data_25070 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 25070 _Entry.Title ; NMR structure of the Rad18-UBZ/ubiquitin complex ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2014-07-03 _Entry.Accession_date 2014-07-03 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _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 Alessandro Rizzo . A. . 25070 2 Paige Salerno . E. . 25070 3 Irina Bezsonova . . . 25070 4 Dmitry Korzhnev . M. . 25070 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' . 25070 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'protein complex' . 25070 NMR . 25070 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 25070 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 732 25070 '13C chemical shifts' 438 25070 '15N chemical shifts' 106 25070 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 2 . . 2014-09-26 2014-07-03 update BMRB 'update entry citation' 25070 1 . . 2014-09-19 2014-07-03 original author 'original release' 25070 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 25071 'ubiquitin-binding zinc finger (UBZ) domain from human Rad18' 25070 PDB 2MRE 'BMRB Entry Tracking System' 25070 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 25070 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI 10.1021/bi500823h _Citation.PubMed_ID 25162118 _Citation.Full_citation . _Citation.Title 'NMR Structure of the Human Rad18 Zinc Finger in Complex with Ubiquitin Defines a Class of UBZ Domains in Proteins Linked to the DNA Damage Response.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 53 _Citation.Journal_issue 37 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1520-4995 _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 5895 _Citation.Page_last 5906 _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 Alessandro Rizzo A. A. . 25070 1 2 Paige Salerno P. E. . 25070 1 3 Irina Bezsonova I. . . 25070 1 4 Dmitry Korzhnev D. M. . 25070 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 25070 _Assembly.ID 1 _Assembly.Name 'Rad18-UBZ/ubiquitin complex' _Assembly.BMRB_code . _Assembly.Number_of_components 3 _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 $entity_1 A . yes native no no . . . 25070 1 2 Ubiquitin-binding_zinc_finger_(UBZ)_domain_from_human_Rad18 2 $entity_2 B . yes native no no . . . 25070 1 3 'ZINC ION' 3 $entity_ZN C . no native no no . . . 25070 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 25070 _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 ; GSHMQIFVKTLTGKTITLEV EPSDTIENVKAKIQDKEGIP PDQQRLIFAGKQLEDGRTLS DYNIQKESTLHLVLRLRGG ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq ; G: -2 S: -1 H: 0 M: 1 (first native residue from ubiquitin) ; _Entity.Polymer_author_seq_details "the first three residues 'GSH' are remnants of the thrombin cleavage site and cloning vector" _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 79 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 8859.192 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 11505 . entity . . . . . 96.20 76 98.68 98.68 3.70e-45 . . . . 25070 1 2 no BMRB 11547 . ubiquitin . . . . . 96.20 76 98.68 98.68 3.70e-45 . . . . 25070 1 3 no BMRB 15047 . denatured_ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 4 no BMRB 15410 . Ubi . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 5 no BMRB 15689 . UBB . . . . . 94.94 103 98.67 100.00 8.52e-44 . . . . 25070 1 6 no BMRB 15907 . Ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 7 no BMRB 16228 . ubiquitin . . . . . 96.20 76 97.37 98.68 1.93e-44 . . . . 25070 1 8 no BMRB 16582 . Ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 9 no BMRB 16626 . Ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 10 no BMRB 16895 . UBB+1 . . . . . 94.94 103 98.67 100.00 8.52e-44 . . . . 25070 1 11 no BMRB 17181 . ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 12 no BMRB 17439 . ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 13 no BMRB 17769 . Ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 14 no BMRB 17919 . entity . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 15 no BMRB 18582 . ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 16 no BMRB 18583 . ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 17 no BMRB 18584 . ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 18 no BMRB 18610 . Ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 19 no BMRB 18611 . Ubiquitin_A_state . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 20 no BMRB 18737 . UBIQUITIN . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 21 no BMRB 19406 . entity . . . . . 96.20 152 100.00 100.00 6.87e-45 . . . . 25070 1 22 no BMRB 19412 . entity . . . . . 96.20 152 100.00 100.00 6.87e-45 . . . . 25070 1 23 no BMRB 25123 . Ubiquitin . . . . . 91.14 72 100.00 100.00 8.35e-43 . . . . 25070 1 24 no BMRB 25601 . entity_1 . . . . . 96.20 76 97.37 97.37 5.80e-44 . . . . 25070 1 25 no BMRB 26604 . Ubiquitin_(microcrystalline) . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 26 no BMRB 4245 . ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 27 no BMRB 4375 . Ubiquitin . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 28 no PDB 1AAR . "Structure Of A Diubiquitin Conjugate And A Model For Interaction With Ubiquitin Conjugating Enzyme (E2)" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 29 no PDB 1CMX . "Structural Basis For The Specificity Of Ubiquitin C- Terminal Hydrolases" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 30 no PDB 1D3Z . "Ubiquitin Nmr Structure" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 31 no PDB 1F9J . "Structure Of A New Crystal Form Of Tetraubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 32 no PDB 1FXT . "Structure Of A Conjugating Enzyme-Ubiquitin Thiolester Complex" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 33 no PDB 1G6J . "Structure Of Recombinant Human Ubiquitin In Aot Reverse Micelles" . . . . . 94.94 76 100.00 100.00 6.73e-45 . . . . 25070 1 34 no PDB 1GJZ . "Solution Structure Of A Dimeric N-Terminal Fragment Of Human Ubiquitin" . . . . . 65.82 53 98.08 98.08 2.77e-26 . . . . 25070 1 35 no PDB 1NBF . "Crystal Structure Of A Ubp-Family Deubiquitinating Enzyme In Isolation And In Complex With Ubiquitin Aldehyde" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 36 no PDB 1OGW . "Synthetic Ubiquitin With Fluoro-Leu At 50 And 67" . . . . . 96.20 76 97.37 97.37 3.37e-44 . . . . 25070 1 37 no PDB 1P3Q . "Mechanism Of Ubiquitin Recognition By The Cue Domain Of Vps9" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 38 no PDB 1Q5W . "Ubiquitin Recognition By Npl4 Zinc-Fingers" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 39 no PDB 1S1Q . "Tsg101(Uev) Domain In Complex With Ubiquitin" . . . . . 94.94 76 100.00 100.00 6.73e-45 . . . . 25070 1 40 no PDB 1TBE . "Structure Of Tetraubiquitin Shows How Multiubiquitin Chains Can Be Formed" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 41 no PDB 1UBI . "Synthetic Structural And Biological Studies Of The Ubiquitin System. Part 1" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 42 no PDB 1UBQ . "Structure Of Ubiquitin Refined At 1.8 Angstroms Resolution" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 43 no PDB 1UZX . "A Complex Of The Vps23 Uev With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 44 no PDB 1V80 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 45 no PDB 1V81 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 46 no PDB 1VX7 . "Cryo-em Structure Of The Plasmodium Falciparum 80s Ribosome Bound To The Anti-protozoan Drug Emetine, Large Subunit (protein On" . . . . . 96.20 128 98.68 100.00 1.46e-45 . . . . 25070 1 47 no PDB 1WR6 . "Crystal Structure Of Gga3 Gat Domain In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 48 no PDB 1WRD . "Crystal Structure Of Tom1 Gat Domain In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 49 no PDB 1XD3 . "Crystal Structure Of Uchl3-Ubvme Complex" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 50 no PDB 1XQQ . "Simultaneous Determination Of Protein Structure And Dynamics" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 51 no PDB 1YD8 . "Complex Of Human Gga3 Gat Domain And Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 52 no PDB 1YIW . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin" . . . . . 96.20 76 98.68 100.00 3.07e-45 . . . . 25070 1 53 no PDB 1YJ1 . "X-Ray Crystal Structure Of A Chemically Synthesized [d-Gln35]ubiquitin" . . . . . 96.20 76 97.37 98.68 3.41e-44 . . . . 25070 1 54 no PDB 1YX5 . "Solution Structure Of S5a Uim-1UBIQUITIN COMPLEX" . . . . . 96.20 98 100.00 100.00 4.21e-46 . . . . 25070 1 55 no PDB 1YX6 . "Solution Structure Of S5a Uim-2UBIQUITIN COMPLEX" . . . . . 96.20 98 100.00 100.00 4.21e-46 . . . . 25070 1 56 no PDB 1ZGU . "Solution Structure Of The Human Mms2-Ubiquitin Complex" . . . . . 96.20 76 98.68 100.00 1.90e-45 . . . . 25070 1 57 no PDB 2AYO . "Structure Of Usp14 Bound To Ubquitin Aldehyde" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 58 no PDB 2BGF . "Nmr Structure Of Lys48-Linked Di-Ubiquitin Using Chemical Shift Perturbation Data Together With Rdcs And 15n- Relaxation Data" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 59 no PDB 2C7M . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 60 no PDB 2C7N . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 61 no PDB 2D3G . "Double Sided Ubiquitin Binding Of Hrs-Uim" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 62 no PDB 2DEN . "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 63 no PDB 2DX5 . "The Complex Structure Between The Mouse Eap45-Glue Domain And Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 64 no PDB 2FCM . "X-Ray Crystal Structure Of A Chemically Synthesized [d-Gln35]ubiquitin With A Cubic Space Group" . . . . . 96.20 76 97.37 98.68 3.41e-44 . . . . 25070 1 65 no PDB 2FCN . "X-Ray Crystal Structure Of A Chemically Synthesized [d-Val35]ubiquitin With A Cubic Space Group" . . . . . 96.20 76 97.37 98.68 3.41e-44 . . . . 25070 1 66 no PDB 2FCQ . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin With A Cubic Space Group" . . . . . 96.20 76 98.68 100.00 3.07e-45 . . . . 25070 1 67 no PDB 2FCS . "X-Ray Crystal Structure Of A Chemically Synthesized [l-Gln35]ubiquitin With A Cubic Space Group" . . . . . 96.20 76 97.37 98.68 3.84e-44 . . . . 25070 1 68 no PDB 2FID . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 69 no PDB 2FIF . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 70 no PDB 2FUH . "Solution Structure Of The Ubch5cUB NON-Covalent Complex" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 71 no PDB 2G45 . "Co-Crystal Structure Of Znf Ubp Domain From The Deubiquitinating Enzyme Isopeptidase T (Isot) In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 72 no PDB 2GMI . Mms2UBC13~UBIQUITIN . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 73 no PDB 2HD5 . "Usp2 In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 74 no PDB 2HTH . "Structural Basis For Ubiquitin Recognition By The Human Eap45ESCRT-Ii Glue Domain" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 75 no PDB 2IBI . "Covalent Ubiquitin-Usp2 Complex" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 76 no PDB 2J7Q . "Crystal Structure Of The Ubiquitin-Specific Protease Encoded By Murine Cytomegalovirus Tegument Protein M48 In Complex With A U" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 77 no PDB 2JF5 . "Crystal Structure Of Lys63-Linked Di-Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 78 no PDB 2JRI . "Solution Structure Of The Josephin Domain Of Ataxin-3 In Complex With Ubiquitin Molecule." . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 79 no PDB 2JY6 . "Solution Structure Of The Complex Of Ubiquitin And Ubiquilin 1 Uba Domain" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 80 no PDB 2JZZ . "Solid-State Nmr Structure Of Microcrystalline Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 81 no PDB 2K25 . "Automated Nmr Structure Of The Ubb By Fapsy" . . . . . 94.94 103 98.67 100.00 8.52e-44 . . . . 25070 1 82 no PDB 2K39 . "Recognition Dynamics Up To Microseconds Revealed From Rdc Derived Ubiquitin Ensemble In Solution" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 83 no PDB 2K6D . "Cin85 Sh3-C Domain In Complex With Ubiquitin" . . . . . 94.94 76 100.00 100.00 4.50e-45 . . . . 25070 1 84 no PDB 2K8B . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Cis Isomer In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 85 no PDB 2K8C . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Trans Isomer In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 86 no PDB 2KDE . "Nmr Structure Of Major S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 87 no PDB 2KDF . "Nmr Structure Of Minor S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 88 no PDB 2KHW . "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 1.50e-48 . . . . 