA H 1 4.529 0.030 . 1 . . . A 48 LYS HA . 11547 1 610 . 1 1 48 48 LYS HB2 H 1 1.924 0.030 . 2 . . . A 48 LYS HB2 . 11547 1 611 . 1 1 48 48 LYS HB3 H 1 1.851 0.030 . 2 . . . A 48 LYS HB3 . 11547 1 612 . 1 1 48 48 LYS HG2 H 1 1.473 0.030 . 1 . . . A 48 LYS HG2 . 11547 1 613 . 1 1 48 48 LYS HG3 H 1 1.473 0.030 . 1 . . . A 48 LYS HG3 . 11547 1 614 . 1 1 48 48 LYS HD2 H 1 1.805 0.030 . 2 . . . A 48 LYS HD2 . 11547 1 615 . 1 1 48 48 LYS HD3 H 1 1.859 0.030 . 2 . . . A 48 LYS HD3 . 11547 1 616 . 1 1 48 48 LYS HE2 H 1 3.170 0.030 . 1 . . . A 48 LYS HE2 . 11547 1 617 . 1 1 48 48 LYS HE3 H 1 3.170 0.030 . 1 . . . A 48 LYS HE3 . 11547 1 618 . 1 1 48 48 LYS C C 13 174.918 0.300 . 1 . . . A 48 LYS C . 11547 1 619 . 1 1 48 48 LYS CA C 13 54.636 0.300 . 1 . . . A 48 LYS CA . 11547 1 620 . 1 1 48 48 LYS CB C 13 34.158 0.300 . 1 . . . A 48 LYS CB . 11547 1 621 . 1 1 48 48 LYS CG C 13 24.451 0.300 . 1 . . . A 48 LYS CG . 11547 1 622 . 1 1 48 48 LYS CD C 13 29.032 0.300 . 1 . . . A 48 LYS CD . 11547 1 623 . 1 1 48 48 LYS CE C 13 42.246 0.300 . 1 . . . A 48 LYS CE . 11547 1 624 . 1 1 48 48 LYS N N 15 123.465 0.300 . 1 . . . A 48 LYS N . 11547 1 625 . 1 1 49 49 GLN H H 1 8.792 0.030 . 1 . . . A 49 GLN H . 11547 1 626 . 1 1 49 49 GLN HA H 1 4.257 0.030 . 1 . . . A 49 GLN HA . 11547 1 627 . 1 1 49 49 GLN HB2 H 1 1.993 0.030 . 2 . . . A 49 GLN HB2 . 11547 1 628 . 1 1 49 49 GLN HB3 H 1 1.951 0.030 . 2 . . . A 49 GLN HB3 . 11547 1 629 . 1 1 49 49 GLN HG2 H 1 2.188 0.030 . 2 . . . A 49 GLN HG2 . 11547 1 630 . 1 1 49 49 GLN HG3 H 1 2.255 0.030 . 2 . . . A 49 GLN HG3 . 11547 1 631 . 1 1 49 49 GLN HE21 H 1 6.940 0.030 . 2 . . . A 49 GLN HE21 . 11547 1 632 . 1 1 49 49 GLN HE22 H 1 7.723 0.030 . 2 . . . A 49 GLN HE22 . 11547 1 633 . 1 1 49 49 GLN C C 13 175.349 0.300 . 1 . . . A 49 GLN C . 11547 1 634 . 1 1 49 49 GLN CA C 13 56.373 0.300 . 1 . . . A 49 GLN CA . 11547 1 635 . 1 1 49 49 GLN CB C 13 28.702 0.300 . 1 . . . A 49 GLN CB . 11547 1 636 . 1 1 49 49 GLN CG C 13 34.309 0.300 . 1 . . . A 49 GLN CG . 11547 1 637 . 1 1 49 49 GLN N N 15 124.369 0.300 . 1 . . . A 49 GLN N . 11547 1 638 . 1 1 49 49 GLN NE2 N 15 114.257 0.300 . 1 . . . A 49 GLN NE2 . 11547 1 639 . 1 1 50 50 LEU H H 1 8.507 0.030 . 1 . . . A 50 LEU H . 11547 1 640 . 1 1 50 50 LEU HA H 1 4.084 0.030 . 1 . . . A 50 LEU HA . 11547 1 641 . 1 1 50 50 LEU HB2 H 1 1.517 0.030 . 2 . . . A 50 LEU HB2 . 11547 1 642 . 1 1 50 50 LEU HB3 H 1 0.953 0.030 . 2 . . . A 50 LEU HB3 . 11547 1 643 . 1 1 50 50 LEU HG H 1 1.489 0.030 . 1 . . . A 50 LEU HG . 11547 1 644 . 1 1 50 50 LEU HD11 H 1 0.486 0.030 . 2 . . . A 50 LEU HD11 . 11547 1 645 . 1 1 50 50 LEU HD12 H 1 0.486 0.030 . 2 . . . A 50 LEU HD12 . 11547 1 646 . 1 1 50 50 LEU HD13 H 1 0.486 0.030 . 2 . . . A 50 LEU HD13 . 11547 1 647 . 1 1 50 50 LEU HD21 H 1 -0.235 0.030 . 2 . . . A 50 LEU HD21 . 11547 1 648 . 1 1 50 50 LEU HD22 H 1 -0.235 0.030 . 2 . . . A 50 LEU HD22 . 11547 1 649 . 1 1 50 50 LEU HD23 H 1 -0.235 0.030 . 2 . . . A 50 LEU HD23 . 11547 1 650 . 1 1 50 50 LEU C C 13 176.749 0.300 . 1 . . . A 50 LEU C . 11547 1 651 . 1 1 50 50 LEU CA C 13 53.760 0.300 . 1 . . . A 50 LEU CA . 11547 1 652 . 1 1 50 50 LEU CB C 13 41.571 0.300 . 1 . . . A 50 LEU CB . 11547 1 653 . 1 1 50 50 LEU CG C 13 25.735 0.300 . 1 . . . A 50 LEU CG . 11547 1 654 . 1 1 50 50 LEU CD1 C 13 26.137 0.300 . 2 . . . A 50 LEU CD1 . 11547 1 655 . 1 1 50 50 LEU CD2 C 13 19.668 0.300 . 