25070 1 89 no PDB 2KJH . "Nmr Based Structural Model Of The Ubch8-Ubiquitin Complex" . . . . . 94.94 76 100.00 100.00 4.50e-45 . . . . 25070 1 90 no PDB 2KLG . "Pere Nmr Structure Of Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 91 no PDB 2KN5 . "A Correspondence Between Solution-State Dynamics Of An Individual Protein And The Sequence And Conformational Diversity Of Its " . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 92 no PDB 2KOX . "Nmr Residual Dipolar Couplings Identify Long Range Correlated Motions In The Backbone Of The Protein Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 93 no PDB 2KTF . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 94 no PDB 2KWU . "Solution Structure Of Ubm2 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 95 no PDB 2KWV . "Solution Structure Of Ubm1 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 96 no PDB 2KX0 . "The Solution Structure Of Ubb+1, Frameshift Mutant Of Ubiquitin B" . . . . . 94.94 103 98.67 100.00 8.52e-44 . . . . 25070 1 97 no PDB 2L0F . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 (P692a Mutant) In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 98 no PDB 2L0T . "Solution Structure Of The Complex Of Ubiquitin And The Vhs Domain Of Stam2" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 99 no PDB 2L3Z . "Proton-Detected 4d Dream Solid-State Nmr Structure Of Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 100 no PDB 2LD9 . "Backbone Structure Of Ubiquitin Determined Using Backbone Amide Noes And Backbone N-H And N-C Rdcs" . . . . . 96.20 77 100.00 100.00 9.24e-46 . . . . 25070 1 101 no PDB 2LJ5 . "Description Of The Structural Fluctuations Of Proteins From Structure- Based Calculations Of Residual Dipolar Couplings" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 102 no PDB 2LVO . "Structure Of The Gp78cue Domain Bound To Monubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 103 no PDB 2LVP . "Gp78cue Domain Bound To The Distal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 104 no PDB 2LVQ . "Gp78cue Domain Bound To The Proximal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 105 no PDB 2LZ6 . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 106 no PDB 2MBB . "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" . . . . . 98.73 78 100.00 100.00 9.93e-48 . . . . 25070 1 107 no PDB 2MBH . "Nmr Structure Of Eklf(22-40)/ubiquitin Complex" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 108 no PDB 2MBO . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 0 Mm Nacl" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 109 no PDB 2MBQ . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 150 Mm Nacl" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 110 no PDB 2MCN . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 111 no PDB 2MJ5 . "Structure Of The Uba Domain Of Human Nbr1 In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 112 no PDB 2MJB . "Solution Nmr Structure Of Ubiquitin Refined Against Dipolar Couplings In 4 Media" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 113 no PDB 2MOR . "A Tensor-free Method For The Structural And Dynamical Refinement Of Proteins Using Residual Dipolar Couplings" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 114 no PDB 2MRE . "Nmr Structure Of The Rad18-ubz/ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 1.50e-48 . . . . 25070 1 115 no PDB 2MRO . "Structure Of The Complex Of Ubiquitin And The Uba Domain From Dna- Damage-inducible 1 Protein (ddi1)" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 116 no PDB 2MSG . "Solid-state Nmr Structure Of Ubiquitin" . . . . . 91.14 72 100.00 100.00 8.35e-43 . . . . 25070 1 117 no PDB 2MUR . "Solution Structure Of The Human Faap20 Ubz-ubiquitin Complex" . . . . . 98.73 78 100.00 100.00 9.93e-48 . . . . 25070 1 118 no PDB 2MWS . "Structure Of The Complex Of Ubiquitin And The Ubiquitin-like (ubl) Domain Of Ddi1" . . . . . 96.20 76 98.68 98.68 4.96e-45 . . . . 25070 1 119 no PDB 2N2K . "Ensemble Structure Of The Closed State Of Lys63-linked Diubiquitin In The Absence Of A Ligand" . . . . . 89.87 71 100.00 100.00 6.28e-42 . . . . 25070 1 120 no PDB 2NR2 . "The Mumo (Minimal Under-Restraining Minimal Over- Restraining) Method For The Determination Of Native States Ensembles Of Prote" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 121 no PDB 2O6V . "Crystal Structure And Solution Nmr Studies Of Lys48-Linked Tetraubiquitin At Neutral Ph" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 122 no PDB 2OJR . "Structure Of Ubiquitin Solved By Sad Using The Lanthanide- Binding Tag" . . . . . 96.20 111 100.00 100.00 2.98e-45 . . . . 25070 1 123 no PDB 2OOB . "Crystal Structure Of The Uba Domain From Cbl-B Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 124 no PDB 2PE9 . "Nmr Based Structure Of The Open Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Tenso" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 125 no PDB 2PEA . "Nmr Based Structure Of The Closed Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Ten" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 126 no PDB 2QHO . "Crystal Structure Of The Uba Domain From Edd Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 127 no PDB 2RR9 . "The Solution Structure Of The K63-Ub2:tuims Complex" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 128 no PDB 2RSU . "Alternative Structure Of Ubiquitin" . . . . . 96.20 76 98.68 98.68 3.70e-45 . . . . 25070 1 129 no PDB 2RU6 . "The Pure Alternative State Of Ubiquitin" . . . . . 96.20 76 98.68 98.68 3.70e-45 . . . . 25070 1 130 no PDB 2W9N . "Crystal Structure Of Linear Di-Ubiquitin" . . . . . 94.94 152 100.00 100.00 6.70e-44 . . . . 25070 1 131 no PDB 2WDT . "Crystal Structure Of Plasmodium Falciparum Uchl3 In Complex With The Suicide Inhibitor Ubvme" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 132 no PDB 2WWZ . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P212121" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 133 no PDB 2WX0 . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P21" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 134 no PDB 2WX1 . "Tab2 Nzf Domain In Complex With Lys63-Linked Tri-Ubiquitin, P212121" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 135 no PDB 2XBB . "Nedd4 Hect:ub Complex" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 136 no PDB 2XEW . "Crystal Structure Of K11-Linked Diubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 137 no PDB 2XK5 . "Crystal Structure Of K6-Linked Diubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 138 no PDB 2Y5B . "Structure Of Usp21 In Complex With Linear Diubiquitin-Aldehyde" . . . . . 94.94 152 100.00 100.00 4.73e-44 . . . . 25070 1 139 no PDB 2Z59 . "Complex Structures Of Mouse Rpn13 (22-130aa) And Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 140 no PDB 2ZCB . "Crystal Structure Of Ubiquitin P37aP38A" . . . . . 96.20 76 97.37 97.37 3.92e-44 . . . . 25070 1 141 no PDB 2ZCC . "Ubiquitin Crystallized Under High Pressure" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 142 no PDB 2ZNV . "Crystal Structure Of Human Amsh-Lp Dub Domain In Complex With Lys63-Linked Ubiquitin Dimer" . . . . . 96.20 77 100.00 100.00 9.04e-46 . . . . 25070 1 143 no PDB 2ZVN . "Nemo Cozi Domain Incomplex With Diubiquitin In P212121 Space Group" . . . . . 96.20 154 100.00 100.00 6.98e-45 . . . . 25070 1 144 no PDB 2ZVO . "Nemo Cozi Domain In Complex With Diubiquitin In C2 Space Group" . . . . . 96.20 154 100.00 100.00 6.98e-45 . . . . 25070 1 145 no PDB 3A1Q . "Crystal Structure Of The Mouse Rap80 Uims In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 96.20 77 100.00 100.00 9.04e-46 . . . . 25070 1 146 no PDB 3A33 . "Ubch5b~ubiquitin Conjugate" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 147 no PDB 3A9J . "Crystal Structure Of The Mouse Tab2-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 96.20 77 100.00 100.00 9.04e-46 . . . . 25070 1 148 no PDB 3A9K . "Crystal Structure Of The Mouse Tab3-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 96.20 77 100.00 100.00 9.04e-46 . . . . 25070 1 149 no PDB 3AI5 . "Crystal Structure Of Yeast Enhanced Green Fluorescent Protein- Ubiquitin Fusion Protein" . . . . . 93.67 307 100.00 100.00 1.95e-41 . . . . 25070 1 150 no PDB 3ALB . "Cyclic Lys48-Linked Tetraubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 151 no PDB 3AUL . "Crystal Structure Of Wild-Type Lys48-Linked Diubiquitin In An Open Conformation" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 152 no PDB 3AXC . "Crystal Structure Of Linear Diubiquitin" . . . . . 96.20 154 100.00 100.00 6.98e-45 . . . . 25070 1 153 no PDB 3B08 . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 96.20 152 100.00 100.00 6.87e-45 . . . . 25070 1 154 no PDB 3B0A . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 96.20 152 100.00 100.00 6.87e-45 . . . . 25070 1 155 no PDB 3BY4 . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 156 no PDB 3C0R . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 157 no PDB 3DVG . "Crystal Structure Of K63-Specific Fab Apu.3a8 Bound To K63-Linked Di- Ubiquitin" . . . . . 100.00 80 100.00 100.00 1.88e-48 . . . . 25070 1 158 no PDB 3DVN . "Crystal Structure Of K63-specific Fab Apu2.16 Bound To K63-linked Di- Ubiquitin" . . . . . 100.00 80 100.00 100.00 1.88e-48 . . . . 25070 1 159 no PDB 3EEC . "X-Ray Structure Of Human Ubiquitin Cd(Ii) Adduct" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 160 no PDB 3EFU . "X-Ray Structure Of Human Ubiquitin-Hg(Ii) Adduct" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 161 no PDB 3EHV . "X-Ray Structure Of Human Ubiquitin Zn(Ii) Adduct" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 162 no PDB 3H1U . "Structure Of Ubiquitin In Complex With Cd Ions" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 163 no PDB 3H7P . "Crystal Structure Of K63-Linked Di-Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 164 no PDB 3H7S . "Crystal Structures Of K63-Linked Di- And Tri-Ubiquitin Reveal A Highly Extended Chain Architecture" . . . . . 96.20 76 98.68 98.68 3.31e-43 . . . . 25070 1 165 no PDB 3HM3 . "The Structure And Conformation Of Lys-63 Linked Tetra-Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 166 no PDB 3I3T . "Crystal Structure Of Covalent Ubiquitin-usp21 Complex" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 167 no PDB 3IFW . "Crystal Structure Of The S18y Variant Of Ubiquitin Carboxy T Hydrolase L1 Bound To Ubiquitin Vinylmethylester." . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 168 no PDB 3IHP . "Covalent Ubiquitin-Usp5 Complex" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 169 no PDB 3JSV . "Crystal Structure Of Mouse Nemo Cozi In Complex With Lys63- Linked Di-Ubiquitin" . . . . . 96.20 77 100.00 100.00 9.04e-46 . . . . 25070 1 170 no PDB 3JVZ . E2~ubiquitin-Hect . . . . . 100.00 81 97.47 97.47 1.49e-46 . . . . 25070 1 171 no PDB 3JW0 . E2~ubiquitin-Hect . . . . . 100.00 81 97.47 97.47 1.49e-46 . . . . 25070 1 172 no PDB 3K9O . "The Crystal Structure Of E2-25k And Ubb+1 Complex" . . . . . 94.94 96 100.00 100.00 1.71e-44 . . . . 25070 1 173 no PDB 3K9P . "The Crystal Structure Of E2-25k And Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 1.50e-48 . . . . 25070 1 174 no PDB 3KVF . "Crystal Structure Of The I93m Mutant Of Ubiquitin Carboxy Te Hydrolase L1 Bound To Ubiquitin Vinylmethylester" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 175 no PDB 3KW5 . "Crystal Structure Of Ubiquitin Carboxy Terminal Hydrolase L1 Ubiquitin Vinylmethylester" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 176 no PDB 3LDZ . "Crystal Structure Of Human Stam1 Vhs Domain In Complex With Ubiquitin" . . . . . 92.41 73 100.00 100.00 2.15e-43 . . . . 25070 1 177 no PDB 3M3J . "A New Crystal Form Of Lys48-Linked Diubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 178 no PDB 3MHS . "Structure Of The Saga Ubp8SGF11SUS1SGF73 DUB MODULE BOUND Ubiquitin Aldehyde" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 179 no PDB 3MTN . "Usp21 In Complex With A Ubiquitin-based, Usp21-specific Inhibitor" . . . . . 88.61 85 98.57 98.57 2.48e-40 . . . . 25070 1 180 no PDB 3N30 . "Crystal Structure Of Cubic Zn3-Hub (Human Ubiquitin) Adduct" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 181 no PDB 3N32 . "The Crystal Structure Of Human Ubiquitin Adduct With Zeise's Salt" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 182 no PDB 3NHE . "High Resolution Structure (1.26a) Of Usp2a In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 183 no PDB 3NOB . "Structure Of K11-linked Di-ubiquitin" . . . . . 