2 . . . A 50 LEU CD2 . 11547 1 656 . 1 1 50 50 LEU N N 15 126.749 0.300 . 1 . . . A 50 LEU N . 11547 1 657 . 1 1 51 51 GLU H H 1 8.768 0.030 . 1 . . . A 51 GLU H . 11547 1 658 . 1 1 51 51 GLU HA H 1 4.407 0.030 . 1 . . . A 51 GLU HA . 11547 1 659 . 1 1 51 51 GLU HB2 H 1 2.222 0.030 . 2 . . . A 51 GLU HB2 . 11547 1 660 . 1 1 51 51 GLU HB3 H 1 1.973 0.030 . 2 . . . A 51 GLU HB3 . 11547 1 661 . 1 1 51 51 GLU HG2 H 1 2.353 0.030 . 2 . . . A 51 GLU HG2 . 11547 1 662 . 1 1 51 51 GLU HG3 H 1 2.450 0.030 . 2 . . . A 51 GLU HG3 . 11547 1 663 . 1 1 51 51 GLU C C 13 176.287 0.300 . 1 . . . A 51 GLU C . 11547 1 664 . 1 1 51 51 GLU CA C 13 56.019 0.300 . 1 . . . A 51 GLU CA . 11547 1 665 . 1 1 51 51 GLU CB C 13 30.929 0.300 . 1 . . . A 51 GLU CB . 11547 1 666 . 1 1 51 51 GLU CG C 13 36.446 0.300 . 1 . . . A 51 GLU CG . 11547 1 667 . 1 1 51 51 GLU N N 15 125.725 0.300 . 1 . . . A 51 GLU N . 11547 1 668 . 1 1 52 52 ASP H H 1 8.495 0.030 . 1 . . . A 52 ASP H . 11547 1 669 . 1 1 52 52 ASP HA H 1 4.388 0.030 . 1 . . . A 52 ASP HA . 11547 1 670 . 1 1 52 52 ASP HB2 H 1 2.690 0.030 . 2 . . . A 52 ASP HB2 . 11547 1 671 . 1 1 52 52 ASP HB3 H 1 2.588 0.030 . 2 . . . A 52 ASP HB3 . 11547 1 672 . 1 1 52 52 ASP CA C 13 56.973 0.300 . 1 . . . A 52 ASP CA . 11547 1 673 . 1 1 52 52 ASP CB C 13 41.032 0.300 . 1 . . . A 52 ASP CB . 11547 1 674 . 1 1 52 52 ASP N N 15 122.741 0.300 . 1 . . . A 52 ASP N . 11547 1 675 . 1 1 53 53 GLY H H 1 9.052 0.030 . 1 . . . A 53 GLY H . 11547 1 676 . 1 1 53 53 GLY HA2 H 1 4.252 0.030 . 2 . . . A 53 GLY HA2 . 11547 1 677 . 1 1 53 53 GLY HA3 H 1 3.890 0.030 . 2 . . . A 53 GLY HA3 . 11547 1 678 . 1 1 53 53 GLY C C 13 175.316 0.300 . 1 . . . A 53 GLY C . 11547 1 679 . 1 1 53 53 GLY CA C 13 45.402 0.300 . 1 . . . A 53 GLY CA . 11547 1 680 . 1 1 54 54 ARG H H 1 7.508 0.030 . 1 . . . A 54 ARG H . 11547 1 681 . 1 1 54 54 ARG HA H 1 4.644 0.030 . 1 . . . A 54 ARG HA . 11547 1 682 . 1 1 54 54 ARG HB2 H 1 2.227 0.030 . 2 . . . A 54 ARG HB2 . 11547 1 683 . 1 1 54 54 ARG HB3 H 1 2.136 0.030 . 2 . . . A 54 ARG HB3 . 11547 1 684 . 1 1 54 54 ARG HG2 H 1 1.621 0.030 . 2 . . . A 54 ARG HG2 . 11547 1 685 . 1 1 54 54 ARG HG3 H 1 1.813 0.030 . 2 . . . A 54 ARG HG3 . 11547 1 686 . 1 1 54 54 ARG HD2 H 1 3.072 0.030 . 2 . . . A 54 ARG HD2 . 11547 1 687 . 1 1 54 54 ARG HD3 H 1 3.168 0.030 . 2 . . . A 54 ARG HD3 . 11547 1 688 . 1 1 54 54 ARG C C 13 174.961 0.300 . 1 . . . A 54 ARG C . 11547 1 689 . 1 1 54 54 ARG CA C 13 54.690 0.300 . 1 . . . A 54 ARG CA . 11547 1 690 . 1 1 54 54 ARG CB C 13 32.403 0.300 . 1 . . . A 54 ARG CB . 11547 1 691 . 1 1 54 54 ARG CG C 13 27.819 0.300 . 1 . . . A 54 ARG CG . 11547 1 692 . 1 1 54 54 ARG CD C 13 42.975 0.300 . 1 . . . A 54 ARG CD . 11547 1 693 . 1 1 54 54 ARG N N 15 121.174 0.300 . 1 . . . A 54 ARG N . 11547 1 694 . 1 1 55 55 THR H H 1 8.914 0.030 . 1 . . . A 55 THR H . 11547 1 695 . 1 1 55 55 THR HA H 1 5.234 0.030 . 1 . . . A 55 THR HA . 11547 1 696 . 1 1 55 55 THR HB H 1 4.534 0.030 . 1 . . . A 55 THR HB . 11547 1 697 . 1 1 55 55 THR HG21 H 1 1.083 0.030 . 1 . . . A 55 THR HG21 . 11547 1 698 . 1 1 55 55 THR HG22 H 1 1.083 0.030 . 1 . . . A 55 THR HG22 . 11547 1 699 . 1 1 55 55 THR HG23 H 1 1.083 0.030 . 1 . . . A 55 THR HG23 . 11547 1 700 . 1 1 55 55 THR C C 13 176.464 0.300 . 1 . . . A 55 THR C . 11547 1 701 . 1 1 55 55 THR CA C 13 59.773 0.300 . 1 . . . A 55 THR CA . 11547 1 702 . 1 1 55 55 THR CB C 13 72.455 0.300 . 