98.73 78 100.00 100.00 9.93e-48 . . . . 25070 1 184 no PDB 3NS8 . "Crystal Structure Of An Open Conformation Of Lys48-Linked Diubiquitin At Ph 7.5" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 185 no PDB 3O65 . "Crystal Structure Of A Josephin-Ubiquitin Complex: Evolutionary Restraints On Ataxin-3 Deubiquitinating Activity" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 186 no PDB 3OFI . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 187 no PDB 3OJ3 . "Crystal Structure Of The A20 Znf4 And Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 1.50e-48 . . . . 25070 1 188 no PDB 3OJ4 . "Crystal Structure Of The A20 Znf4, Ubiquitin And Ubch5a Complex" . . . . . 100.00 79 100.00 100.00 1.50e-48 . . . . 25070 1 189 no PDB 3ONS . "Crystal Structure Of Human Ubiquitin In A New Crystal Form" . . . . . 91.14 72 100.00 100.00 8.35e-43 . . . . 25070 1 190 no PDB 3PHD . "Crystal Structure Of Human Hdac6 In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 191 no PDB 3PHW . "Otu Domain Of Crimean Congo Hemorrhagic Fever Virus In Complex With Ubiquitin" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 192 no PDB 3PRM . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 193 no PDB 3PRP . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 194 no PDB 3PT2 . "Structure Of A Viral Otu Domain Protease Bound To Ubiquitin" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 195 no PDB 3PTF . "X-Ray Structure Of The Non-Covalent Complex Between Ubch5a And Ubiquitin" . . . . . 100.00 79 100.00 100.00 1.50e-48 . . . . 25070 1 196 no PDB 3Q3F . "Engineering Domain-Swapped Binding Interfaces By Mutually Exclusive Folding: Insertion Of Ubiquitin Into Position 103 Of Barnas" . . . . . 94.94 189 100.00 100.00 6.11e-44 . . . . 25070 1 197 no PDB 3RUL . "New Strategy To Analyze Structures Of Glycopeptide-Target Complexes" . . . . . 94.94 79 100.00 100.00 5.05e-45 . . . . 25070 1 198 no PDB 3TBL . "Structure Of Mono-ubiquitinated Pcna: Implications For Dna Polymerase Switching And Okazaki Fragment Maturation" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 199 no PDB 3TMP . "The Catalytic Domain Of Human Deubiquitinase Duba In Complex With Ubiquitin Aldehyde" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 200 no PDB 3U30 . "Crystal Structure Of A Linear-Specific Ubiquitin Fab Bound To Linear Ubiquitin" . . . . . 96.20 172 100.00 100.00 9.87e-45 . . . . 25070 1 201 no PDB 3UGB . "Ubch5c~ubiquitin Conjugate" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 202 no PDB 3VDZ . "Tailoring Encodable Lanthanide-Binding Tags As Mri Contrast Agents: Xq-Dse3-Ubiquitin At 2.4 Angstroms" . . . . . 96.20 111 100.00 100.00 1.45e-45 . . . . 25070 1 203 no PDB 3VFK . "The Structure Of Monodechloro-teicoplanin In Complex With Its Ligand, Using Ubiquitin As A Ligand Carrier" . . . . . 94.94 79 100.00 100.00 5.05e-45 . . . . 25070 1 204 no PDB 3VHT . "Crystal Structure Of Gfp-Wrnip1 Ubz Domain Fusion Protein In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 205 no PDB 3VUW . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form I" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 206 no PDB 3VUX . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form Ii" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 207 no PDB 3VUY . "Crystal Structure Of A20 Zf7 In Complex With Linear Tetraubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 208 no PDB 3WWQ . "Crystal Structure Of Faap20 Ubz Domain In Complex With Lys63-linked Diubiquitin" . . . . . 96.20 77 100.00 100.00 9.04e-46 . . . . 25070 1 209 no PDB 3WXE . "Crystal Structure Of Cyld Usp Domain (c596s) In Complex With Met1- Linked Diubiquitin" . . . . . 91.14 148 100.00 100.00 8.91e-42 . . . . 25070 1 210 no PDB 3WXF . "Crystal Structure Of Cyld Usp Domain (c596s E674q) In Complex With Met1-linked Diubiquitin" . . . . . 91.14 148 100.00 100.00 8.91e-42 . . . . 25070 1 211 no PDB 3WXG . "Crystal Structure Of Cyld Usp Domain (c596a) In Complex With Lys63- Linked Diubiquitin" . . . . . 91.14 72 100.00 100.00 8.35e-43 . . . . 25070 1 212 no PDB 3ZLZ . "Lys6-linked Tri-ubiquitin" . . . . . 96.20 76 98.68 100.00 1.90e-45 . . . . 25070 1 213 no PDB 3ZNH . "Crimean Congo Hemorrhagic Fever Virus Otu Domain In Complex With Ubiquitin-propargyl." . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 214 no PDB 3ZNI . "Structure Of Phosphotyr363-cbl-b - Ubch5b-ub - Zap-70 Peptide Complex" . . . . . 100.00 81 97.47 97.47 1.49e-46 . . . . 25070 1 215 no PDB 3ZNZ . "Crystal Structure Of Otulin Otu Domain (c129a) In Complex With Met1-di Ubiquitin" . . . . . 96.20 152 100.00 100.00 6.87e-45 . . . . 25070 1 216 no PDB 4A18 . "T.Thermophila 60s Ribosomal Subunit In Complex With Initiation Factor 6. This File Contains 26s Rrna And Proteins Of Molecule 1" . . . . . 96.20 129 97.37 98.68 2.24e-44 . . . . 25070 1 217 no PDB 4A19 . "T.Thermophila 60s Ribosomal Subunit In Complex With Initiation Factor 6. This File Contains 26s Rrna And Proteins Of Molecule 2" . . . . . 96.20 129 97.37 98.68 2.24e-44 . . . . 25070 1 218 no PDB 4A1B . "T.Thermophila 60s Ribosomal Subunit In Complex With Initiation Factor 6. This File Contains 26s Rrna And Proteins Of Molecule 3" . . . . . 96.20 129 97.37 98.68 2.24e-44 . . . . 25070 1 219 no PDB 4A1D . "T.Thermophila 60s Ribosomal Subunit In Complex With Initiation Factor 6. This File Contains 26s Rrna And Proteins Of Molecule 4" . . . . . 96.20 129 97.37 98.68 2.24e-44 . . . . 25070 1 220 no PDB 4ADX . "The Cryo-em Structure Of The Archaeal 50s Ribosomal Subunit In Complex With Initiation Factor 6" . . . . . 96.20 129 97.37 98.68 2.24e-44 . . . . 25070 1 221 no PDB 4AP4 . "Rnf4 - Ubch5a - Ubiquitin Heterotrimeric Complex" . . . . . 96.20 80 100.00 100.00 7.73e-46 . . . . 25070 1 222 no PDB 4AUQ . "Structure Of Birc7-Ubch5b-Ub Complex." . . . . . 100.00 81 97.47 97.47 1.49e-46 . . . . 25070 1 223 no PDB 4BBN . "Nedd4 Hect-ub:ub Complex" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 224 no PDB 4BOS . "Structure Of Otud2 Otu Domain In Complex With Ubiquitin K11- Linked Peptide" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 225 no PDB 4BOZ . "Structure Of Otud2 Otu Domain In Complex With K11-linked Di Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 226 no PDB 4BVU . "Structure Of Shigella Effector Ospg In Complex With Host Ubch5c-ubiquitin Conjugate" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 227 no PDB 4CXC . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 228 no PDB 4CXD . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 229 no PDB 4D5L . "Cryo-em Structures Of Ribosomal 80s Complexes With Termination Factors And Cricket Paralysis Virus Ires Reveal The Ires In The " . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 230 no PDB 4D61 . "Cryo-em Structures Of Ribosomal 80s Complexes With Termination Factors And Cricket Paralysis Virus Ires Reveal The Ires In The " . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 231 no PDB 4DDG . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 232 no PDB 4DDI . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 233 no PDB 4DHJ . "The Structure Of A Ceotub1 Ubiquitin Aldehyde Ubc13~ub Complex" . . . . . 94.94 76 100.00 100.00 4.50e-45 . . . . 25070 1 234 no PDB 4DHZ . "The Structure Of HCEOTUB1-Ubiquitin Aldehyde-Ubc13~ub" . . . . . 94.94 76 100.00 100.00 4.50e-45 . . . . 25070 1 235 no PDB 4FJV . "Crystal Structure Of Human Otubain2 And Ubiquitin Complex" . . . . . 98.73 86 98.72 100.00 3.94e-47 . . . . 25070 1 236 no PDB 4HXD . "Diversity Of Ubiquitin And Isg15 Specificity Amongst Nairoviruses Viral Ovarian Tumor Domain Proteases" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 237 no PDB 4I6N . "Crystal Structure Of Trichinella Spiralis Uch37 Catalytic Domain Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 93.67 75 100.00 100.00 4.64e-44 . . . . 25070 1 238 no PDB 4IG7 . "Crystal Structure Of Trichinella Spiralis Uch37 Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 239 no PDB 4IUM . "Equine Arteritis Virus Papain-like Protease 2 (plp2) Covalently Bound To Ubiquitin" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 240 no PDB 4JIO . "Bro1 V Domain And Ubiquitin" . . . . . 96.20 76 98.68 98.68 4.86e-45 . . . . 25070 1 241 no PDB 4JQW . "Crystal Structure Of A Complex Of Nod1 Card And Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 242 no PDB 4K1R . "Crystal Structure Of Schizosaccharomyces Pombe Sst2 Catalytic Domain And Ubiquitin" . . . . . 96.20 81 100.00 100.00 1.24e-45 . . . . 25070 1 243 no PDB 4K7S . "Crystal Structure Of Zn2-hub (human Ubiquitin) Adduct From A Solution 35 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 244 no PDB 4K7U . "Crystal Structure Of Zn2.3-hub (human Ubiquitin) Adduct From A Solution 70 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 245 no PDB 4K7W . "Crystal Structure Of Zn3-hub(human Ubiquitin) Adduct From A Solution 100 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 246 no PDB 4KSK . "Gumby/fam105b In Complex With Ubiquitin" . . . . . 96.20 80 100.00 100.00 7.73e-46 . . . . 25070 1 247 no PDB 4KSL . "Gumby/fam105b In Complex With Linear Di-ubiquitin" . . . . . 96.20 156 100.00 100.00 7.39e-45 . . . . 25070 1 248 no PDB 4KZX . "Rabbit 40s Ribosomal Subunit In Complex With Eif1." . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 249 no PDB 4KZY . "Rabbit 40s Ribosomal Subunit In Complex With Eif1 And Eif1a." . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 250 no PDB 4KZZ . "Rabbit 40s Ribosomal Subunit In Complex With Mrna, Initiator Trna And Eif1a" . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 251 no PDB 4LCD . "Structure Of An Rsp5xubxsna3 Complex: Mechanism Of Ubiquitin Ligation And Lysine Prioritization By A Hect E3" . . . . . 94.94 83 100.00 100.00 2.44e-45 . . . . 25070 1 252 no PDB 4LDT . "The Structure Of H/ceotub1-ubiquitin Aldehyde-ubch5b~ub" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 253 no PDB 4LJO . "Structure Of An Active Ligase (hoip)/ubiquitin Transfer Complex" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 254 no PDB 4LJP . "Structure Of An Active Ligase (hoip-h889a)/ubiquitin Transfer Complex" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 255 no PDB 4M0W . "Crystal Structure Of Sars-cov Papain-like Protease C112s Mutant In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 256 no PDB 4MDK . "Cdc34-ubiquitin-cc0651 Complex" . . . . . 96.20 80 100.00 100.00 7.73e-46 . . . . 25070 1 257 no PDB 4MM3 . "Crystal Structure Of Sars-cov Papain-like Protease Plpro In Complex With Ubiquitin Aldehyde" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 258 no PDB 4MSM . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 E286a Mutant Bound To Ubiquitin" . . . . . 96.20 81 100.00 100.00 1.24e-45 . . . . 25070 1 259 no PDB 4MSQ . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 Catalytic Domain Bound To Ubiquitin" . . . . . 96.20 81 100.00 100.00 1.24e-45 . . . . 25070 1 260 no PDB 4NQK . "Structure Of An Ubiquitin Complex" . . . . . 100.00 79 97.47 97.47 4.46e-46 . . . . 25070 1 261 no PDB 4NQL . "The Crystal Structure Of The Dub Domain Of Amsh Orthologue, Sst2 From S. Pombe, In Complex With Lysine 63-linked Diubiquitin" . . . . . 96.20 77 100.00 100.00 9.04e-46 . . . . 25070 1 262 no PDB 4P4H . "Caught-in-action Signaling Complex Of Rig-i 2card Domain And Mavs Card Domain" . . . . . 100.00 79 97.47 97.47 4.46e-46 . . . . 25070 1 263 no PDB 4PIG . "Crystal Structure Of The Ubiquitin K11s Mutant" . . . . . 96.20 76 98.68 98.68 3.43e-45 . . . . 25070 1 264 no PDB 4PIH . "X-ray Crystal Structure Of The K33s Mutant Of Ubiquitin" . . . . . 96.20 76 98.68 98.68 3.43e-45 . . . . 25070 1 265 no PDB 4PIJ . "X-ray Crystal Structure Of The K11s/k63s Double Mutant Of Ubiquitin" . . . . . 94.94 75 97.33 97.33 8.63e-44 . . . . 25070 1 266 no PDB 4PQT . "Insights Into The Mechanism Of Deubiquitination By Jamm Deubiquitinases From Co-crystal Structures Of Enzyme With Substrate And" . . . . . 96.20 81 100.00 100.00 1.24e-45 . . . . 25070 1 267 no PDB 4R62 . "Structure Of Rad6~ub" . . . . . 97.47 78 98.70 98.70 6.15e-46 . . . . 25070 1 268 no PDB 4RF0 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 269 no PDB 4RF1 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 94.94 75 100.00 100.00 4.57e-45 . . . . 25070 1 270 no PDB 4S1Z . "Crystal Structure Of Trabid Nzf1 In Complex With K29 Linked Di- Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 271 no PDB 4S22 . "Crystal Structure Of K29 Linked Di-ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 272 no PDB 4UEL . "Uch-l5 In Complex With Ubiquitin-propargyl Bound To The Rpn13 Deubad Domain" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 273 no PDB 4UF6 . "Uch-l5 In Complex With Ubiquitin-propargyl Bound To An Activating Fragment Of Ino80g" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 274 no PDB 4UN2 . "Crystal Structure Of The Uba Domain Of Dsk2 In Complex With Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 275 no PDB 4UPX . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 276 no PDB 4UQ1 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 277 no PDB 4UQ4 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 278 no PDB 4UQ5 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 279 no PDB 4V3K . "Rnf38-ubch5b-ub Complex" . . . . . 100.00 81 97.47 97.47 1.49e-46 . . . . 25070 1 280 no PDB 4V3L . "Rnf38-ub-ubch5b-ub Complex" . . . . . 100.00 81 97.47 97.47 1.49e-46 . . . . 25070 1 281 no PDB 4W20 . "Structure Of The Mammalian 60s Ribosomal Subunit (this Entry Contains The Large Ribosomal Proteins)" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 282 no PDB 4W22 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 283 no PDB 4W23 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Small Ribosomal Subunit)" . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 284 no PDB 4W25 . "Structure Of The Idle Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 285 no PDB 4W27 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 286 no PDB 4W28 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Small Ribosomal Subunit)" . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 287 no PDB 4WHV . Rnf8/ubc13c87k~ub . . . . . 96.20 83 100.00 100.00 2.12e-45 . . . . 25070 1 288 no PDB 4WLR . "Crystal Structure Of Much37-hrpn13 Ctd-hub Complex" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 289 no PDB 4WUR . "The Crystal Structure Of The Mers-cov Papain-like Protease (c111s) With Human Ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 290 no PDB 4WZP . "Ser65 Phosphorylated Ubiquitin, Major Conformation" . . . . . 96.20 76 98.68 98.68 4.96e-45 . . . . 25070 1 291 no PDB 4XKL . "Crystal Structure Of Ndp52 Zf2 In Complex With Mono-ubiquitin" . . . . . 96.20 80 100.00 100.00 1.22e-45 . . . . 25070 1 292 no PDB 4XOF . "Observing The Overall Rocking Motion Of A Protein In A Crystal - Orthorhombic Ubiquitin Crystals Without Zinc." . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 293 no PDB 4XOK . "Observing The Overall Rocking Motion Of A Protein In A Crystal." . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 294 no PDB 4XOL . "Observing The Overall Rocking Motion Of A Protein In A Crystal - Cubic Ubiquitin Crystals." . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 295 no PDB 4XYZ . "Crystal Structure Of K33 Linked Di-ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 296 no PDB 4Y1H . "Crystal Structure Of K33 Linked Tri-ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 297 no PDB 4Z9S . "Non-covalent Assembly Of Monoubiquitin That Mimics K11 Poly-ubiquitin" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 298 no PDB 4ZFR . "Catalytic Domain Of Sst2 F403a Mutant Bound To Ubiquitin" . . . . . 96.20 81 100.00 100.00 1.24e-45 . . . . 25070 1 299 no PDB 4ZFT . "Catalytic Domain Of Sst2 F403w Mutant Bound To Ubiquitin" . . . . . 96.20 81 100.00 100.00 1.24e-45 . . . . 25070 1 300 no PDB 4ZPZ . "Crystal Structure Of Semi-synthetic Ubiquitin With Phospho-ser65 And Ala46cys" . . . . . 96.20 76 97.37 97.37 1.93e-44 . . . . 25070 1 301 no PDB 5A5B . "Structure Of The 26s Proteasome-ubp6 Complex" . . . . . 94.94 76 100.00 100.00 4.70e-45 . . . . 25070 1 302 no PDB 5AF4 . "Structure Of Lys33-linked Diub" . . . . . 96.20 76 98.68 100.00 1.90e-45 . . . . 25070 1 303 no PDB 5AF5 . "Structure Of Lys33-linked Triub S.g. P 212121" . . . . . 92.41 73 98.63 100.00 4.92e-43 . . . . 25070 1 304 no PDB 5AF6 . "Structure Of Lys33-linked Diub Bound To Trabid Nzf1" . . . . . 96.20 76 98.68 100.00 1.90e-45 . . . . 25070 1 305 no PDB 5AIT . "A Complex Of Of Rnf4-ring Domain, Ubev2, Ubc13-ub (isopeptide Crosslink)" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 306 no PDB 5AIU . "A Complex Of Rnf4-ring Domain, Ubc13-ub (isopeptide Crosslink)" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 307 no PDB 5CAW . "Structure Of Pediculus Humanus Parkin Bound To Phospho-ubiquitin" . . . . . 94.94 76 98.67 98.67 3.02e-44 . . . . 25070 1 308 no DBJ BAA03983 . "polyubiquitin [Rattus norvegicus]" . . . . . 96.20 305 100.00 100.00 3.71e-43 . . . . 25070 1 309 no DBJ BAA09860 . "polyubiquitin [Homo sapiens]" . . . . . 96.20 611 98.68 98.68 2.06e-40 . . . . 25070 1 310 no DBJ BAA11842 . "ubiquitin [Cavia porcellus]" . . . . . 96.20 311 100.00 100.00 4.20e-43 . . . . 25070 1 311 no DBJ BAA11843 . "ubiquitin extention protein [Cavia porcellus]" . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 312 no DBJ BAA23486 . "polyubiquitin [Homo sapiens]" . . . . . 96.20 609 98.68 98.68 9.03e-41 . . . . 25070 1 313 no EMBL CAA26488 . "unnamed protein product [Gallus gallus]" . . . . . 96.20 157 98.68 98.68 4.04e-44 . . . . 25070 1 314 no EMBL CAA28495 . "ubiquitin [Homo sapiens]" . . . . . 96.20 229 100.00 100.00 6.59e-44 . . . . 25070 1 315 no EMBL CAA30183 . "unnamed protein product [Dictyostelium discoideum]" . . . . . 96.20 128 97.37 97.37 1.04e-43 . . . . 25070 1 316 no EMBL CAA30815 . "unnamed protein product [Cricetulus sp.]" . . . . . 89.87 223 100.00 100.00 5.62e-40 . . . . 25070 1 317 no EMBL CAA33466 . "unnamed protein product [Chlamydomonas reinhardtii]" . . . . . 96.20 128 97.37 98.68 2.15e-44 . . . . 25070 1 318 no GB AAA02769 . "polyprotein [Bovine viral diarrhea virus 1-Osloss]" . . . . . 94.94 3975 97.33 100.00 3.16e-39 . . . . 25070 1 319 no GB AAA28154 . "polyubiquitin [Caenorhabditis elegans]" . . . . . 96.20 838 97.37 98.68 1.34e-39 . . . . 25070 1 320 no GB AAA28997 . "ubiquitin [Drosophila melanogaster]" . . . . . 96.20 231 100.00 100.00 5.31e-44 . . . . 25070 1 321 no GB AAA28998 . "ubiquitin-hybrid protein precursor [Drosophila melanogaster]" . . . . . 96.20 156 100.00 100.00 1.62e-45 . . . . 25070 1 322 no GB AAA28999 . "ubiquitin, partial [Drosophila melanogaster]" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 323 no PIR I50437 . "polyubiquitin 4 - chicken [Gallus gallus]" . . . . . 96.20 305 100.00 100.00 3.71e-43 . . . . 25070 1 324 no PIR I51568 . "polyubiquitin - African clawed frog (fragment)" . . . . . 96.20 167 100.00 100.00 9.74e-45 . . . . 25070 1 325 no PIR I65237 . "ubiquitin / ribosomal protein L40, cytosolic [validated] - rat" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 326 no PIR JN0790 . "ubiquitin/ribosomal protein CEP52 fusion protein - Leishmania major" . . . . . 96.20 128 97.37 98.68 4.22e-45 . . . . 25070 1 327 no PIR S13928 . "ubiquitin precursor - chicken [Gallus gallus]" . . . . . 96.20 229 100.00 100.00 5.49e-44 . . . . 25070 1 328 no PRF 0412265A . ubiquitin . . . . . 94.94 75 98.67 98.67 1.78e-44 . . . . 25070 1 329 no PRF 1212243A . "ubiquitin S1" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 330 no PRF 1212243B . "ubiquitin S5" . . . . . 88.61 77 98.57 98.57 1.19e-40 . . . . 25070 1 331 no PRF 1212243C . "ubiquitin S3" . . . . . 96.20 76 100.00 100.00 6.92e-46 . . . . 25070 1 332 no PRF 1212243D . "ubiquitin S2" . . . . . 88.61 77 98.57 98.57 1.38e-40 . . . . 25070 1 333 no REF NP_001005123 . "ubiquitin-60S ribosomal protein L40 [Xenopus (Silurana) tropicalis]" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 334 no REF NP_001006688 . "ubiquitin C [Xenopus (Silurana) tropicalis]" . . . . . 96.20 609 100.00 100.00 1.57e-41 . . . . 25070 1 335 no REF NP_001009117 . "polyubiquitin-B [Pan troglodytes]" . . . . . 96.20 229 100.00 100.00 6.59e-44 . . . . 25070 1 336 no REF NP_001009202 . "polyubiquitin-B [Ovis aries]" . . . . . 96.20 305 98.68 100.00 7.10e-43 . . . . 25070 1 337 no REF NP_001009286 . "ubiquitin-60S ribosomal protein L40 [Ovis aries]" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 338 no SP P0C273 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 339 no SP P0C275 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 340 no SP P0C276 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 1 341 no SP P0CG47 . "RecName: Full=Polyubiquitin-B; Contains: RecName: Full=Ubiquitin; Flags: Precursor" . . . . . 96.20 229 100.00 100.00 6.59e-44 . . . . 25070 1 342 no SP P0CG48 . "RecName: Full=Polyubiquitin-C; Contains: RecName: Full=Ubiquitin; Flags: Precursor" . . . . . 96.20 685 100.00 100.00 2.33e-41 . . . . 25070 1 343 no TPD FAA00319 . "TPA: polyubiquitin [Cryptococcus neoformans var. neoformans B-3501A]" . . . . . 96.20 456 97.37 98.68 1.46e-40 . . . . 25070 1 344 no TPE CEL68433 . "TPA: ubiquitin / ribosomal protein CEP52 fusion protein, putative [Neospora caninum Liverpool]" . . . . . 96.20 129 98.68 100.00 1.95e-45 . . . . 25070 1 345 no TPE CEL70397 . "TPA: Ubiquitin, related [Neospora caninum Liverpool]" . . . . . 96.20 535 98.68 100.00 3.65e-41 . . . . 25070 1 346 no TPE CEL75964 . "TPA: ubiquitin / ribosomal protein CEP52 fusion protein, putative [Toxoplasma gondii VEG]" . . . . . 96.20 129 98.68 100.00 1.95e-45 . . . . 25070 1 347 no TPE CEL78064 . "TPA: polyubiquitin, putative [Toxoplasma gondii VEG]" . . . . . 96.20 307 98.68 100.00 1.39e-42 . . . . 25070 1 348 no TPG DAA18802 . "TPA: polyubiquitin [Bos taurus]" . . . . . 96.20 305 100.00 100.00 4.04e-43 . . . . 25070 1 349 no TPG DAA20663 . "TPA: ubiquitin C [Bos taurus]" . . . . . 94.94 314 98.67 100.00 1.24e-41 . . . . 25070 1 350 no TPG DAA20672 . "TPA: ubiquitin B-like [Bos taurus]" . . . . . 96.20 77 98.68 98.68 5.88e-45 . . . . 25070 1 351 no TPG DAA24675 . "TPA: 40S ribosomal protein S27a [Bos taurus]" . . . . . 96.20 156 100.00 100.00 1.02e-45 . . . . 25070 1 352 no TPG DAA28295 . "TPA: ubiquitin and ribosomal protein L40 [Bos taurus]" . . . . . 96.20 128 100.00 100.00 5.79e-46 . . . . 25070 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 -2 GLY . 25070 1 2 -1 SER . 25070 1 3 0 HIS . 25070 1 4 1 MET . 25070 1 5 2 GLN . 25070 1 6 3 ILE . 25070 1 7 4 PHE . 25070 1 8 5 VAL . 25070 1 9 6 LYS . 25070 1 10 7 THR . 25070 1 11 8 LEU . 25070 1 12 9 THR . 25070 1 13 10 GLY . 25070 1 14 11 LYS . 25070 1 15 12 THR . 25070 1 16 13 ILE . 25070 1 17 14 THR . 25070 1 18 15 LEU . 25070 1 19 16 GLU . 25070 1 20 17 VAL . 25070 1 21 18 GLU . 25070 1 22 19 PRO . 25070 1 23 20 SER . 25070 1 24 21 ASP . 25070 1 25 22 THR . 25070 1 26 23 ILE . 25070 1 27 24 GLU . 25070 1 28 25 ASN . 25070 1 29 26 VAL . 25070 1 30 27 LYS . 25070 1 31 28 ALA . 25070 1 32 29 LYS . 25070 1 33 30 ILE . 25070 1 34 31 GLN . 25070 1 35 32 ASP . 25070 1 36 33 LYS . 25070 1 37 34 GLU . 25070 1 38 35 GLY . 25070 1 39 36 ILE . 25070 1 40 37 PRO . 25070 1 41 38 PRO . 25070 1 42 39 ASP . 25070 1 43 40 GLN . 25070 1 44 41 GLN . 25070 1 45 42 ARG . 25070 1 46 43 LEU . 25070 1 47 44 ILE . 25070 1 48 45 PHE . 25070 1 49 46 ALA . 25070 1 50 47 GLY . 25070 1 51 48 LYS . 25070 1 52 49 GLN . 25070 1 53 50 LEU . 25070 1 54 51 GLU . 25070 1 55 52 ASP . 25070 1 56 53 GLY . 25070 1 57 54 ARG . 25070 1 58 55 THR . 25070 1 59 56 LEU . 25070 1 60 57 SER . 25070 1 61 58 ASP . 25070 1 62 59 TYR . 25070 1 63 60 ASN . 25070 1 64 61 ILE . 25070 1 65 62 GLN . 25070 1 66 63 LYS . 25070 1 67 64 GLU . 25070 1 68 65 SER . 25070 1 69 66 THR . 25070 1 70 67 LEU . 25070 1 71 68 HIS . 25070 1 72 69 LEU . 25070 1 73 70 VAL . 25070 1 74 71 LEU . 25070 1 75 72 ARG . 25070 1 76 73 LEU . 25070 1 77 74 ARG . 25070 1 78 75 GLY . 25070 1 79 76 GLY . 