1 . . . A 55 THR CB . 11547 1 703 . 1 1 55 55 THR CG2 C 13 22.711 0.300 . 1 . . . A 55 THR CG2 . 11547 1 704 . 1 1 55 55 THR N N 15 109.302 0.300 . 1 . . . A 55 THR N . 11547 1 705 . 1 1 56 56 LEU H H 1 8.147 0.030 . 1 . . . A 56 LEU H . 11547 1 706 . 1 1 56 56 LEU HA H 1 4.014 0.030 . 1 . . . A 56 LEU HA . 11547 1 707 . 1 1 56 56 LEU HB2 H 1 2.140 0.030 . 2 . . . A 56 LEU HB2 . 11547 1 708 . 1 1 56 56 LEU HB3 H 1 1.193 0.030 . 2 . . . A 56 LEU HB3 . 11547 1 709 . 1 1 56 56 LEU HG H 1 1.657 0.030 . 1 . . . A 56 LEU HG . 11547 1 710 . 1 1 56 56 LEU HD11 H 1 0.734 0.030 . 2 . . . A 56 LEU HD11 . 11547 1 711 . 1 1 56 56 LEU HD12 H 1 0.734 0.030 . 2 . . . A 56 LEU HD12 . 11547 1 712 . 1 1 56 56 LEU HD13 H 1 0.734 0.030 . 2 . . . A 56 LEU HD13 . 11547 1 713 . 1 1 56 56 LEU HD21 H 1 0.608 0.030 . 2 . . . A 56 LEU HD21 . 11547 1 714 . 1 1 56 56 LEU HD22 H 1 0.608 0.030 . 2 . . . A 56 LEU HD22 . 11547 1 715 . 1 1 56 56 LEU HD23 H 1 0.608 0.030 . 2 . . . A 56 LEU HD23 . 11547 1 716 . 1 1 56 56 LEU C C 13 180.848 0.300 . 1 . . . A 56 LEU C . 11547 1 717 . 1 1 56 56 LEU CA C 13 58.659 0.300 . 1 . . . A 56 LEU CA . 11547 1 718 . 1 1 56 56 LEU CB C 13 40.357 0.300 . 1 . . . A 56 LEU CB . 11547 1 719 . 1 1 56 56 LEU CG C 13 26.953 0.300 . 1 . . . A 56 LEU CG . 11547 1 720 . 1 1 56 56 LEU CD1 C 13 27.376 0.300 . 2 . . . A 56 LEU CD1 . 11547 1 721 . 1 1 56 56 LEU CD2 C 13 23.819 0.300 . 2 . . . A 56 LEU CD2 . 11547 1 722 . 1 1 56 56 LEU N N 15 119.065 0.300 . 1 . . . A 56 LEU N . 11547 1 723 . 1 1 57 57 SER H H 1 8.751 0.030 . 1 . . . A 57 SER H . 11547 1 724 . 1 1 57 57 SER HA H 1 4.247 0.030 . 1 . . . A 57 SER HA . 11547 1 725 . 1 1 57 57 SER HB2 H 1 3.819 0.030 . 2 . . . A 57 SER HB2 . 11547 1 726 . 1 1 57 57 SER HB3 H 1 3.707 0.030 . 2 . . . A 57 SER HB3 . 11547 1 727 . 1 1 57 57 SER C C 13 178.652 0.300 . 1 . . . A 57 SER C . 11547 1 728 . 1 1 57 57 SER CA C 13 60.829 0.300 . 1 . . . A 57 SER CA . 11547 1 729 . 1 1 57 57 SER CB C 13 62.521 0.300 . 1 . . . A 57 SER CB . 11547 1 730 . 1 1 57 57 SER N N 15 114.937 0.300 . 1 . . . A 57 SER N . 11547 1 731 . 1 1 58 58 ASP H H 1 8.046 0.030 . 1 . . . A 58 ASP H . 11547 1 732 . 1 1 58 58 ASP HA H 1 4.248 0.030 . 1 . . . A 58 ASP HA . 11547 1 733 . 1 1 58 58 ASP HB2 H 1 2.984 0.030 . 2 . . . A 58 ASP HB2 . 11547 1 734 . 1 1 58 58 ASP HB3 H 1 2.266 0.030 . 2 . . . A 58 ASP HB3 . 11547 1 735 . 1 1 58 58 ASP C C 13 177.321 0.300 . 1 . . . A 58 ASP C . 11547 1 736 . 1 1 58 58 ASP CA C 13 57.240 0.300 . 1 . . . A 58 ASP CA . 11547 1 737 . 1 1 58 58 ASP CB C 13 40.165 0.300 . 1 . . . A 58 ASP CB . 11547 1 738 . 1 1 58 58 ASP N N 15 125.966 0.300 . 1 . . . A 58 ASP N . 11547 1 739 . 1 1 59 59 TYR H H 1 7.292 0.030 . 1 . . . A 59 TYR H . 11547 1 740 . 1 1 59 59 TYR HA H 1 4.693 0.030 . 1 . . . A 59 TYR HA . 11547 1 741 . 1 1 59 59 TYR HB2 H 1 3.474 0.030 . 2 . . . A 59 TYR HB2 . 11547 1 742 . 1 1 59 59 TYR HB3 H 1 2.498 0.030 . 2 . . . A 59 TYR HB3 . 11547 1 743 . 1 1 59 59 TYR HD1 H 1 7.277 0.030 . 1 . . . A 59 TYR HD1 . 11547 1 744 . 1 1 59 59 TYR HD2 H 1 7.277 0.030 . 1 . . . A 59 TYR HD2 . 11547 1 745 . 1 1 59 59 TYR HE1 H 1 6.911 0.030 . 1 . . . A 59 TYR HE1 . 11547 1 746 . 1 1 59 59 TYR HE2 H 1 6.911 0.030 . 1 . . . A 59 TYR HE2 . 11547 1 747 . 1 1 59 59 TYR C C 13 174.661 0.300 . 1 . . . A 59 TYR C . 11547 1 748 . 1 1 59 59 TYR CA C 13 58.133 0.300 . 1 . . . A 59 TYR CA . 11547 1 749 . 1 1 59 59 TYR CB C 13 39.918 0.300 . 1 . . . A 59 TYR CB . 11547 1 750 . 1 1 59 59 TYR CD1 C 13 134.016 0.300 . 1 . . . A 59 TYR CD1 . 11547 1 751 . 1 1 59 59 TYR CD2 C 13 134.016 0.300 . 1 . . . A 59 TYR CD2 . 11547 1 752 . 1 1 59 59 TYR CE1 C 13 118.583 0.300 . 1 . . . A 59 TYR CE1 . 11547 1 753 . 1 1 59 59 TYR CE2 C 13 118.583 0.300 . 1 . . . A 59 TYR CE2 . 11547 1 754 . 1 1 59 59 TYR N N 15 117.167 0.300 . 1 . . . A 59 TYR N . 11547 1 755 . 1 1 60 60 ASN H H 1 8.200 0.030 . 1 . . . A 60 ASN H . 11547 1 756 . 1 1 60 60 ASN HA H 1 4.377 0.030 . 1 . . . A 60 ASN HA . 11547 1 757 . 1 1 60 60 ASN HB2 H 1 3.285 0.030 . 2 . . . A 60 ASN HB2 . 11547 1 758 . 1 1 60 60 ASN HB3 H 1 2.808 0.030 . 2 . . . A 60 ASN HB3 . 11547 1 759 . 1 1 60 60 ASN HD21 H 1 6.936 0.030 . 2 . . . A 60 ASN HD21 . 11547 1 760 . 1 1 60 60 ASN HD22 H 1 7.640 0.030 . 2 . . . A 60 ASN HD22 . 11547 1 761 . 1 1 60 60 ASN C C 13 174.393 0.300 . 1 . . . A 60 ASN C . 11547 1 762 . 1 1 60 60 ASN CA C 13 54.046 0.300 . 1 . . . A 60 ASN CA . 11547 1 763 . 1 1 60 60 ASN CB C 13 37.466 0.300 . 1 . . . A 60 ASN CB . 11547 1 764 . 1 1 60 60 ASN N N 15 117.739 0.300 . 1 . . . A 60 ASN N . 11547 1 765 . 1 1 60 60 ASN ND2 N 15 113.880 0.300 . 1 . . . A 60 ASN ND2 . 11547 1 766 . 1 1 61 61 ILE H H 1 7.427 0.030 . 1 . . . A 61 ILE H . 11547 1 767 . 1 1 61 61 ILE HA H 1 3.341 0.030 . 1 . . . A 61 ILE HA . 11547 1 768 . 1 1 61 61 ILE HB H 1 1.384 0.030 . 1 . . . A 61 ILE HB . 11547 1 769 . 1 1 61 61 ILE HG12 H 1 -0.482 0.030 . 2 . . . A 61 ILE HG12 . 11547 1 770 . 1 1 61 61 ILE HG13 H 1 1.082 0.030 . 2 . . . A 61 ILE HG13 . 11547 1 771 . 1 1 61 61 ILE HG21 H 1 0.439 0.030 . 1 . . . A 61 ILE HG21 . 11547 1 772 . 1 1 61 61 ILE HG22 H 1 0.439 0.030 . 1 . . . A 61 ILE HG22 . 11547 1 773 . 1 1 61 61 ILE HG23 H 1 0.439 0.030 . 1 . . . A 61 ILE HG23 . 11547 1 774 . 1 1 61 61 ILE HD11 H 1 0.470 0.030 . 1 . . . A 61 ILE HD11 . 11547 1 775 . 1 1 61 61 ILE HD12 H 1 0.470 0.030 . 1 . . . A 61 ILE HD12 . 11547 1 776 . 1 1 61 61 ILE HD13 H 1 0.470 0.030 . 1 . . . A 61 ILE HD13 . 11547 1 777 . 1 1 61 61 ILE C C 13 174.665 0.300 . 1 . . . A 61 ILE C . 11547 1 778 . 1 1 61 61 ILE CA C 13 62.316 0.300 . 1 . . . A 61 ILE CA . 11547 1 779 . 1 1 61 61 ILE CB C 13 36.316 0.300 . 1 . . . A 61 ILE CB . 11547 1 780 . 1 1 61 61 ILE CG1 C 13 28.220 0.300 . 1 . . . A 61 ILE CG1 . 11547 1 781 . 1 1 61 61 ILE CG2 C 13 17.981 0.300 . 1 . . . A 61 ILE CG2 . 11547 1 782 . 1 1 61 61 ILE CD1 C 13 15.249 0.300 . 1 . . . A 61 ILE CD1 . 11547 1 783 . 1 1 61 61 ILE N N 15 120.150 0.300 . 1 . . . A 61 ILE N . 11547 1 784 . 1 1 62 62 GLN H H 1 7.916 0.030 . 1 . . . A 62 GLN H . 11547 1 785 . 1 1 62 62 GLN HA H 1 4.474 0.030 . 1 . . . A 62 GLN HA . 11547 1 786 . 1 1 62 62 GLN HB2 H 1 1.912 0.030 . 2 . . . A 62 GLN HB2 . 11547 1 787 . 1 1 62 62 GLN HB3 H 1 2.226 0.030 . 2 . . . A 62 GLN HB3 . 11547 1 788 . 1 1 62 62 GLN HG2 H 1 2.339 0.030 . 2 . . . A 62 GLN HG2 . 11547 1 789 . 1 1 62 62 GLN HG3 H 1 2.290 0.030 . 2 . . . A 62 GLN HG3 . 11547 1 790 . 1 1 62 62 GLN HE21 H 1 6.934 0.030 . 2 . . . A 62 GLN HE21 . 11547 1 791 . 1 1 62 62 GLN HE22 H 1 7.369 0.030 . 2 . . . A 62 GLN HE22 . 11547 1 792 . 1 1 62 62 GLN C C 13 175.921 0.300 . 1 . . . A 62 GLN C . 11547 1 793 . 1 1 62 62 GLN CA C 13 53.760 0.300 . 1 . . . A 62 GLN CA . 11547 1 794 . 1 1 62 62 GLN CB C 13 31.534 0.300 . 1 . . . A 62 GLN CB . 11547 1 795 . 