25070 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . GLY 1 1 25070 1 . SER 2 2 25070 1 . HIS 3 3 25070 1 . MET 4 4 25070 1 . GLN 5 5 25070 1 . ILE 6 6 25070 1 . PHE 7 7 25070 1 . VAL 8 8 25070 1 . LYS 9 9 25070 1 . THR 10 10 25070 1 . LEU 11 11 25070 1 . THR 12 12 25070 1 . GLY 13 13 25070 1 . LYS 14 14 25070 1 . THR 15 15 25070 1 . ILE 16 16 25070 1 . THR 17 17 25070 1 . LEU 18 18 25070 1 . GLU 19 19 25070 1 . VAL 20 20 25070 1 . GLU 21 21 25070 1 . PRO 22 22 25070 1 . SER 23 23 25070 1 . ASP 24 24 25070 1 . THR 25 25 25070 1 . ILE 26 26 25070 1 . GLU 27 27 25070 1 . ASN 28 28 25070 1 . VAL 29 29 25070 1 . LYS 30 30 25070 1 . ALA 31 31 25070 1 . LYS 32 32 25070 1 . ILE 33 33 25070 1 . GLN 34 34 25070 1 . ASP 35 35 25070 1 . LYS 36 36 25070 1 . GLU 37 37 25070 1 . GLY 38 38 25070 1 . ILE 39 39 25070 1 . PRO 40 40 25070 1 . PRO 41 41 25070 1 . ASP 42 42 25070 1 . GLN 43 43 25070 1 . GLN 44 44 25070 1 . ARG 45 45 25070 1 . LEU 46 46 25070 1 . ILE 47 47 25070 1 . PHE 48 48 25070 1 . ALA 49 49 25070 1 . GLY 50 50 25070 1 . LYS 51 51 25070 1 . GLN 52 52 25070 1 . LEU 53 53 25070 1 . GLU 54 54 25070 1 . ASP 55 55 25070 1 . GLY 56 56 25070 1 . ARG 57 57 25070 1 . THR 58 58 25070 1 . LEU 59 59 25070 1 . SER 60 60 25070 1 . ASP 61 61 25070 1 . TYR 62 62 25070 1 . ASN 63 63 25070 1 . ILE 64 64 25070 1 . GLN 65 65 25070 1 . LYS 66 66 25070 1 . GLU 67 67 25070 1 . SER 68 68 25070 1 . THR 69 69 25070 1 . LEU 70 70 25070 1 . HIS 71 71 25070 1 . LEU 72 72 25070 1 . VAL 73 73 25070 1 . LEU 74 74 25070 1 . ARG 75 75 25070 1 . LEU 76 76 25070 1 . ARG 77 77 25070 1 . GLY 78 78 25070 1 . GLY 79 79 25070 1 stop_ save_ save_entity_2 _Entity.Sf_category entity _Entity.Sf_framecode entity_2 _Entity.Entry_ID 25070 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name Ubiquitin-binding_zinc_finger_(UBZ)_domain_from_human_Rad18 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID B _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; GSRQVTKVDCPVCGVNIPES HINKHLDSCLSRE ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq ; G: 195 S: 196 R: 197 Q: 198 (first native residue) ; _Entity.Polymer_author_seq_details 'GSR are remnants of the thrombin cleavage tag. Q198 is the first native residue' _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 33 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all other bound' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 3628.145 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-29 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 25071 . Rad18-UBZ . . . . . 100.00 33 100.00 100.00 2.03e-14 . . . . 25070 2 2 no PDB 2MRE . "Nmr Structure Of The Rad18-ubz/ubiquitin Complex" . . . . . 100.00 33 100.00 100.00 2.03e-14 . . . . 25070 2 3 no PDB 2MRF . "Nmr Structure Of The Ubiquitin-binding Zinc Finger (ubz) Domain From Human Rad18" . . . . . 100.00 33 100.00 100.00 2.03e-14 . . . . 25070 2 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 1 195 GLY . 25070 2 2 196 SER . 25070 2 3 197 ARG . 25070 2 4 198 GLN . 25070 2 5 199 VAL . 25070 2 6 200 THR . 25070 2 7 201 LYS . 25070 2 8 202 VAL . 25070 2 9 203 ASP . 25070 2 10 204 CYS . 25070 2 11 205 PRO . 25070 2 12 206 VAL . 25070 2 13 207 CYS . 25070 2 14 208 GLY . 25070 2 15 209 VAL . 25070 2 16 210 ASN . 25070 2 17 211 ILE . 25070 2 18 212 PRO . 25070 2 19 213 GLU . 25070 2 20 214 SER . 25070 2 21 215 HIS . 25070 2 22 216 ILE . 25070 2 23 217 ASN . 25070 2 24 218 LYS . 25070 2 25 219 HIS . 25070 2 26 220 LEU . 25070 2 27 221 ASP . 25070 2 28 222 SER . 25070 2 29 223 CYS . 25070 2 30 224 LEU . 25070 2 31 225 SER . 25070 2 32 226 ARG . 25070 2 33 227 GLU . 25070 2 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . GLY 1 1 25070 2 . SER 2 2 25070 2 . ARG 3 3 25070 2 . GLN 4 4 25070 2 . VAL 5 5 25070 2 . THR 6 6 25070 2 . LYS 7 7 25070 2 . VAL 8 8 25070 2 . ASP 9 9 25070 2 . CYS 10 10 25070 2 . PRO 11 11 25070 2 . VAL 12 12 25070 2 . CYS 13 13 25070 2 . GLY 14 14 25070 2 . VAL 15 15 25070 2 . ASN 16 16 25070 2 . ILE 17 17 25070 2 . PRO 18 18 25070 2 . GLU 19 19 25070 2 . SER 20 20 25070 2 . HIS 21 21 25070 2 . ILE 22 22 25070 2 . ASN 23 23 25070 2 . LYS 24 24 25070 2 . HIS 25 25 25070 2 . LEU 26 26 25070 2 . ASP 27 27 25070 2 . SER 28 28 25070 2 . CYS 29 29 25070 2 . LEU 30 30 25070 2 . SER 31 31 25070 2 . ARG 32 32 25070 2 . GLU 33 33 25070 2 stop_ save_ save_entity_ZN _Entity.Sf_category entity _Entity.Sf_framecode entity_ZN _Entity.Entry_ID 25070 _Entity.ID 3 _Entity.BMRB_code ZN _Entity.Name 'ZINC ION' _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID ZN _Entity.Nonpolymer_comp_label $chem_comp_ZN _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components 1 _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 3 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 65.409 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'ZINC ION' BMRB 25070 3 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID 'ZINC ION' BMRB 25070 3 ZN 'Three letter code' 25070 3 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 ZN $chem_comp_ZN 25070 3 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 25070 _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 $entity_1 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 25070 1 2 2 $entity_2 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 25070 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 25070 _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 $entity_1 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli BL21(DE3) . . . . . . . . . . . . . . . pET15b . . . . . . 25070 1 2 2 $entity_2 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli BL21(DE3) . . . . . . . . . . . . . . . pGEX . . . . . . 25070 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_ZN _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_ZN _Chem_comp.Entry_ID 25070 _Chem_comp.ID ZN _Chem_comp.Provenance PDB _Chem_comp.Name 'ZINC ION' _Chem_comp.Type NON-POLYMER _Chem_comp.BMRB_code ZN _Chem_comp.PDB_code ZN _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-11-20 _Chem_comp.Modified_date 2012-11-20 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code ZN _Chem_comp.Number_atoms_all 1 _Chem_comp.Number_atoms_nh 1 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/Zn/q+2 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Zn _Chem_comp.Formula_weight 65.409 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID InChI=1S/Zn/q+2 InChI InChI 1.03 25070 ZN PTFCDOFLOPIGGS-UHFFFAOYSA-N InChIKey InChI 1.03 25070 ZN [Zn++] SMILES CACTVS 3.341 25070 ZN [Zn++] SMILES_CANONICAL CACTVS 3.341 25070 ZN [Zn+2] SMILES ACDLabs 10.04 25070 ZN [Zn+2] SMILES 'OpenEye OEToolkits' 1.5.0 25070 ZN [Zn+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 25070 ZN stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID zinc 'SYSTEMATIC NAME' ACDLabs 10.04 25070 ZN 'zinc(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 25070 ZN stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID ZN ZN ZN ZN . ZN . . N 2 . . . 0 no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 25070 ZN stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_13C-15N-UBZ_saturated_with_unlabeled_ubiquitin _Sample.Sf_category sample _Sample.Sf_framecode 13C-15N-UBZ_saturated_with_unlabeled_ubiquitin _Sample.Entry_ID 25070 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'UBZ concentrations are inexact since it has no aromatics' _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'Ubiquitin-binding zinc finger (UBZ) domain from human Rad18' '[U-13C; U-15N]' . . 1 $entity_1 . . 0.5 . . mM . . . . 25070 1 2 Ubiquitin 'natural abundance' . . 2 $entity_2 . . 5 . . mM . . . . 25070 1 3 MOPS 'natural abundance' . . . . . . 25 . . mM . . . . 25070 1 4 NaCl 'natural abundance' . . . . . . 50 . . mM . . . . 25070 1 5 ZnCl2 'natural abundance' . . 3 $entity_ZN . . 0.05 . . mM . . . . 25070 1 6 H2O 'natural abundance' . . . . . . 90 . . % . . . . 25070 1 7 D2O 'natural abundance' . . . . . . 10 . . % . . . . 25070 1 stop_ save_ save_13C-15N-ubiquitin_saturated_with_unlabeled_UBZ _Sample.Sf_category sample _Sample.Sf_framecode 13C-15N-ubiquitin_saturated_with_unlabeled_UBZ _Sample.Entry_ID 25070 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'UBZ concentrations are inexact since it has no aromatics' _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Ubiquitin '[U-13C; U-15N]' . . 1 $entity_1 . . 2 . . mM . . . . 25070 2 2 'Ubiquitin-binding zinc finger (UBZ) domain from human Rad18' 'natural abundance' . . 2 $entity_2 . . . 7 10 mM . . . . 25070 2 3 MOPS 'natural abundance' . . . . . . 25 . . mM . . . . 25070 2 4 NaCl 'natural abundance' . . . . . . 50 . . mM . . . . 25070 2 5 ZnCl2 'natural abundance' . . 3 $entity_ZN . . 0.05 . . mM . . . . 25070 2 6 H2O 'natural abundance' . . . . . . 90 . . % . . . . 25070 2 7 D2O 'natural abundance' . . . . . . 10 . . % . . . . 25070 2 stop_ save_ ####################### # Sample conditions # ####################### save_MOPS_NMR_buffer _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode MOPS_NMR_buffer _Sample_condition_list.Entry_ID 25070 _Sample_condition_list.ID 1 _Sample_condition_list.Details '25 mM MOPS, 50 mM NaCl, 0.05 mM ZnCl2, pH=6.5 before dilution to include 10% D20' 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 temperature 273 . K 25070 1 pH 6.5 . pH 25070 1 pressure 1 . atm 25070 1 'ionic strength' 125 . mM 25070 1 stop_ save_ ############################ # Computer software used # ############################ save_Analysis _Software.Sf_category software _Software.Sf_framecode Analysis _Software.Entry_ID 25070 _Software.ID 1 _Software.Name Analysis _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID CCPN . . 25070 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 25070 1 stop_ save_ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 25070 _Software.ID 2 _Software.Name CYANA _Software.Version 2.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 25070 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 25070 2 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 25070 _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' . . 25070 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 25070 3 stop_ save_ save_CNS _Software.Sf_category software _Software.Sf_framecode CNS _Software.Entry_ID 25070 _Software.ID 4 _Software.Name CNS _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Brunger, Adams, Clore, Gros, Nilges and Read' . . 25070 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'water refinement' 25070 4 stop_ save_ save_TALOS+ _Software.Sf_category software _Software.Sf_framecode TALOS+ _Software.Entry_ID 25070 _Software.ID 5 _Software.Name TALOS+ _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Cornilescu, Delaglio and Bax' . . 25070 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'dihedral angles' 25070 5 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 25070 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model VNMRS _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 25070 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model VNMRS _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 25070 _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 Varian VNMRS . 600 . . . 25070 1 2 spectrometer_2 Varian VNMRS . 800 . . . 25070 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 25070 _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 $13C-15N-UBZ_saturated_with_unlabeled_ubiquitin isotropic . . 1 $MOPS_NMR_buffer . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25070 1 2 '3D HNCO' no . . . . . . . . . . 1 $13C-15N-UBZ_saturated_with_unlabeled_ubiquitin isotropic . . 1 $MOPS_NMR_buffer . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25070 1 3 '3D HNCACB' no . . . . . . . . . . 1 $13C-15N-UBZ_saturated_with_unlabeled_ubiquitin isotropic . . 1 $MOPS_NMR_buffer . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25070 1 4 '3D HBHA(CO)NH' no . . . . . . . . . . 1 $13C-15N-UBZ_saturated_with_unlabeled_ubiquitin isotropic . . 1 $MOPS_NMR_buffer . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25070 1 5 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $13C-15N-UBZ_saturated_with_unlabeled_ubiquitin isotropic . . 1 $MOPS_NMR_buffer . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25070 1 6 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $13C-15N-UBZ_saturated_with_unlabeled_ubiquitin isotropic . . 1 $MOPS_NMR_buffer . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25070 1 7 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $13C-15N-UBZ_saturated_with_unlabeled_ubiquitin isotropic . . 1 $MOPS_NMR_buffer . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25070 1 8 '3D 15N/13C-filtered NOESY' no . . . . . . . . . . 1 $13C-15N-UBZ_saturated_with_unlabeled_ubiquitin isotropic . . 1 $MOPS_NMR_buffer . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25070 1 9 '2D 1H-15N HSQC' no . . . . . . . . . . 2 $13C-15N-ubiquitin_saturated_with_unlabeled_UBZ isotropic . . 1 $MOPS_NMR_buffer . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25070 1 10 '3D HNCO' no . . . . . . . . . . 2 $13C-15N-ubiquitin_saturated_with_unlabeled_UBZ isotropic . . 1 $MOPS_NMR_buffer . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25070 1 11 '3D HNCACB' no . . . . . . . . . . 2 $13C-15N-ubiquitin_saturated_with_unlabeled_UBZ isotropic . . 1 $MOPS_NMR_buffer . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25070 1 12 '3D HCCH-TOCSY' no . . . . . . . . . . 2 $13C-15N-ubiquitin_saturated_with_unlabeled_UBZ isotropic . . 1 $MOPS_NMR_buffer . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25070 1 13 '3D HBHA(CO)NH' no . . . . . . . . . . 2 $13C-15N-ubiquitin_saturated_with_unlabeled_UBZ isotropic . . 1 $MOPS_NMR_buffer . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25070 1 14 '3D 1H-15N NOESY' no . . . . . . . . . . 