1 1 62 62 GLN CG C 13 33.616 0.300 . 1 . . . A 62 GLN CG . 11547 1 796 . 1 1 62 62 GLN N N 15 126.388 0.300 . 1 . . . A 62 GLN N . 11547 1 797 . 1 1 62 62 GLN NE2 N 15 114.600 0.300 . 1 . . . A 62 GLN NE2 . 11547 1 798 . 1 1 63 63 LYS H H 1 8.645 0.030 . 1 . . . A 63 LYS H . 11547 1 799 . 1 1 63 63 LYS HA H 1 4.042 0.030 . 1 . . . A 63 LYS HA . 11547 1 800 . 1 1 63 63 LYS HB2 H 1 2.069 0.030 . 2 . . . A 63 LYS HB2 . 11547 1 801 . 1 1 63 63 LYS HB3 H 1 1.873 0.030 . 2 . . . A 63 LYS HB3 . 11547 1 802 . 1 1 63 63 LYS HG2 H 1 1.430 0.030 . 2 . . . A 63 LYS HG2 . 11547 1 803 . 1 1 63 63 LYS HG3 H 1 1.488 0.030 . 2 . . . A 63 LYS HG3 . 11547 1 804 . 1 1 63 63 LYS HD2 H 1 0.752 0.030 . 2 . . . A 63 LYS HD2 . 11547 1 805 . 1 1 63 63 LYS HD3 H 1 1.709 0.030 . 2 . . . A 63 LYS HD3 . 11547 1 806 . 1 1 63 63 LYS HE2 H 1 3.022 0.030 . 1 . . . A 63 LYS HE2 . 11547 1 807 . 1 1 63 63 LYS HE3 H 1 3.022 0.030 . 1 . . . A 63 LYS HE3 . 11547 1 808 . 1 1 63 63 LYS C C 13 176.259 0.300 . 1 . . . A 63 LYS C . 11547 1 809 . 1 1 63 63 LYS CA C 13 57.604 0.300 . 1 . . . A 63 LYS CA . 11547 1 810 . 1 1 63 63 LYS CB C 13 32.507 0.300 . 1 . . . A 63 LYS CB . 11547 1 811 . 1 1 63 63 LYS CG C 13 23.982 0.300 . 1 . . . A 63 LYS CG . 11547 1 812 . 1 1 63 63 LYS CD C 13 29.792 0.300 . 1 . . . A 63 LYS CD . 11547 1 813 . 1 1 63 63 LYS CE C 13 42.168 0.300 . 1 . . . A 63 LYS CE . 11547 1 814 . 1 1 63 63 LYS N N 15 121.536 0.300 . 1 . . . A 63 LYS N . 11547 1 815 . 1 1 64 64 GLU H H 1 9.526 0.030 . 1 . . . A 64 GLU H . 11547 1 816 . 1 1 64 64 GLU HA H 1 3.432 0.030 . 1 . . . A 64 GLU HA . 11547 1 817 . 1 1 64 64 GLU HB2 H 1 2.412 0.030 . 2 . . . A 64 GLU HB2 . 11547 1 818 . 1 1 64 64 GLU HB3 H 1 2.526 0.030 . 2 . . . A 64 GLU HB3 . 11547 1 819 . 1 1 64 64 GLU HG2 H 1 2.260 0.030 . 1 . . . A 64 GLU HG2 . 11547 1 820 . 1 1 64 64 GLU HG3 H 1 2.260 0.030 . 1 . . . A 64 GLU HG3 . 11547 1 821 . 1 1 64 64 GLU C C 13 175.397 0.300 . 1 . . . A 64 GLU C . 11547 1 822 . 1 1 64 64 GLU CA C 13 58.087 0.300 . 1 . . . A 64 GLU CA . 11547 1 823 . 1 1 64 64 GLU CB C 13 26.276 0.300 . 1 . . . A 64 GLU CB . 11547 1 824 . 1 1 64 64 GLU CG C 13 37.320 0.300 . 1 . . . A 64 GLU CG . 11547 1 825 . 1 1 64 64 GLU N N 15 115.992 0.300 . 1 . . . A 64 GLU N . 11547 1 826 . 1 1 65 65 SER H H 1 7.741 0.030 . 1 . . . A 65 SER H . 11547 1 827 . 1 1 65 65 SER HA H 1 4.634 0.030 . 1 . . . A 65 SER HA . 11547 1 828 . 1 1 65 65 SER HB2 H 1 3.591 0.030 . 2 . . . A 65 SER HB2 . 11547 1 829 . 1 1 65 65 SER HB3 H 1 3.869 0.030 . 2 . . . A 65 SER HB3 . 11547 1 830 . 1 1 65 65 SER C C 13 172.160 0.300 . 1 . . . A 65 SER C . 11547 1 831 . 1 1 65 65 SER CA C 13 60.832 0.300 . 1 . . . A 65 SER CA . 11547 1 832 . 1 1 65 65 SER CB C 13 65.013 0.300 . 1 . . . A 65 SER CB . 11547 1 833 . 1 1 65 65 SER N N 15 116.624 0.300 . 1 . . . A 65 SER N . 11547 1 834 . 1 1 66 66 THR H H 1 8.971 0.030 . 1 . . . A 66 THR H . 11547 1 835 . 1 1 66 66 THR HA H 1 5.295 0.030 . 1 . . . A 66 THR HA . 11547 1 836 . 1 1 66 66 THR HB H 1 4.118 0.030 . 1 . . . A 66 THR HB . 11547 1 837 . 1 1 66 66 THR HG21 H 1 0.960 0.030 . 1 . . . A 66 THR HG21 . 11547 1 838 . 1 1 66 66 THR HG22 H 1 0.960 0.030 . 1 . . . A 66 THR HG22 . 11547 1 839 . 1 1 66 66 THR HG23 H 1 0.960 0.030 . 1 . . . A 66 THR HG23 . 11547 1 840 . 1 1 66 66 THR C C 13 173.594 0.300 . 1 . . . A 66 THR C . 11547 1 841 . 1 1 66 66 THR CA C 13 62.388 0.300 . 1 . . . A 66 THR CA . 11547 1 842 . 1 1 66 66 THR CB C 13 69.878 0.300 . 1 . . . A 66 THR CB . 11547 1 843 . 1 1 66 66 THR CG2 C 13 21.814 0.300 . 1 . . . A 66 THR CG2 . 11547 1 844 . 1 1 66 66 THR N N 15 118.432 0.300 . 1 . . . A 66 THR N . 11547 1 845 . 1 1 67 67 LEU H H 1 9.403 0.030 . 1 . . . A 67 LEU H . 11547 1 846 . 1 1 67 67 LEU HA H 1 5.212 0.030 . 1 . . . A 67 LEU HA . 11547 1 847 . 1 1 67 67 LEU HB2 H 1 1.564 0.030 . 2 . . . A 67 LEU HB2 . 11547 1 848 . 1 1 67 67 LEU HB3 H 1 1.786 0.030 . 2 . . . A 67 LEU HB3 . 11547 1 849 . 1 1 67 67 LEU HG H 1 1.811 0.030 . 1 . . . A 67 LEU HG . 11547 1 850 . 1 1 67 67 LEU HD11 H 1 0.715 0.030 . 2 . . . A 67 LEU HD11 . 11547 1 851 . 1 1 67 67 LEU HD12 H 1 0.715 0.030 . 2 . . . A 67 LEU HD12 . 11547 1 852 . 1 1 67 67 LEU HD13 H 1 0.715 0.030 . 2 . . . A 67 LEU HD13 . 11547 1 853 . 1 1 67 67 LEU HD21 H 1 0.657 0.030 . 2 . . . A 67 LEU HD21 . 11547 1 854 . 1 1 67 67 LEU HD22 H 1 0.657 0.030 . 2 . . . A 67 LEU HD22 . 11547 1 855 . 1 1 67 67 LEU HD23 H 1 0.657 0.030 . 2 . . . A 67 LEU HD23 . 11547 1 856 . 1 1 67 67 LEU C C 13 175.047 0.300 . 1 . . . A 67 LEU C . 11547 1 857 . 1 1 67 67 LEU CA C 13 54.167 0.300 . 1 . . . A 67 LEU CA . 11547 1 858 . 1 1 67 67 LEU CB C 13 44.636 0.300 . 1 . . . A 67 LEU CB . 11547 1 859 . 1 1 67 67 LEU CG C 13 29.939 0.300 . 1 . . . A 67 LEU CG . 11547 1 860 . 1 1 67 67 LEU CD1 C 13 25.519 0.300 . 2 . . . A 67 LEU CD1 . 11547 1 861 . 1 1 67 67 LEU CD2 C 13 26.065 0.300 . 2 . . . A 67 LEU CD2 . 11547 1 862 . 1 1 67 67 LEU N N 15 129.913 0.300 . 1 . . . A 67 LEU N . 11547 1 863 . 1 1 68 68 HIS H H 1 9.134 0.030 . 1 . . . A 68 HIS H . 11547 1 864 . 1 1 68 68 HIS HA H 1 5.116 0.030 . 1 . . . A 68 HIS HA . 11547 1 865 . 1 1 68 68 HIS HB2 H 1 2.822 0.030 . 2 . . . A 68 HIS HB2 . 11547 1 866 . 1 1 68 68 HIS HB3 H 1 2.987 0.030 . 2 . . . A 68 HIS HB3 . 11547 1 867 . 1 1 68 68 HIS HD2 H 1 6.908 0.030 . 1 . . . A 68 HIS HD2 . 11547 1 868 . 1 1 68 68 HIS HE1 H 1 7.714 0.030 . 1 . . . A 68 HIS HE1 . 11547 1 869 . 1 1 68 68 HIS C C 13 173.999 0.300 . 1 . . . A 68 HIS C . 11547 1 870 . 1 1 68 68 HIS CA C 13 56.032 0.300 . 1 . . . A 68 HIS CA . 11547 1 871 . 1 1 68 68 HIS CB C 13 33.167 0.300 . 1 . . . A 68 HIS CB . 11547 1 872 . 1 1 68 68 HIS CD2 C 13 118.975 0.300 . 1 . . . A 68 HIS CD2 . 11547 1 873 . 1 1 68 68 HIS CE1 C 13 138.725 0.300 . 1 . . . A 68 HIS CE1 . 11547 1 874 . 1 1 68 68 HIS N N 15 119.246 0.300 . 1 . . . A 68 HIS N . 11547 1 875 . 1 1 69 69 LEU H H 1 8.299 0.030 . 1 . . . A 69 LEU H . 11547 1 876 . 1 1 69 69 LEU HA H 1 5.134 0.030 . 1 . . . A 69 LEU HA . 11547 1 877 . 1 1 69 69 LEU HB2 H 1 1.276 0.030 . 2 . . . A 69 LEU HB2 . 11547 1 878 . 1 1 69 69 LEU HB3 H 1 1.615 0.030 . 2 . . . A 69 LEU HB3 . 11547 1 879 . 1 1 69 69 LEU HG H 1 1.375 0.030 . 1 . . . A 69 LEU HG . 11547 1 880 . 1 1 69 69 LEU HD11 H 1 0.834 0.030 . 2 . . . A 69 LEU HD11 . 11547 1 881 . 1 1 69 69 LEU HD12 H 1 0.834 0.030 . 2 . . . A 69 LEU HD12 . 11547 1 882 . 1 1 69 69 LEU HD13 H 1 0.834 0.030 . 2 . . . A 69 LEU HD13 . 11547 1 883 . 1 1 69 69 LEU HD21 H 1 0.797 0.030 . 2 . . . A 69 LEU HD21 . 11547 1 884 . 1 1 69 69 LEU HD22 H 1 0.797 0.030 . 2 . . . A 69 LEU HD22 . 11547 1 885 . 1 1 69 69 LEU HD23 H 1 0.797 0.030 . 2 . . . A 69 LEU HD23 . 11547 1 886 . 1 1 69 69 LEU C C 13 176.192 0.300 . 1 . . . A 69 LEU C . 11547 1 887 . 1 1 69 69 LEU CA C 13 53.975 0.300 . 1 . . . A 69 LEU CA . 11547 1 888 . 