2 $13C-15N-ubiquitin_saturated_with_unlabeled_UBZ isotropic . . 1 $MOPS_NMR_buffer . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25070 1 15 '3D 1H-13C NOESY' no . . . . . . . . . . 2 $13C-15N-ubiquitin_saturated_with_unlabeled_UBZ isotropic . . 1 $MOPS_NMR_buffer . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25070 1 16 '3D 15N/13C-filtered NOESY' no . . . . . . . . . . 2 $13C-15N-ubiquitin_saturated_with_unlabeled_UBZ isotropic . . 1 $MOPS_NMR_buffer . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25070 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 25070 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 25070 1 C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 25070 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 25070 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 25070 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $MOPS_NMR_buffer _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' . . . 25070 1 2 '3D HNCO' . . . 25070 1 3 '3D HNCACB' . . . 25070 1 4 '3D HBHA(CO)NH' . . . 25070 1 5 '3D HCCH-TOCSY' . . . 25070 1 9 '2D 1H-15N HSQC' . . . 25070 1 10 '3D HNCO' . . . 25070 1 11 '3D HNCACB' . . . 25070 1 12 '3D HCCH-TOCSY' . . . 25070 1 13 '3D HBHA(CO)NH' . . . 25070 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 1 $Analysis . . 25070 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 4 4 MET H H 1 9.144 0.04 . 1 . . . A 1 MET H . 25070 1 2 . 1 1 4 4 MET HA H 1 4.646 0.04 . 1 . . . A 1 MET HA . 25070 1 3 . 1 1 4 4 MET HB2 H 1 1.893 0.04 . 2 . . . A 1 MET HB2 . 25070 1 4 . 1 1 4 4 MET HB3 H 1 1.873 0.04 . 2 . . . A 1 MET HB3 . 25070 1 5 . 1 1 4 4 MET HG2 H 1 1.989 0.04 . 2 . . . A 1 MET HG2 . 25070 1 6 . 1 1 4 4 MET HG3 H 1 2.335 0.04 . 2 . . . A 1 MET HG3 . 25070 1 7 . 1 1 4 4 MET C C 13 172.845 0.4 . 1 . . . A 1 MET C . 25070 1 8 . 1 1 4 4 MET CA C 13 54.639 0.40 . 1 . . . A 1 MET CA . 25070 1 9 . 1 1 4 4 MET CB C 13 35.102 0.40 . 1 . . . A 1 MET CB . 25070 1 10 . 1 1 4 4 MET CG C 13 31.867 0.40 . 1 . . . A 1 MET CG . 25070 1 11 . 1 1 4 4 MET N N 15 120.065 0.40 . 1 . . . A 1 MET N . 25070 1 12 . 1 1 5 5 GLN H H 1 8.374 0.04 . 1 . . . A 2 GLN H . 25070 1 13 . 1 1 5 5 GLN HA H 1 5.363 0.04 . 1 . . . A 2 GLN HA . 25070 1 14 . 1 1 5 5 GLN HB2 H 1 1.589 0.04 . 2 . . . A 2 GLN HB2 . 25070 1 15 . 1 1 5 5 GLN HB3 H 1 1.779 0.04 . 2 . . . A 2 GLN HB3 . 25070 1 16 . 1 1 5 5 GLN HG2 H 1 2.180 0.04 . 2 . . . A 2 GLN HG2 . 25070 1 17 . 1 1 5 5 GLN HG3 H 1 1.942 0.04 . 2 . . . A 2 GLN HG3 . 25070 1 18 . 1 1 5 5 GLN HE21 H 1 7.696 0.04 . 1 . . . A 2 GLN HE21 . 25070 1 19 . 1 1 5 5 GLN HE22 H 1 6.743 0.04 . 2 . . . A 2 GLN HE22 . 25070 1 20 . 1 1 5 5 GLN C C 13 176.031 0.4 . 1 . . . A 2 GLN C . 25070 1 21 . 1 1 5 5 GLN CA C 13 54.298 0.40 . 1 . . . A 2 GLN CA . 25070 1 22 . 1 1 5 5 GLN CB C 13 30.846 0.40 . 1 . . . A 2 GLN CB . 25070 1 23 . 1 1 5 5 GLN CG C 13 34.555 0.40 . 1 . . . A 2 GLN CG . 25070 1 24 . 1 1 5 5 GLN N N 15 120.901 0.40 . 1 . . . A 2 GLN N . 25070 1 25 . 1 1 5 5 GLN NE2 N 15 111.551 0.04 . 1 . . . A 2 GLN NE2 . 25070 1 26 . 1 1 6 6 ILE H H 1 8.304 0.04 . 1 . . . A 3 ILE H . 25070 1 27 . 1 1 6 6 ILE HA H 1 4.155 0.04 . 1 . . . A 3 ILE HA . 25070 1 28 . 1 1 6 6 ILE HB H 1 1.713 0.04 . 1 . . . A 3 ILE HB . 25070 1 29 . 1 1 6 6 ILE HG12 H 1 0.790 0.04 . 2 . . . A 3 ILE HG12 . 25070 1 30 . 1 1 6 6 ILE HG13 H 1 1.026 0.04 . 2 . . . A 3 ILE HG13 . 25070 1 31 . 1 1 6 6 ILE HG21 H 1 0.598 0.04 . 1 . . . A 3 ILE HG21 . 25070 1 32 . 1 1 6 6 ILE HG22 H 1 0.598 0.04 . 1 . . . A 3 ILE HG22 . 25070 1 33 . 1 1 6 6 ILE HG23 H 1 0.598 0.04 . 1 . . . A 3 ILE HG23 . 25070 1 34 . 1 1 6 6 ILE HD11 H 1 0.556 0.04 . 1 . . . A 3 ILE HD11 . 25070 1 35 . 1 1 6 6 ILE HD12 H 1 0.556 0.04 . 1 . . . A 3 ILE HD12 . 25070 1 36 . 1 1 6 6 ILE HD13 H 1 0.556 0.04 . 1 . . . A 3 ILE HD13 . 25070 1 37 . 1 1 6 6 ILE C C 13 172.420 0.4 . 1 . . . A 3 ILE C . 25070 1 38 . 1 1 6 6 ILE CA C 13 59.485 0.40 . 1 . . . A 3 ILE CA . 25070 1 39 . 1 1 6 6 ILE CB C 13 41.975 0.40 . 1 . . . A 3 ILE CB . 25070 1 40 . 1 1 6 6 ILE CG1 C 13 24.843 0.40 . 1 . . . A 3 ILE CG1 . 25070 1 41 . 1 1 6 6 ILE CG2 C 13 17.894 0.40 . 1 . . . A 3 ILE CG2 . 25070 1 42 . 1 1 6 6 ILE CD1 C 13 14.071 0.40 . 1 . . . A 3 ILE CD1 . 25070 1 43 . 1 1 6 6 ILE N N 15 114.155 0.40 . 1 . . . A 3 ILE N . 25070 1 44 . 1 1 7 7 PHE H H 1 8.591 0.04 . 1 . . . A 4 PHE H . 25070 1 45 . 1 1 7 7 PHE HA H 1 5.491 0.04 . 1 . . . A 4 PHE HA . 25070 1 46 . 1 1 7 7 PHE HB2 H 1 2.812 0.04 . 2 . . . A 4 PHE HB2 . 25070 1 47 . 1 1 7 7 PHE HB3 H 1 3.019 0.04 . 2 . . . A 4 PHE HB3 . 25070 1 48 . 1 1 7 7 PHE C C 13 174.783 0.4 . 1 . . . A 4 PHE C . 25070 1 49 . 1 1 7 7 PHE CA C 13 55.216 0.40 . 1 . . . A 4 PHE CA . 25070 1 50 . 1 1 7 7 PHE CB C 13 41.068 0.40 . 1 . . . A 4 PHE CB . 25070 1 51 . 1 1 7 7 PHE N N 15 118.637 0.40 . 1 . . . A 4 PHE N . 25070 1 52 . 1 1 8 8 VAL H H 1 9.353 0.04 . 1 . . . A 5 VAL H . 25070 1 53 . 1 1 8 8 VAL HA H 1 4.687 0.04 . 1 . . . A 5 VAL HA . 25070 1 54 . 1 1 8 8 VAL HB H 1 1.930 0.04 . 1 . . . A 5 VAL HB . 25070 1 55 . 1 1 8 8 VAL HG11 H 1 0.700 0.04 . 1 . . . A 5 VAL HG11 . 25070 1 56 . 1 1 8 8 VAL HG12 H 1 0.700 0.04 . 1 . . . A 5 VAL HG12 . 25070 1 57 . 1 1 8 8 VAL HG13 H 1 0.700 0.04 . 1 . . . A 5 VAL HG13 . 25070 1 58 . 1 1 8 8 VAL HG21 H 1 0.675 0.04 . 1 . . . A 5 VAL HG21 . 25070 1 59 . 1 1 8 8 VAL HG22 H 1 0.675 0.04 . 1 . . . A 5 VAL HG22 . 25070 1 60 . 1 1 8 8 VAL HG23 H 1 0.675 0.04 . 1 . . . A 5 VAL HG23 . 25070 1 61 . 1 1 8 8 VAL C C 13 174.507 0.4 . 1 . . . A 5 VAL C . 25070 1 62 . 1 1 8 8 VAL CA C 13 60.687 0.40 . 1 . . . A 5 VAL CA . 25070 1 63 . 1 1 8 8 VAL CB C 13 33.524 0.40 . 1 . . . A 5 VAL CB . 25070 1 64 . 1 1 8 8 VAL CG1 C 13 20.475 0.40 . 1 . . . A 5 VAL CG1 . 25070 1 65 . 1 1 8 8 VAL CG2 C 13 22.846 0.40 . 1 . . . A 5 VAL CG2 . 25070 1 66 . 1 1 8 8 VAL N N 15 122.329 0.40 . 1 . . . A 5 VAL N . 25070 1 67 . 1 1 9 9 LYS H H 1 9.143 0.04 . 1 . . . A 6 LYS H . 25070 1 68 . 1 1 9 9 LYS HA H 1 5.447 0.04 . 1 . . . A 6 LYS HA . 25070 1 69 . 1 1 9 9 LYS HB2 H 1 1.675 0.04 . 2 . . . A 6 LYS HB2 . 25070 1 70 . 1 1 9 9 LYS HB3 H 1 1.325 0.04 . 2 . . . A 6 LYS HB3 . 25070 1 71 . 1 1 9 9 LYS HG2 H 1 1.566 0.04 . 2 . . . A 6 LYS HG2 . 25070 1 72 . 1 1 9 9 LYS HG3 H 1 1.268 0.04 . 2 . . . A 6 LYS HG3 . 25070 1 73 . 1 1 9 9 LYS HD2 H 1 1.580 0.04 . 2 . . . A 6 LYS HD2 . 25070 1 74 . 1 1 9 9 LYS HD3 H 1 1.580 0.04 . 2 . . . A 6 LYS HD3 . 25070 1 75 . 1 1 9 9 LYS HE2 H 1 2.894 0.04 . 2 . . . A 6 LYS HE2 . 25070 1 76 . 1 1 9 9 LYS HE3 H 1 2.894 0.04 . 2 . . . A 6 LYS HE3 . 25070 1 77 . 1 1 9 9 LYS C C 13 177.564 0.4 . 1 . . . A 6 LYS C . 25070 1 78 . 1 1 9 9 LYS CA C 13 54.528 0.40 . 1 . . . A 6 LYS CA . 25070 1 79 . 1 1 9 9 LYS CB C 13 35.446 0.40 . 1 . . . A 6 LYS CB . 25070 1 80 . 1 1 9 9 LYS CG C 13 25.065 0.40 . 1 . . . A 6 LYS CG . 25070 1 81 . 1 1 9 9 LYS CD C 13 29.576 0.40 . 1 . . . A 6 LYS CD . 25070 1 82 . 1 1 9 9 LYS CE C 13 42.117 0.40 . 1 . . . A 6 LYS CE . 25070 1 83 . 1 1 9 9 LYS N N 15 128.507 0.40 . 1 . . . A 6 LYS N . 25070 1 84 . 1 1 10 10 THR H H 1 8.903 0.04 . 1 . . . A 7 THR H . 25070 1 85 . 1 1 10 10 THR HA H 1 5.172 0.04 . 1 . . . A 7 THR HA . 25070 1 86 . 1 1 10 10 THR HB H 1 4.905 0.04 . 1 . . . A 7 THR HB . 25070 1 87 . 1 1 10 10 THR HG21 H 1 1.223 0.04 . 1 . . . A 7 THR HG21 . 25070 1 88 . 1 1 10 10 THR HG22 H 1 1.223 0.04 . 1 . . . A 7 THR HG22 . 25070 1 89 . 1 1 10 10 THR HG23 H 1 1.223 0.04 . 1 . . . A 7 THR HG23 . 25070 1 90 . 1 1 10 10 THR C C 13 177.067 0.4 . 1 . . . A 7 THR C . 25070 1 91 . 1 1 10 10 THR CA C 13 60.535 0.40 . 1 . . . A 7 THR CA . 25070 1 92 . 1 1 10 10 THR CB C 13 70.474 0.40 . 1 . . . A 7 THR CB . 25070 1 93 . 1 1 10 10 THR CG2 C 13 21.126 0.40 . 1 . . . A 7 THR CG2 . 25070 1 94 . 1 1 10 10 THR N N 15 115.899 0.40 . 1 . . . A 7 THR N . 25070 1 95 . 1 1 11 11 LEU H H 1 9.348 0.04 . 1 . . . A 8 LEU H . 25070 1 96 . 1 1 11 11 LEU HA H 1 4.417 0.04 . 1 . . . A 8 LEU HA . 25070 1 97 . 1 1 11 11 LEU HB2 H 1 1.999 0.04 . 2 . . . A 8 LEU HB2 . 25070 1 98 . 1 1 11 11 LEU HB3 H 1 1.759 0.04 . 2 . . . A 8 LEU HB3 . 25070 1 99 . 1 1 11 11 LEU HG H 1 2.042 0.04 . 1 . . . A 8 LEU HG . 25070 1 100 . 1 1 11 11 LEU HD11 H 1 0.970 0.04 . 1 . . . A 8 LEU HD11 . 25070 1 101 . 1 1 11 11 LEU HD12 H 1 0.970 0.04 . 1 . . . A 8 LEU HD12 . 25070 1 102 . 1 1 11 11 LEU HD13 H 1 0.970 0.04 . 1 . . . A 8 LEU HD13 . 25070 1 103 . 1 1 11 11 LEU HD21 H 1 1.104 0.04 . 1 . . . A 8 LEU HD21 . 25070 1 104 . 1 1 11 11 LEU HD22 H 1 1.104 0.04 . 1 . . . A 8 LEU HD22 . 25070 1 105 . 1 1 11 11 LEU HD23 H 1 1.104 0.04 . 1 . . . A 8 LEU HD23 . 25070 1 106 . 1 1 11 11 LEU C C 13 178.319 0.4 . 1 . . . A 8 LEU C . 25070 1 107 . 1 1 11 11 LEU CA C 13 56.884 0.40 . 1 . . . A 8 LEU CA . 25070 1 108 . 1 1 11 11 LEU CB C 13 40.955 0.40 . 1 . . . A 8 LEU CB . 25070 1 109 . 1 1 11 11 LEU CG C 13 26.913 0.40 . 1 . . . A 8 LEU CG . 25070 1 110 . 1 1 11 11 LEU CD1 C 13 22.841 0.40 . 1 . . . A 8 LEU CD1 . 25070 1 111 . 1 1 11 11 LEU CD2 C 13 26.757 0.40 . 1 . . . A 8 LEU CD2 . 25070 1 112 . 1 1 11 11 LEU N N 15 119.810 0.40 . 1 . . . A 8 LEU N . 25070 1 113 . 1 1 12 12 THR H H 1 7.634 0.04 . 1 . . . A 9 THR H . 25070 1 114 . 1 1 12 12 THR HA H 1 4.463 0.04 . 1 . . . A 9 THR HA . 25070 1 115 . 1 1 12 12 THR HB H 1 4.597 0.04 . 1 . . . A 9 THR HB . 25070 1 116 . 1 1 12 12 THR HG21 H 1 1.180 0.04 . 1 . . . A 9 THR HG21 . 25070 1 117 . 1 1 12 12 THR HG22 H 1 1.180 0.04 . 1 . . . A 9 THR HG22 . 25070 1 118 . 1 1 12 12 THR HG23 H 1 1.180 0.04 . 1 . . . A 9 THR HG23 . 25070 1 119 . 1 1 12 12 THR C C 13 175.508 0.4 . 1 . . . A 9 THR C . 25070 1 120 . 1 1 12 12 THR CA C 13 61.082 0.40 . 1 . . . A 9 THR CA . 25070 1 121 . 1 1 12 12 THR CB C 13 68.889 0.40 . 1 . . . A 9 THR CB . 25070 1 122 . 1 1 12 12 THR CG2 C 13 21.648 0.40 . 1 . . . A 9 THR CG2 . 25070 1 123 . 1 1 12 12 THR N N 15 104.851 0.40 . 1 . . . A 9 THR N . 25070 1 124 . 1 1 13 13 GLY H H 1 7.672 0.04 . 1 . . . A 10 GLY H . 25070 1 125 . 1 1 13 13 GLY HA2 H 1 3.602 0.04 . 2 . . . A 10 GLY HA2 . 25070 1 126 . 1 1 13 13 GLY HA3 H 1 4.326 0.04 . 2 . . . A 10 GLY HA3 . 25070 1 127 . 1 1 13 13 GLY C C 13 174.073 0.4 . 1 . . . A 10 GLY C . 25070 1 128 . 1 1 13 13 GLY CA C 13 45.887 0.40 . 1 . . . A 10 GLY CA . 25070 1 129 . 1 1 13 13 GLY N N 15 108.799 0.40 . 1 . . . A 10 GLY N . 25070 1 130 . 1 1 14 14 LYS H H 1 7.483 0.04 . 1 . . . A 11 LYS H . 25070 1 131 . 1 1 14 14 LYS HA H 1 4.387 0.04 . 1 . . . A 11 LYS HA . 25070 1 132 . 1 1 14 14 LYS HB2 H 1 1.832 0.04 . 2 . . . A 11 LYS HB2 . 25070 1 133 . 1 1 14 14 LYS HB3 H 1 1.715 0.04 . 2 . . . A 11 LYS HB3 . 25070 1 134 . 1 1 14 14 LYS HG2 H 1 1.195 0.04 . 2 . . . A 11 LYS HG2 . 25070 1 135 . 1 1 14 14 LYS HG3 H 1 1.389 0.04 . 2 . . . A 11 LYS HG3 . 25070 1 136 . 1 1 14 14 LYS HD2 H 1 1.595 0.04 . 2 . . . A 11 LYS HD2 . 25070 1 137 . 1 1 14 14 LYS HD3 H 1 1.595 0.04 . 2 . . . A 11 LYS HD3 . 25070 1 138 . 1 1 14 14 LYS HE2 H 1 2.881 0.04 . 2 . . . A 11 LYS HE2 . 25070 1 139 . 1 1 14 14 LYS HE3 H 1 2.881 0.04 . 2 . . . A 11 LYS HE3 . 25070 1 140 . 1 1 14 14 LYS C C 13 175.797 0.4 . 1 . . . A 11 LYS C . 25070 1 141 . 1 1 14 14 LYS CA C 13 56.519 0.40 . 1 . . . A 11 LYS CA . 25070 1 142 . 1 1 14 14 LYS CB C 13 33.470 0.40 . 1 . . . A 11 LYS CB . 25070 1 143 . 1 1 14 14 LYS CG C 13 25.268 0.40 . 1 . . . A 11 LYS CG . 25070 1 144 . 1 1 14 14 LYS CD C 13 29.423 0.40 . 1 . . . A 11 LYS CD . 25070 1 145 . 1 1 14 14 LYS CE C 13 41.936 0.40 . 1 . . . A 11 LYS CE . 25070 1 146 . 1 1 14 14 LYS N N 15 123.011 0.40 . 1 . . . A 11 LYS N . 25070 1 147 . 1 1 15 15 THR H H 1 8.701 0.04 . 1 . . . A 12 THR H . 25070 1 148 . 1 1 15 15 THR HA H 1 5.022 0.04 . 1 . . . A 12 THR HA . 25070 1 149 . 1 1 15 15 THR HB H 1 3.912 0.04 . 1 . . . A 12 THR HB . 25070 1 150 . 1 1 15 15 THR HG21 H 1 1.051 0.04 . 1 . . . A 12 THR HG21 . 25070 1 151 . 1 1 15 15 THR HG22 H 1 1.051 0.04 . 1 . . . A 12 THR HG22 . 25070 1 152 . 1 1 15 15 THR HG23 H 1 1.051 0.04 . 1 . . . A 12 THR HG23 . 25070 1 153 . 1 1 15 15 THR C C 13 173.927 0.4 . 1 . . . A 12 THR C . 25070 1 154 . 1 1 15 15 THR CA C 13 62.410 0.40 . 1 . . . A 12 THR CA . 25070 1 155 . 1 1 15 15 THR CB C 13 69.978 0.40 . 1 . . . A 12 THR CB . 25070 1 156 . 1 1 15 15 THR CG2 C 13 21.536 0.40 . 1 . . . A 12 THR CG2 . 25070 1 157 . 1 1 15 15 THR N N 15 121.542 0.40 . 1 . . . A 12 THR N . 25070 1 158 . 1 1 16 16 ILE H H 1 9.673 0.04 . 1 . . . A 13 ILE H . 25070 1 159 . 1 1 16 16 ILE HA H 1 4.410 0.04 . 1 . . . A 13 ILE HA . 25070 1 160 . 1 1 16 16 ILE HB H 1 1.846 0.04 . 1 . . . A 13 ILE HB . 25070 1 161 . 1 1 16 16 ILE HG12 H 1 1.046 0.04 . 2 . . . A 13 ILE HG12 . 25070 1 162 . 1 1 16 16 ILE HG13 H 1 1.425 0.04 . 2 . . . A 13 ILE HG13 . 25070 1 163 . 1 1 16 16 ILE HG21 H 1 0.842 0.04 . 1 . . . A 13 ILE HG21 . 25070 1 164 . 1 1 16 16 ILE HG22 H 1 0.842 0.04 . 1 . . . A 13 ILE HG22 . 25070 1 165 . 1 1 16 16 ILE HG23 H 1 0.842 0.04 . 1 . . . A 13 ILE HG23 . 25070 1 166 . 1 1 16 16 ILE HD11 H 1 0.690 0.04 . 1 . . . A 13 ILE HD11 . 25070 1 167 . 1 1 16 16 ILE HD12 H 1 0.690 0.04 . 1 . . . A 13 ILE HD12 . 25070 1 168 . 1 1 16 16 ILE HD13 H 1 0.690 0.04 . 1 . . . A 13 ILE HD13 . 25070 1 169 . 1 1 16 16 ILE C C 13 175.089 0.4 . 1 . . . A 13 ILE C . 25070 1 170 . 1 1 16 16 ILE CA C 13 60.205 0.40 . 1 . . . A 13 ILE CA . 25070 1 171 . 1 1 16 16 ILE CB C 13 40.989 0.40 . 1 . . . A 13 ILE CB . 25070 1 172 . 1 1 16 16 ILE CG1 C 13 27.123 0.40 . 1 . . . A 13 ILE CG1 . 25070 1 173 . 1 1 16 16 ILE CG2 C 13 17.647 0.40 . 1 . . . A 13 ILE CG2 . 25070 1 174 . 1 1 16 16 ILE CD1 C 13 14.603 0.40 . 1 . . . A 13 ILE CD1 . 25070 1 175 . 1 1 16 16 ILE N N 15 129.326 0.40 . 1 . . . A 13 ILE N . 25070 1 176 . 1 1 17 17 THR H H 1 8.788 0.04 . 1 . . . A 14 THR H . 25070 1 177 . 1 1 17 17 THR HA H 1 4.902 0.04 . 1 . . . A 14 THR HA . 25070 1 178 . 1 1 17 17 THR HB H 1 4.002 0.04 . 1 . . . A 14 THR HB . 25070 1 179 . 1 1 17 17 THR HG21 H 1 1.086 0.04 . 1 . . . A 14 THR HG21 . 25070 1 180 . 1 1 17 17 THR HG22 H 1 1.086 0.04 . 1 . . . A 14 THR HG22 . 25070 1 181 . 1 1 17 17 THR HG23 H 1 1.086 0.04 . 1 . . . A 14 THR HG23 . 25070 1 182 . 1 1 17 17 THR C C 13 173.735 0.4 . 1 . . . A 14 THR C . 25070 1 183 . 1 1 17 17 THR CA C 13 62.295 0.40 . 1 . . . A 14 THR CA . 25070 1 184 . 1 1 17 17 THR CB C 13 69.562 0.40 . 1 . . . A 14 THR CB . 25070 1 185 . 1 1 17 17 THR CG2 C 13 21.543 0.40 . 1 . . . A 14 THR CG2 . 25070 1 186 . 1 1 17 17 THR N N 15 122.917 0.40 . 1 . . . A 14 THR N . 25070 1 187 . 1 1 18 18 LEU H H 1 8.738 0.04 . 1 . . . A 15 LEU H . 25070 1 188 . 1 1 18 18 LEU HA H 1 4.761 0.04 . 1 . . . A 15 LEU HA . 25070 1 189 . 1 1 18 18 LEU HB2 H 1 1.345 0.04 . 2 . . . A 15 LEU HB2 . 25070 1 190 . 1 1 18 18 LEU HB3 H 1 1.179 0.04 . 2 . . . A 15 LEU HB3 . 25070 1 191 . 1 1 18 18 LEU HG H 1 1.403 0.04 . 1 . . . A 15 LEU HG . 25070 1 192 . 1 1 18 18 LEU HD11 H 1 0.689 0.04 . 1 . . . A 15 LEU HD11 . 25070 1 193 . 1 1 18 18 LEU HD12 H 1 0.689 0.04 . 1 . . . A 15 LEU HD12 . 25070 1 194 . 1 1 18 18 LEU HD13 H 1 0.689 0.04 . 1 . . . A 15 LEU HD13 . 25070 1 195 . 1 1 18 18 LEU HD21 H 1 0.728 0.04 . 1 . . . A 15 LEU HD21 . 25070 1 196 . 1 1 18 18 LEU HD22 H 1 0.728 0.04 . 1 . . . A 15 LEU HD22 . 25070 1 197 . 1 1 18 18 LEU HD23 H 1 0.728 0.04 . 1 . . . A 15 LEU HD23 . 25070 1 198 . 1 1 18 18 LEU C C 13 174.822 0.4 . 1 . . . A 15 LEU C . 25070 1 199 . 1 1 18 18 LEU CA C 13 52.774 0.40 . 1 . . . A 15 LEU CA . 25070 1 200 . 1 1 18 18 LEU CB C 13 46.774 0.40 . 1 . . . A 15 LEU CB . 25070 1 201 . 1 1 18 18 LEU CG C 13 26.557 0.40 . 1 . . . A 15 LEU CG . 25070 1 202 . 1 1 18 18 LEU CD1 C 13 27.049 0.40 . 1 . . . A 15 LEU CD1 . 25070 1 203 . 1 1 18 18 LEU CD2 C 13 23.977 0.40 . 1 . . . A 15 LEU CD2 . 25070 1 204 . 1 1 18 18 LEU N N 15 125.286 0.40 . 1 . . . A 15 LEU N . 25070 1 205 . 1 1 19 19 GLU H H 1 8.193 0.04 . 1 . . . A 16 GLU H . 25070 1 206 . 1 1 19 19 GLU HA H 1 4.874 0.04 . 1 . . . A 16 GLU HA . 25070 1 207 . 1 1 19 19 GLU HB2 H 1 1.794 0.04 . 2 . . . A 16 GLU HB2 . 25070 1 208 . 1 1 19 19 GLU HB3 H 1 1.853 0.04 . 2 . . . A 16 GLU HB3 . 25070 1 209 . 1 1 19 19 GLU HG2 H 1 2.160 0.04 . 2 . . . A 16 GLU HG2 . 25070 1 210 . 1 1 19 19 GLU HG3 H 1 2.042 0.04 . 2 . . . A 16 GLU HG3 . 25070 1 211 . 1 1 19 19 GLU C C 13 175.895 0.4 . 1 . . . A 16 GLU C . 25070 1 212 . 1 1 19 19 GLU CA C 13 55.463 0.40 . 1 . . . A 16 GLU CA . 25070 1 213 . 1 1 19 19 GLU CB C 13 30.423 0.40 . 1 . . . A 16 GLU CB . 25070 1 214 . 1 1 19 19 GLU CG C 13 36.347 0.40 . 1 . . . A 16 GLU CG . 25070 1 215 . 1 1 19 19 GLU N N 15 122.011 0.40 . 1 . . . A 16 GLU N . 25070 1 216 . 1 1 20 20 VAL H H 1 8.812 0.04 . 1 . . . A 17 VAL H . 25070 1 217 . 1 1 20 20 VAL HA H 1 4.723 0.04 . 1 . . . A 17 VAL HA . 25070 1 218 . 1 1 20 20 VAL HB H 1 2.342 0.04 . 1 . . . A 17 VAL HB . 25070 1 219 . 1 1 20 20 VAL HG11 H 1 0.655 0.04 . 1 . . . A 17 VAL HG11 . 25070 1 220 . 1 1 20 20 VAL HG12 H 1 0.655 0.04 . 1 . . . A 17 VAL HG12 . 25070 1 221 . 1 1 20 20 VAL HG13 H 1 0.655 0.04 . 1 . . . A 17 VAL HG13 . 25070 1 222 . 1 1 20 20 VAL HG21 H 1 0.408 0.04 . 1 . . . A 17 VAL HG21 . 25070 1 223 . 1 1 20 20 VAL HG22 H 1 0.408 0.04 . 1 . . . A 17 VAL HG22 . 25070 1 224 . 1 1 20 20 VAL HG23 H 1 0.408 0.04 . 1 . . . A 17 VAL HG23 . 25070 1 225 . 1 1 20 20 VAL C C 13 173.790 0.4 . 1 . . . A 17 VAL C . 25070 1 226 . 1 1 20 20 VAL CA C 13 58.699 0.40 . 1 . . . A 17 VAL CA . 25070 1 227 . 1 1 20 20 VAL CB C 13 36.531 0.40 . 1 . . . A 17 VAL CB . 25070 1 228 . 1 1 20 20 VAL CG1 C 13 22.060 0.40 . 1 . . . A 17 VAL CG1 . 25070 1 229 . 1 1 20 20 VAL CG2 C 13 19.246 0.40 . 1 . . . A 17 VAL CG2 . 25070 1 230 . 1 1 20 20 VAL N N 15 116.809 0.40 . 1 . . . A 17 VAL N . 25070 1 231 . 1 1 21 21 GLU H H 1 8.549 0.04 . 1 . . . A 18 GLU H . 25070 1 232 . 1 1 21 21 GLU HA H 1 4.936 0.04 . 1 . . . A 18 GLU HA . 25070 1 233 . 1 1 21 21 GLU HB2 H 1 1.616 0.04 . 2 . . . A 18 GLU HB2 . 25070 1 234 . 1 1 21 21 GLU HB3 H 1 2.032 0.04 . 2 . . . A 18 GLU HB3 . 25070 1 235 . 1 1 21 21 GLU HG2 H 1 2.029 0.04 . 2 . . . A 18 GLU HG2 . 25070 1 236 . 1 1 21 21 GLU HG3 H 1 2.124 0.04 . 2 . . . A 18 GLU HG3 . 25070 1 237 . 1 1 21 21 GLU CA C 13 53.469 0.40 . 1 . . . A 18 GLU CA . 25070 1 238 . 1 1 21 21 GLU CB C 13 31.329 0.40 . 1 . . . A 18 GLU CB . 25070 1 239 . 1 1 21 21 GLU CG C 13 36.393 0.40 . 1 . . . A 18 GLU CG . 25070 1 240 . 1 1 21 21 GLU N N 15 118.350 0.40 . 1 . . . A 18 GLU N . 25070 1 241 . 1 1 22 22 PRO HA H 1 4.083 0.04 . 1 . . . A 19 PRO HA . 25070 1 242 . 1 1 22 22 PRO HB2 H 1 2.393 0.04 . 2 . . . A 19 PRO HB2 . 25070 1 243 . 1 1 22 22 PRO HB3 H 1 1.962 0.04 . 2 . . . A 19 PRO HB3 . 25070 1 244 . 1 1 22 22 PRO HG2 H 1 2.014 0.04 . 2 . . . A 19 PRO HG2 . 25070 1 245 . 1 1 22 22 PRO HG3 H 1 2.140 0.04 . 2 . . . A 19 PRO HG3 . 25070 1 246 . 1 1 22 22 PRO HD2 H 1 3.768 0.04 . 2 . . . A 19 PRO HD2 . 25070 1 247 . 1 1 22 22 PRO HD3 H 1 3.878 0.04 . 2 . . . A 19 PRO HD3 . 25070 1 248 . 1 1 22 22 PRO C C 13 175.250 0.4 . 1 . . . A 19 PRO C . 25070 1 249 . 1 1 22 22 PRO CA C 13 65.476 0.40 . 1 . . . A 19 PRO CA . 25070 1 250 . 1 1 22 22 PRO CB C 13 31.840 0.40 . 1 . . . A 19 PRO CB . 25070 1 251 . 1 1 22 22 PRO CG C 13 27.917 0.40 . 1 . . . A 19 PRO CG . 25070 1 252 . 1 1 22 22 PRO CD C 13 50.741 0.40 . 1 . . . A 19 PRO CD . 25070 1 253 . 1 1 23 23 SER H H 1 7.071 0.04 . 1 . . . A 20 SER H . 25070 1 254 . 1 1 23 23 SER HA H 1 4.342 0.04 . 1 . . . A 20 SER HA . 25070 1 255 . 1 1 23 23 SER HB2 H 1 3.747 0.04 . 2 . . . A 20 SER HB2 . 25070 1 256 . 1 1 23 23 SER HB3 H 1 4.115 0.04 . 2 . . . A 20 SER HB3 . 25070 1 257 . 1 1 23 23 SER C C 13 174.574 0.4 . 1 . . . A 20 SER C . 25070 1 258 . 1 1 23 23 SER CA C 13 57.351 0.40 . 1 . . . A 20 SER CA . 25070 1 259 . 1 1 23 23 SER CB C 13 63.368 0.40 . 1 . . . A 20 SER CB . 25070 1 260 . 1 1 23 23 SER N N 15 103.757 0.40 . 1 . . . A 20 SER N . 25070 1 261 . 1 1 24 24 ASP H H 1 8.019 0.04 . 1 . . . A 21 ASP H . 25070 1 262 . 1 1 24 24 ASP HA H 1 4.643 0.04 . 1 . . . A 21 ASP HA . 25070 1 263 . 1 1 24 24 ASP HB2 H 1 2.469 0.04 . 2 . . . A 21 ASP HB2 . 25070 1 264 . 1 1 24 24 ASP HB3 H 1 2.897 0.04 . 2 . . . A 21 ASP HB3 . 25070 1 265 . 1 1 24 24 ASP C C 13 176.320 0.4 . 1 . . . A 21 ASP C . 25070 1 266 . 1 1 24 24 ASP CA C 13 55.976 0.40 . 1 . . . A 21 ASP CA . 25070 1 267 . 1 1 24 24 ASP CB C 13 40.935 0.40 . 1 . . . A 21 ASP CB . 25070 1 268 . 1 1 24 24 ASP N N 15 123.881 0.40 . 1 . . . A 21 ASP N . 25070 1 269 . 1 1 25 25 THR H H 1 7.872 0.04 . 1 . . . A 22 THR H . 25070 1 270 . 1 1 25 25 THR HA H 1 4.879 0.04 . 1 . . . A 22 THR HA . 25070 1 271 . 1 1 25 25 THR HB H 1 4.877 0.04 . 1 . . . A 22 THR HB . 25070 1 272 . 1 1 25 25 THR C C 13 176.720 0.4 . 1 . . . A 22 THR C . 25070 1 273 . 1 1 25 25 THR CA C 13 59.607 0.40 . 1 . . . A 22 THR CA . 25070 1 274 . 1 1 25 25 THR CB C 13 71.138 0.40 . 1 . . . A 22 THR CB . 25070 1 275 . 1 1 25 25 THR N N 15 109.189 0.40 . 1 . . . A 22 THR N . 25070 1 276 . 1 1 26 26 ILE H H 1 8.581 0.04 . 1 . . . A 23 ILE H . 25070 1 277 . 1 1 26 26 ILE HA H 1 3.611 0.04 . 1 . . . A 23 ILE HA . 25070 1 278 . 1 1 26 26 ILE HB H 1 2.490 0.04 . 1 . . . A 23 ILE HB . 25070 1 279 . 1 1 26 26 ILE HG12 H 1 1.289 0.04 . 2 . . . A 23 ILE HG12 . 25070 1 280 . 1 1 26 26 ILE HG13 H 1 1.886 0.04 . 2 . . . A 23 ILE HG13 . 25070 1 281 . 1 1 26 26 ILE HG21 H 1 0.721 0.04 . 1 . . . A 23 ILE HG21 . 25070 1 282 . 1 1 26 26 ILE HG22 H 1 0.721 0.04 . 1 . . . A 23 ILE HG22 . 25070 1 283 . 1 1 26 26 ILE HG23 H 1 0.721 0.04 . 1 . . . A 23 ILE HG23 . 25070 1 284 . 1 1 26 26 ILE HD11 H 1 0.529 0.04 . 1 . . . A 23 ILE HD11 . 25070 1 285 . 1 1 26 26 ILE HD12 H 1 0.529 0.04 . 1 . . . A 23 ILE HD12 . 25070 1 286 . 1 1 26 26 ILE HD13 H 1 0.529 0.04 . 1 . . . A 23 ILE HD13 . 25070 1 287 . 1 1 26 26 ILE CA C 13 62.184 0.40 . 1 . . . A 23 ILE CA . 25070 1 288 . 1 1 26 26 ILE CB C 13 34.272 0.40 . 1 . . . A 23 ILE CB . 25070 1 289 . 1 1 26 26 ILE CG1 C 13 27.601 0.40 . 1 . . . A 23 ILE CG1 . 25070 1 290 . 1 1 26 26 ILE CG2 C 13 17.938 0.40 . 1 . . . A 23 ILE CG2 . 25070 1 291 . 1 1 26 26 ILE CD1 C 13 9.072 0.40 . 1 . . . A 23 ILE CD1 . 25070 1 292 . 1 1 26 26 ILE N N 15 121.391 0.40 . 1 . . . A 23 ILE N . 25070 1 293 . 1 1 27 27 GLU HA H 1 3.861 0.04 . 1 . . . A 24 GLU HA . 25070 1 294 . 1 1 27 27 GLU HB2 H 1 1.977 0.04 . 2 . . . A 24 GLU HB2 . 25070 1 295 . 1 1 27 27 GLU HB3 H 1 2.017 0.04 . 2 . . . A 24 GLU HB3 . 25070 1 296 . 1 1 27 27 GLU HG2 H 1 2.318 0.04 . 2 . . . A 24 GLU HG2 . 25070 1 297 . 1 1 27 27 GLU HG3 H 1 2.288 0.04 . 2 . . . A 24 GLU HG3 . 25070 1 298 . 1 1 27 27 GLU C C 13 178.944 0.4 . 1 . . . A 24 GLU C . 25070 1 299 . 1 1 27 27 GLU CA C 13 60.514 0.40 . 1 . . . A 24 GLU CA . 25070 1 300 . 1 1 27 27 GLU CB C 13 28.719 0.40 . 1 . . . A 24 GLU CB . 25070 1 301 . 1 1 27 27 GLU CG C 13 36.224 0.40 . 1 . . . A 24 GLU CG . 25070 1 302 . 1 1 28 28 ASN H H 1 7.920 0.04 . 1 . . . A 25 ASN H . 25070 1 303 . 1 1 28 28 ASN HA H 1 4.521 0.04 . 1 . . . A 25 ASN HA . 25070 1 304 . 1 1 28 28 ASN HB2 H 1 2.829 0.04 . 2 . . . A 25 ASN HB2 . 25070 1 305 . 1 1 28 28 ASN HB3 H 1 3.190 0.04 . 2 . . . A 25 ASN HB3 . 25070 1 306 . 1 1 28 28 ASN HD21 H 1 7.882 0.04 . 1 . . . A 25 ASN HD21 . 25070 1 307 . 1 1 28 28 ASN HD22 H 1 6.882 0.04 . 2 . . . A 25 ASN HD22 . 25070 1 308 . 1 1 28 28 ASN C C 13 178.260 0.4 . 1 . . . A 25 ASN C . 25070 1 309 . 1 1 28 28 ASN CA C 13 55.941 0.40 . 1 . . . A 25 ASN CA . 25070 1 310 . 1 1 28 28 ASN CB C 13 38.342 0.40 . 1 . . . A 25 ASN CB . 25070 1 311 . 1 1 28 28 ASN N N 15 121.433 0.40 . 1 . . . A 25 ASN N . 25070 1 312 . 1 1 28 28 ASN ND2 N 15 109.591 0.04 . 1 . . . A 25 ASN ND2 . 25070 1 313 . 1 1 29 29 VAL H H 1 8.129 0.04 . 1 . . . A 26 VAL H . 25070 1 314 . 1 1 29 29 VAL HA H 1 3.360 0.04 . 1 . . . A 26 VAL HA . 25070 1 315 . 1 1 29 29 VAL HB H 1 2.324 0.04 . 1 . . . A 26 VAL HB . 25070 1 316 . 1 1 29 29 VAL HG11 H 1 0.942 0.04 . 1 . . . A 26 VAL HG11 . 25070 1 317 . 1 1 29 29 VAL HG12 H 1 0.942 0.04 . 1 . . . A 26 VAL HG12 . 25070 1 318 . 1 1 29 29 VAL HG13 H 1 0.942 0.04 . 1 . . . A 26 VAL HG13 . 25070 1 319 . 1 1 29 29 VAL HG21 H 1 0.659 0.04 . 1 . . . A 26 VAL HG21 . 25070 1 320 . 1 1 29 29 VAL HG22 H 1 0.659 0.04 . 1 . . . A 26 VAL HG22 . 25070 1 321 . 1 1 29 29 VAL HG23 H 1 0.659 0.04 . 1 . . . A 26 VAL HG23 . 25070 1 322 . 1 1 29 29 VAL C C 13 177.758 0.4 . 1 . . . A 26 VAL C . 25070 1 323 . 1 1 29 29 VAL CA C 13 67.678 0.40 . 1 . . . A 26 VAL CA . 25070 1 324 . 1 1 29 29 VAL CB C 13 30.844 0.40 . 1 . . . A 26 VAL CB . 25070 1 325 . 1 1 29 29 VAL CG1 C 13 23.680 0.40 . 1 . . . A 26 VAL CG1 . 25070 1 326 . 1 1 29 29 VAL CG2 C 13 21.057 0.40 . 1 . . . A 26 VAL CG2 . 25070 1 327 . 1 1 29 29 VAL N N 15 122.450 0.40 . 1 . . . A 26 VAL N . 25070 1 328 . 1 1 30 30 LYS H H 1 8.606 0.04 . 1 . . . A 27 LYS H . 25070 1 329 . 1 1 30 30 LYS HA H 1 4.607 0.04 . 1 . . . A 27 LYS HA . 25070 1 330 . 1 1 30 30 LYS HB2 H 1 1.971 0.04 . 2 . . . A 27 LYS HB2 . 25070 1 331 . 1 1 30 30 LYS HB3 H 1 1.423 0.04 . 2 . . . A 27 LYS HB3 . 25070 1 332 . 1 1 30 30 LYS HG2 H 1 1.459 0.04 . 2 . . . A 27 LYS HG2 . 25070 1 333 . 1 1 30 30 LYS HG3 H 1 1.459 0.04 . 2 . . . A 27 LYS HG3 . 25070 1 334 . 1 1 30 30 LYS HD2 H 1 1.667 0.04 . 2 . . . A 27 LYS HD2 . 25070 1 335 . 1 1 30 30 LYS HD3 H 1 1.667 0.04 . 2 . . . A 27 LYS HD3 . 25070 1 336 . 1 1 30 30 LYS HE2 H 1 2.720 0.04 . 2 . . . A 27 LYS HE2 . 25070 1 337 . 1 1 30 30 LYS HE3 H 1 2.581 0.04 . 2 . . . A 27 LYS HE3 . 25070 1 338 . 1 1 30 30 LYS C C 13 180.552 0.4 . 1 . . . A 27 LYS C . 25070 1 339 . 1 1 30 30 LYS CA C 13 59.233 0.40 . 1 . . . A 27 LYS CA . 25070 1 340 . 1 1 30 30 LYS CB C 13 33.744 0.40 . 1 . . . A 27 LYS CB . 25070 1 341 . 