1 1 69 69 LEU CB C 13 44.061 0.300 . 1 . . . A 69 LEU CB . 11547 1 889 . 1 1 69 69 LEU CG C 13 26.903 0.300 . 1 . . . A 69 LEU CG . 11547 1 890 . 1 1 69 69 LEU CD1 C 13 26.463 0.300 . 2 . . . A 69 LEU CD1 . 11547 1 891 . 1 1 69 69 LEU CD2 C 13 25.752 0.300 . 2 . . . A 69 LEU CD2 . 11547 1 892 . 1 1 69 69 LEU N N 15 125.001 0.300 . 1 . . . A 69 LEU N . 11547 1 893 . 1 1 70 70 VAL H H 1 9.004 0.030 . 1 . . . A 70 VAL H . 11547 1 894 . 1 1 70 70 VAL HA H 1 4.630 0.030 . 1 . . . A 70 VAL HA . 11547 1 895 . 1 1 70 70 VAL HB H 1 2.154 0.030 . 1 . . . A 70 VAL HB . 11547 1 896 . 1 1 70 70 VAL HG11 H 1 0.856 0.030 . 2 . . . A 70 VAL HG11 . 11547 1 897 . 1 1 70 70 VAL HG12 H 1 0.856 0.030 . 2 . . . A 70 VAL HG12 . 11547 1 898 . 1 1 70 70 VAL HG13 H 1 0.856 0.030 . 2 . . . A 70 VAL HG13 . 11547 1 899 . 1 1 70 70 VAL HG21 H 1 0.767 0.030 . 2 . . . A 70 VAL HG21 . 11547 1 900 . 1 1 70 70 VAL HG22 H 1 0.767 0.030 . 2 . . . A 70 VAL HG22 . 11547 1 901 . 1 1 70 70 VAL HG23 H 1 0.767 0.030 . 2 . . . A 70 VAL HG23 . 11547 1 902 . 1 1 70 70 VAL C C 13 174.585 0.300 . 1 . . . A 70 VAL C . 11547 1 903 . 1 1 70 70 VAL CA C 13 59.564 0.300 . 1 . . . A 70 VAL CA . 11547 1 904 . 1 1 70 70 VAL CB C 13 35.440 0.300 . 1 . . . A 70 VAL CB . 11547 1 905 . 1 1 70 70 VAL CG1 C 13 21.763 0.300 . 2 . . . A 70 VAL CG1 . 11547 1 906 . 1 1 70 70 VAL CG2 C 13 20.266 0.300 . 2 . . . A 70 VAL CG2 . 11547 1 907 . 1 1 70 70 VAL N N 15 121.506 0.300 . 1 . . . A 70 VAL N . 11547 1 908 . 1 1 71 71 LEU H H 1 8.348 0.030 . 1 . . . A 71 LEU H . 11547 1 909 . 1 1 71 71 LEU HA H 1 4.511 0.030 . 1 . . . A 71 LEU HA . 11547 1 910 . 1 1 71 71 LEU HB2 H 1 1.620 0.030 . 2 . . . A 71 LEU HB2 . 11547 1 911 . 1 1 71 71 LEU HB3 H 1 1.575 0.030 . 2 . . . A 71 LEU HB3 . 11547 1 912 . 1 1 71 71 LEU HD11 H 1 0.969 0.030 . 2 . . . A 71 LEU HD11 . 11547 1 913 . 1 1 71 71 LEU HD12 H 1 0.969 0.030 . 2 . . . A 71 LEU HD12 . 11547 1 914 . 1 1 71 71 LEU HD13 H 1 0.969 0.030 . 2 . . . A 71 LEU HD13 . 11547 1 915 . 1 1 71 71 LEU HD21 H 1 0.927 0.030 . 2 . . . A 71 LEU HD21 . 11547 1 916 . 1 1 71 71 LEU HD22 H 1 0.927 0.030 . 2 . . . A 71 LEU HD22 . 11547 1 917 . 1 1 71 71 LEU HD23 H 1 0.927 0.030 . 2 . . . A 71 LEU HD23 . 11547 1 918 . 1 1 71 71 LEU C C 13 178.321 0.300 . 1 . . . A 71 LEU C . 11547 1 919 . 1 1 71 71 LEU CA C 13 55.651 0.300 . 1 . . . A 71 LEU CA . 11547 1 920 . 1 1 71 71 LEU CB C 13 42.714 0.300 . 1 . . . A 71 LEU CB . 11547 1 921 . 1 1 71 71 LEU CD1 C 13 25.494 0.300 . 2 . . . A 71 LEU CD1 . 11547 1 922 . 1 1 71 71 LEU CD2 C 13 24.519 0.300 . 2 . . . A 71 LEU CD2 . 11547 1 923 . 1 1 71 71 LEU N N 15 123.826 0.300 . 1 . . . A 71 LEU N . 11547 1 924 . 1 1 72 72 ARG H H 1 8.409 0.030 . 1 . . . A 72 ARG H . 11547 1 925 . 1 1 72 72 ARG HA H 1 4.127 0.030 . 1 . . . A 72 ARG HA . 11547 1 926 . 1 1 72 72 ARG HB2 H 1 1.731 0.030 . 2 . . . A 72 ARG HB2 . 11547 1 927 . 1 1 72 72 ARG HB3 H 1 1.529 0.030 . 2 . . . A 72 ARG HB3 . 11547 1 928 . 1 1 72 72 ARG HG2 H 1 1.459 0.030 . 2 . . . A 72 ARG HG2 . 11547 1 929 . 1 1 72 72 ARG HG3 H 1 1.789 0.030 . 2 . . . A 72 ARG HG3 . 11547 1 930 . 1 1 72 72 ARG HD2 H 1 3.106 0.030 . 1 . . . A 72 ARG HD2 . 11547 1 931 . 1 1 72 72 ARG HD3 H 1 3.106 0.030 . 1 . . . A 72 ARG HD3 . 11547 1 932 . 1 1 72 72 ARG C C 13 175.621 0.300 . 1 . . . A 72 ARG C . 11547 1 933 . 1 1 72 72 ARG CA C 13 56.461 0.300 . 1 . . . A 72 ARG CA . 11547 1 934 . 1 1 72 72 ARG CB C 13 30.987 0.300 . 1 . . . A 72 ARG CB . 11547 1 935 . 1 1 72 72 ARG CG C 13 27.340 0.300 . 1 . . . A 72 ARG CG . 11547 1 936 . 1 1 72 72 ARG CD C 13 43.639 0.300 . 1 . . . A 72 ARG CD . 11547 1 937 . 1 1 72 72 ARG N N 15 123.645 0.300 . 1 . . . A 72 ARG N . 11547 1 938 . 1 1 73 73 LEU H H 1 8.515 0.030 . 1 . . . A 73 LEU H . 11547 1 939 . 1 1 73 73 LEU HA H 1 4.360 0.030 . 1 . . . A 73 LEU HA . 11547 1 940 . 1 1 73 73 LEU HB2 H 1 1.633 0.030 . 2 . . . A 73 LEU HB2 . 11547 1 941 . 1 1 73 73 LEU HB3 H 1 1.567 0.030 . 2 . . . A 73 LEU HB3 . 11547 1 942 . 1 1 73 73 LEU HG H 1 1.659 0.030 . 1 . . . A 73 LEU HG . 11547 1 943 . 1 1 73 73 LEU HD11 H 1 0.925 0.030 . 2 . . . A 73 LEU HD11 . 11547 1 944 . 1 1 73 73 LEU HD12 H 1 0.925 0.030 . 2 . . . A 73 LEU HD12 . 11547 1 945 . 1 1 73 73 LEU HD13 H 1 0.925 0.030 . 2 . . . A 73 LEU HD13 . 11547 1 946 . 1 1 73 73 LEU HD21 H 1 0.871 0.030 . 2 . . . A 73 LEU HD21 . 11547 1 947 . 1 1 73 73 LEU HD22 H 1 0.871 0.030 . 2 . . . A 73 LEU HD22 . 11547 1 948 . 1 1 73 73 LEU HD23 H 1 0.871 0.030 . 2 . . . A 73 LEU HD23 . 11547 1 949 . 1 1 73 73 LEU C C 13 177.321 0.300 . 1 . . . A 73 LEU C . 11547 1 950 . 1 1 73 73 LEU CA C 13 54.850 0.300 . 1 . . . A 73 LEU CA . 11547 1 951 . 1 1 73 73 LEU CB C 13 42.248 0.300 . 1 . . . A 73 LEU CB . 11547 1 952 . 1 1 73 73 LEU CG C 13 27.017 0.300 . 1 . . . A 73 LEU CG . 11547 1 953 . 1 1 73 73 LEU CD1 C 13 25.415 0.300 . 2 . . . A 73 LEU CD1 . 11547 1 954 . 1 1 73 73 LEU CD2 C 13 23.920 0.300 . 2 . . . A 73 LEU CD2 . 11547 1 955 . 1 1 73 73 LEU N N 15 125.634 0.300 . 1 . . . A 73 LEU N . 11547 1 956 . 1 1 74 74 ARG H H 1 8.601 0.030 . 1 . . . A 74 ARG H . 11547 1 957 . 1 1 74 74 ARG HA H 1 4.311 0.030 . 1 . . . A 74 ARG HA . 11547 1 958 . 1 1 74 74 ARG HB2 H 1 1.803 0.030 . 2 . . . A 74 ARG HB2 . 11547 1 959 . 1 1 74 74 ARG HB3 H 1 1.866 0.030 . 2 . . . A 74 ARG HB3 . 11547 1 960 . 1 1 74 74 ARG HG2 H 1 1.649 0.030 . 1 . . . A 74 ARG HG2 . 11547 1 961 . 1 1 74 74 ARG HG3 H 1 1.649 0.030 . 1 . . . A 74 ARG HG3 . 11547 1 962 . 1 1 74 74 ARG HD2 H 1 3.203 0.030 . 1 . . . A 74 ARG HD2 . 11547 1 963 . 1 1 74 74 ARG HD3 H 1 3.203 0.030 . 1 . . . A 74 ARG HD3 . 11547 1 964 . 1 1 74 74 ARG C C 13 177.126 0.300 . 1 . . . A 74 ARG C . 11547 1 965 . 1 1 74 74 ARG CA C 13 56.511 0.300 . 1 . . . A 74 ARG CA . 11547 1 966 . 1 1 74 74 ARG CB C 13 30.613 0.300 . 1 . . . A 74 ARG CB . 11547 1 967 . 1 1 74 74 ARG CG C 13 27.017 0.300 . 1 . . . A 74 ARG CG . 11547 1 968 . 1 1 74 74 ARG CD C 13 43.406 0.300 . 1 . . . A 74 ARG CD . 11547 1 969 . 1 1 74 74 ARG N N 15 123.856 0.300 . 1 . . . A 74 ARG N . 11547 1 970 . 1 1 75 75 GLY H H 1 8.539 0.030 . 1 . . . A 75 GLY H . 11547 1 971 . 1 1 75 75 GLY HA2 H 1 3.989 0.030 . 1 . . . A 75 GLY HA2 . 11547 1 972 . 1 1 75 75 GLY HA3 H 1 3.989 0.030 . 1 . . . A 75 GLY HA3 . 11547 1 973 . 1 1 75 75 GLY C C 13 173.723 0.300 . 1 . . . A 75 GLY C . 11547 1 974 . 1 1 75 75 GLY CA C 13 45.478 0.300 . 1 . . . A 75 GLY CA . 11547 1 975 . 1 1 75 75 GLY N N 15 112.436 0.300 . 1 . . . A 75 GLY N . 11547 1 976 . 1 1 76 76 GLY H H 1 8.071 0.030 . 1 . . . A 76 GLY H . 11547 1 977 . 1 1 76 76 GLY HA2 H 1 3.772 0.030 . 2 . . . A 76 GLY HA2 . 11547 1 978 . 1 1 76 76 GLY HA3 H 1 3.833 0.030 . 2 . . . A 76 GLY HA3 . 11547 1 979 . 1 1 76 76 GLY CA C 13 46.354 0.300 . 1 . . . A 76 GLY CA . 11547 1 980 . 1 1 76 76 GLY N N 15 116.474 0.300 . 1 . . . A 76 GLY N . 11547 1 stop_ save_