1 1 30 30 LYS CG C 13 26.414 0.40 . 1 . . . A 27 LYS CG . 25070 1 342 . 1 1 30 30 LYS CD C 13 30.438 0.40 . 1 . . . A 27 LYS CD . 25070 1 343 . 1 1 30 30 LYS CE C 13 42.574 0.40 . 1 . . . A 27 LYS CE . 25070 1 344 . 1 1 30 30 LYS N N 15 119.093 0.40 . 1 . . . A 27 LYS N . 25070 1 345 . 1 1 31 31 ALA H H 1 8.018 0.04 . 1 . . . A 28 ALA H . 25070 1 346 . 1 1 31 31 ALA HA H 1 4.141 0.04 . 1 . . . A 28 ALA HA . 25070 1 347 . 1 1 31 31 ALA HB1 H 1 1.601 0.04 . 1 . . . A 28 ALA HB1 . 25070 1 348 . 1 1 31 31 ALA HB2 H 1 1.601 0.04 . 1 . . . A 28 ALA HB2 . 25070 1 349 . 1 1 31 31 ALA HB3 H 1 1.601 0.04 . 1 . . . A 28 ALA HB3 . 25070 1 350 . 1 1 31 31 ALA C C 13 180.203 0.4 . 1 . . . A 28 ALA C . 25070 1 351 . 1 1 31 31 ALA CA C 13 55.264 0.40 . 1 . . . A 28 ALA CA . 25070 1 352 . 1 1 31 31 ALA CB C 13 17.759 0.40 . 1 . . . A 28 ALA CB . 25070 1 353 . 1 1 31 31 ALA N N 15 123.538 0.40 . 1 . . . A 28 ALA N . 25070 1 354 . 1 1 32 32 LYS H H 1 7.970 0.04 . 1 . . . A 29 LYS H . 25070 1 355 . 1 1 32 32 LYS HA H 1 4.169 0.04 . 1 . . . A 29 LYS HA . 25070 1 356 . 1 1 32 32 LYS HB2 H 1 2.124 0.04 . 2 . . . A 29 LYS HB2 . 25070 1 357 . 1 1 32 32 LYS HB3 H 1 1.909 0.04 . 2 . . . A 29 LYS HB3 . 25070 1 358 . 1 1 32 32 LYS HG2 H 1 1.778 0.04 . 2 . . . A 29 LYS HG2 . 25070 1 359 . 1 1 32 32 LYS HG3 H 1 1.586 0.04 . 2 . . . A 29 LYS HG3 . 25070 1 360 . 1 1 32 32 LYS HD2 H 1 1.765 0.04 . 2 . . . A 29 LYS HD2 . 25070 1 361 . 1 1 32 32 LYS HD3 H 1 1.413 0.04 . 2 . . . A 29 LYS HD3 . 25070 1 362 . 1 1 32 32 LYS HE2 H 1 2.925 0.04 . 2 . . . A 29 LYS HE2 . 25070 1 363 . 1 1 32 32 LYS HE3 H 1 3.166 0.04 . 2 . . . A 29 LYS HE3 . 25070 1 364 . 1 1 32 32 LYS C C 13 180.295 0.4 . 1 . . . A 29 LYS C . 25070 1 365 . 1 1 32 32 LYS CA C 13 59.799 0.40 . 1 . . . A 29 LYS CA . 25070 1 366 . 1 1 32 32 LYS CB C 13 33.413 0.40 . 1 . . . A 29 LYS CB . 25070 1 367 . 1 1 32 32 LYS CG C 13 26.327 0.40 . 1 . . . A 29 LYS CG . 25070 1 368 . 1 1 32 32 LYS CD C 13 30.205 0.40 . 1 . . . A 29 LYS CD . 25070 1 369 . 1 1 32 32 LYS CE C 13 42.299 0.40 . 1 . . . A 29 LYS CE . 25070 1 370 . 1 1 32 32 LYS N N 15 120.634 0.40 . 1 . . . A 29 LYS N . 25070 1 371 . 1 1 33 33 ILE H H 1 8.277 0.04 . 1 . . . A 30 ILE H . 25070 1 372 . 1 1 33 33 ILE HA H 1 3.465 0.04 . 1 . . . A 30 ILE HA . 25070 1 373 . 1 1 33 33 ILE HB H 1 2.300 0.04 . 1 . . . A 30 ILE HB . 25070 1 374 . 1 1 33 33 ILE HG12 H 1 1.991 0.04 . 2 . . . A 30 ILE HG12 . 25070 1 375 . 1 1 33 33 ILE HG13 H 1 0.655 0.04 . 2 . . . A 30 ILE HG13 . 25070 1 376 . 1 1 33 33 ILE HG21 H 1 0.657 0.04 . 1 . . . A 30 ILE HG21 . 25070 1 377 . 1 1 33 33 ILE HG22 H 1 0.657 0.04 . 1 . . . A 30 ILE HG22 . 25070 1 378 . 1 1 33 33 ILE HG23 H 1 0.657 0.04 . 1 . . . A 30 ILE HG23 . 25070 1 379 . 1 1 33 33 ILE HD11 H 1 0.856 0.04 . 1 . . . A 30 ILE HD11 . 25070 1 380 . 1 1 33 33 ILE HD12 H 1 0.856 0.04 . 1 . . . A 30 ILE HD12 . 25070 1 381 . 1 1 33 33 ILE HD13 H 1 0.856 0.04 . 1 . . . A 30 ILE HD13 . 25070 1 382 . 1 1 33 33 ILE C C 13 178.109 0.4 . 1 . . . A 30 ILE C . 25070 1 383 . 1 1 33 33 ILE CA C 13 66.240 0.40 . 1 . . . A 30 ILE CA . 25070 1 384 . 1 1 33 33 ILE CB C 13 36.819 0.40 . 1 . . . A 30 ILE CB . 25070 1 385 . 1 1 33 33 ILE CG1 C 13 31.140 0.40 . 1 . . . A 30 ILE CG1 . 25070 1 386 . 1 1 33 33 ILE CG2 C 13 17.079 0.40 . 1 . . . A 30 ILE CG2 . 25070 1 387 . 1 1 33 33 ILE CD1 C 13 14.911 0.40 . 1 . . . A 30 ILE CD1 . 25070 1 388 . 1 1 33 33 ILE N N 15 121.554 0.40 . 1 . . . A 30 ILE N . 25070 1 389 . 1 1 34 34 GLN H H 1 8.533 0.04 . 1 . . . A 31 GLN H . 25070 1 390 . 1 1 34 34 GLN HA H 1 3.805 0.04 . 1 . . . A 31 GLN HA . 25070 1 391 . 1 1 34 34 GLN HB2 H 1 2.449 0.04 . 2 . . . A 31 GLN HB2 . 25070 1 392 . 1 1 34 34 GLN HB3 H 1 1.969 0.04 . 2 . . . A 31 GLN HB3 . 25070 1 393 . 1 1 34 34 GLN HG2 H 1 1.878 0.04 . 2 . . . A 31 GLN HG2 . 25070 1 394 . 1 1 34 34 GLN HG3 H 1 2.239 0.04 . 2 . . . A 31 GLN HG3 . 25070 1 395 . 1 1 34 34 GLN HE21 H 1 7.653 0.04 . 1 . . . A 31 GLN HE21 . 25070 1 396 . 1 1 34 34 GLN HE22 H 1 6.812 0.04 . 2 . . . A 31 GLN HE22 . 25070 1 397 . 1 1 34 34 GLN C C 13 178.933 0.4 . 1 . . . A 31 GLN C . 25070 1 398 . 1 1 34 34 GLN CA C 13 60.057 0.40 . 1 . . . A 31 GLN CA . 25070 1 399 . 1 1 34 34 GLN CB C 13 27.806 0.40 . 1 . . . A 31 GLN CB . 25070 1 400 . 1 1 34 34 GLN CG C 13 33.841 0.40 . 1 . . . A 31 GLN CG . 25070 1 401 . 1 1 34 34 GLN N N 15 123.668 0.40 . 1 . . . A 31 GLN N . 25070 1 402 . 1 1 34 34 GLN NE2 N 15 109.752 0.04 . 1 . . . A 31 GLN NE2 . 25070 1 403 . 1 1 35 35 ASP H H 1 8.183 0.04 . 1 . . . A 32 ASP H . 25070 1 404 . 1 1 35 35 ASP HA H 1 4.299 0.04 . 1 . . . A 32 ASP HA . 25070 1 405 . 1 1 35 35 ASP HB2 H 1 2.809 0.04 . 2 . . . A 32 ASP HB2 . 25070 1 406 . 1 1 35 35 ASP HB3 H 1 2.721 0.04 . 2 . . . A 32 ASP HB3 . 25070 1 407 . 1 1 35 35 ASP C C 13 177.413 0.4 . 1 . . . A 32 ASP C . 25070 1 408 . 1 1 35 35 ASP CA C 13 57.518 0.40 . 1 . . . A 32 ASP CA . 25070 1 409 . 1 1 35 35 ASP CB C 13 41.119 0.40 . 1 . . . A 32 ASP CB . 25070 1 410 . 1 1 35 35 ASP N N 15 120.284 0.40 . 1 . . . A 32 ASP N . 25070 1 411 . 1 1 36 36 LYS H H 1 7.519 0.04 . 1 . . . A 33 LYS H . 25070 1 412 . 1 1 36 36 LYS HA H 1 4.255 0.04 . 1 . . . A 33 LYS HA . 25070 1 413 . 1 1 36 36 LYS HB2 H 1 1.976 0.04 . 2 . . . A 33 LYS HB2 . 25070 1 414 . 1 1 36 36 LYS HB3 H 1 1.813 0.04 . 2 . . . A 33 LYS HB3 . 25070 1 415 . 1 1 36 36 LYS HG2 H 1 1.578 0.04 . 2 . . . A 33 LYS HG2 . 25070 1 416 . 1 1 36 36 LYS HG3 H 1 1.583 0.04 . 2 . . . A 33 LYS HG3 . 25070 1 417 . 1 1 36 36 LYS HD2 H 1 1.676 0.04 . 2 . . . A 33 LYS HD2 . 25070 1 418 . 1 1 36 36 LYS HD3 H 1 1.676 0.04 . 2 . . . A 33 LYS HD3 . 25070 1 419 . 1 1 36 36 LYS HE2 H 1 3.153 0.04 . 2 . . . A 33 LYS HE2 . 25070 1 420 . 1 1 36 36 LYS HE3 H 1 3.093 0.04 . 2 . . . A 33 LYS HE3 . 25070 1 421 . 1 1 36 36 LYS C C 13 177.920 0.4 . 1 . . . A 33 LYS C . 25070 1 422 . 1 1 36 36 LYS CA C 13 58.388 0.40 . 1 . . . A 33 LYS CA . 25070 1 423 . 1 1 36 36 LYS CB C 13 34.010 0.40 . 1 . . . A 33 LYS CB . 25070 1 424 . 1 1 36 36 LYS CG C 13 25.291 0.40 . 1 . . . A 33 LYS CG . 25070 1 425 . 1 1 36 36 LYS CD C 13 28.926 0.40 . 1 . . . A 33 LYS CD . 25070 1 426 . 1 1 36 36 LYS CE C 13 42.344 0.40 . 1 . . . A 33 LYS CE . 25070 1 427 . 1 1 36 36 LYS N N 15 115.735 0.40 . 1 . . . A 33 LYS N . 25070 1 428 . 1 1 37 37 GLU H H 1 8.664 0.04 . 1 . . . A 34 GLU H . 25070 1 429 . 1 1 37 37 GLU HA H 1 4.545 0.04 . 1 . . . A 34 GLU HA . 25070 1 430 . 1 1 37 37 GLU HB2 H 1 2.256 0.04 . 2 . . . A 34 GLU HB2 . 25070 1 431 . 1 1 37 37 GLU HB3 H 1 1.631 0.04 . 2 . . . A 34 GLU HB3 . 25070 1 432 . 1 1 37 37 GLU HG2 H 1 2.030 0.04 . 2 . . . A 34 GLU HG2 . 25070 1 433 . 1 1 37 37 GLU HG3 H 1 2.132 0.04 . 2 . . . A 34 GLU HG3 . 25070 1 434 . 1 1 37 37 GLU C C 13 177.854 0.4 . 1 . . . A 34 GLU C . 25070 1 435 . 1 1 37 37 GLU CA C 13 55.330 0.40 . 1 . . . A 34 GLU CA . 25070 1 436 . 1 1 37 37 GLU CB C 13 33.286 0.40 . 1 . . . A 34 GLU CB . 25070 1 437 . 1 1 37 37 GLU CG C 13 36.166 0.40 . 1 . . . A 34 GLU CG . 25070 1 438 . 1 1 37 37 GLU N N 15 113.992 0.40 . 1 . . . A 34 GLU N . 25070 1 439 . 1 1 38 38 GLY H H 1 8.517 0.04 . 1 . . . A 35 GLY H . 25070 1 440 . 1 1 38 38 GLY HA2 H 1 3.889 0.04 . 2 . . . A 35 GLY HA2 . 25070 1 441 . 1 1 38 38 GLY HA3 H 1 4.097 0.04 . 2 . . . A 35 GLY HA3 . 25070 1 442 . 1 1 38 38 GLY C C 13 173.957 0.4 . 1 . . . A 35 GLY C . 25070 1 443 . 1 1 38 38 GLY CA C 13 45.960 0.40 . 1 . . . A 35 GLY CA . 25070 1 444 . 1 1 38 38 GLY N N 15 109.282 0.40 . 1 . . . A 35 GLY N . 25070 1 445 . 1 1 39 39 ILE H H 1 6.130 0.04 . 1 . . . A 36 ILE H . 25070 1 446 . 1 1 39 39 ILE HA H 1 4.359 0.04 . 1 . . . A 36 ILE HA . 25070 1 447 . 1 1 39 39 ILE HB H 1 1.372 0.04 . 1 . . . A 36 ILE HB . 25070 1 448 . 1 1 39 39 ILE HG12 H 1 1.066 0.04 . 2 . . . A 36 ILE HG12 . 25070 1 449 . 1 1 39 39 ILE HG13 H 1 1.357 0.04 . 2 . . . A 36 ILE HG13 . 25070 1 450 . 1 1 39 39 ILE HG21 H 1 0.904 0.04 . 1 . . . A 36 ILE HG21 . 25070 1 451 . 1 1 39 39 ILE HG22 H 1 0.904 0.04 . 1 . . . A 36 ILE HG22 . 25070 1 452 . 1 1 39 39 ILE HG23 H 1 0.904 0.04 . 1 . . . A 36 ILE HG23 . 25070 1 453 . 1 1 39 39 ILE HD11 H 1 0.741 0.04 . 1 . . . A 36 ILE HD11 . 25070 1 454 . 1 1 39 39 ILE HD12 H 1 0.741 0.04 . 1 . . . A 36 ILE HD12 . 25070 1 455 . 1 1 39 39 ILE HD13 H 1 0.741 0.04 . 1 . . . A 36 ILE HD13 . 25070 1 456 . 1 1 39 39 ILE CA C 13 57.857 0.40 . 1 . . . A 36 ILE CA . 25070 1 457 . 1 1 39 39 ILE CB C 13 40.555 0.40 . 1 . . . A 36 ILE CB . 25070 1 458 . 1 1 39 39 ILE CG1 C 13 26.757 0.40 . 1 . . . A 36 ILE CG1 . 25070 1 459 . 1 1 39 39 ILE CG2 C 13 18.105 0.40 . 1 . . . A 36 ILE CG2 . 25070 1 460 . 1 1 39 39 ILE CD1 C 13 13.453 0.40 . 1 . . . A 36 ILE CD1 . 25070 1 461 . 1 1 39 39 ILE N N 15 120.580 0.40 . 1 . . . A 36 ILE N . 25070 1 462 . 1 1 40 40 PRO HA H 1 4.605 0.04 . 1 . . . A 37 PRO HA . 25070 1 463 . 1 1 40 40 PRO HB2 H 1 2.378 0.04 . 2 . . . A 37 PRO HB2 . 25070 1 464 . 1 1 40 40 PRO HB3 H 1 1.936 0.04 . 2 . . . A 37 PRO HB3 . 25070 1 465 . 1 1 40 40 PRO HG2 H 1 1.995 0.04 . 2 . . . A 37 PRO HG2 . 25070 1 466 . 1 1 40 40 PRO HG3 H 1 2.072 0.04 . 2 . . . A 37 PRO HG3 . 25070 1 467 . 1 1 40 40 PRO HD2 H 1 3.559 0.04 . 2 . . . A 37 PRO HD2 . 25070 1 468 . 1 1 40 40 PRO HD3 H 1 4.168 0.04 . 2 . . . A 37 PRO HD3 . 25070 1 469 . 1 1 40 40 PRO CA C 13 61.614 0.40 . 1 . . . A 37 PRO CA . 25070 1 470 . 1 1 40 40 PRO CB C 13 31.683 0.40 . 1 . . . A 37 PRO CB . 25070 1 471 . 1 1 40 40 PRO CG C 13 28.195 0.40 . 1 . . . A 37 PRO CG . 25070 1 472 . 1 1 40 40 PRO CD C 13 51.006 0.40 . 1 . . . A 37 PRO CD . 25070 1 473 . 1 1 41 41 PRO HA H 1 4.102 0.04 . 1 . . . A 38 PRO HA . 25070 1 474 . 1 1 41 41 PRO HB2 H 1 2.234 0.04 . 2 . . . A 38 PRO HB2 . 25070 1 475 . 1 1 41 41 PRO HB3 H 1 2.005 0.04 . 2 . . . A 38 PRO HB3 . 25070 1 476 . 1 1 41 41 PRO HG2 H 1 1.601 0.04 . 2 . . . A 38 PRO HG2 . 25070 1 477 . 1 1 41 41 PRO HG3 H 1 2.154 0.04 . 2 . . . A 38 PRO HG3 . 25070 1 478 . 1 1 41 41 PRO HD2 H 1 3.726 0.04 . 2 . . . A 38 PRO HD2 . 25070 1 479 . 1 1 41 41 PRO HD3 H 1 3.726 0.04 . 2 . . . A 38 PRO HD3 . 25070 1 480 . 1 1 41 41 PRO C C 13 178.383 0.4 . 1 . . . A 38 PRO C . 25070 1 481 . 1 1 41 41 PRO CA C 13 66.064 0.40 . 1 . . . A 38 PRO CA . 25070 1 482 . 1 1 41 41 PRO CB C 13 32.891 0.40 . 1 . . . A 38 PRO CB . 25070 1 483 . 1 1 41 41 PRO CG C 13 27.707 0.40 . 1 . . . A 38 PRO CG . 25070 1 484 . 1 1 41 41 PRO CD C 13 51.094 0.40 . 1 . . . A 38 PRO CD . 25070 1 485 . 1 1 42 42 ASP H H 1 8.538 0.04 . 1 . . . A 39 ASP H . 25070 1 486 . 1 1 42 42 ASP HA H 1 4.358 0.04 . 1 . . . A 39 ASP HA . 25070 1 487 . 1 1 42 42 ASP HB2 H 1 2.733 0.04 . 2 . . . A 39 ASP HB2 . 25070 1 488 . 1 1 42 42 ASP HB3 H 1 2.643 0.04 . 2 . . . A 39 ASP HB3 . 25070 1 489 . 1 1 42 42 ASP C C 13 177.038 0.4 . 1 . . . A 39 ASP C . 25070 1 490 . 1 1 42 42 ASP CA C 13 55.686 0.40 . 1 . . . A 39 ASP CA . 25070 1 491 . 1 1 42 42 ASP CB C 13 39.711 0.40 . 1 . . . A 39 ASP CB . 25070 1 492 . 1 1 42 42 ASP N N 15 113.741 0.40 . 1 . . . A 39 ASP N . 25070 1 493 . 1 1 43 43 GLN H H 1 7.799 0.04 . 1 . . . A 40 GLN H . 25070 1 494 . 1 1 43 43 GLN HA H 1 4.436 0.04 . 1 . . . A 40 GLN HA . 25070 1 495 . 1 1 43 43 GLN HB2 H 1 2.374 0.04 . 2 . . . A 40 GLN HB2 . 25070 1 496 . 1 1 43 43 GLN HB3 H 1 1.798 0.04 . 2 . . . A 40 GLN HB3 . 25070 1 497 . 1 1 43 43 GLN HG2 H 1 2.382 0.04 . 2 . . . A 40 GLN HG2 . 25070 1 498 . 1 1 43 43 GLN HG3 H 1 2.382 0.04 . 2 . . . A 40 GLN HG3 . 25070 1 499 . 1 1 43 43 GLN HE21 H 1 7.617 0.04 . 1 . . . A 40 GLN HE21 . 25070 1 500 . 1 1 43 43 GLN HE22 H 1 6.699 0.04 . 2 . . . A 40 GLN HE22 . 25070 1 501 . 1 1 43 43 GLN C C 13 175.221 0.4 . 1 . . . A 40 GLN C . 25070 1 502 . 1 1 43 43 GLN CA C 13 55.517 0.40 . 1 . . . A 40 GLN CA . 25070 1 503 . 1 1 43 43 GLN CB C 13 30.278 0.40 . 1 . . . A 40 GLN CB . 25070 1 504 . 1 1 43 43 GLN CG C 13 34.702 0.40 . 1 . . . A 40 GLN CG . 25070 1 505 . 1 1 43 43 GLN N N 15 117.382 0.40 . 1 . . . A 40 GLN N . 25070 1 506 . 1 1 43 43 GLN NE2 N 15 109.521 0.04 . 1 . . . A 40 GLN NE2 . 25070 1 507 . 1 1 44 44 GLN H H 1 7.453 0.04 . 1 . . . A 41 GLN H . 25070 1 508 . 1 1 44 44 GLN HA H 1 4.080 0.04 . 1 . . . A 41 GLN HA . 25070 1 509 . 1 1 44 44 GLN HB2 H 1 1.954 0.04 . 2 . . . A 41 GLN HB2 . 25070 1 510 . 1 1 44 44 GLN HB3 H 1 1.827 0.04 . 2 . . . A 41 GLN HB3 . 25070 1 511 . 1 1 44 44 GLN HG2 H 1 1.584 0.04 . 2 . . . A 41 GLN HG2 . 25070 1 512 . 1 1 44 44 GLN HG3 H 1 2.513 0.04 . 2 . . . A 41 GLN HG3 . 25070 1 513 . 1 1 44 44 GLN C C 13 175.508 0.4 . 1 . . . A 41 GLN C . 25070 1 514 . 1 1 44 44 GLN CA C 13 56.774 0.40 . 1 . . . A 41 GLN CA . 25070 1 515 . 1 1 44 44 GLN CB C 13 30.787 0.40 . 1 . . . A 41 GLN CB . 25070 1 516 . 1 1 44 44 GLN CG C 13 33.403 0.40 . 1 . . . A 41 GLN CG . 25070 1 517 . 1 1 44 44 GLN N N 15 117.867 0.40 . 1 . . . A 41 GLN N . 25070 1 518 . 1 1 45 45 ARG H H 1 8.706 0.04 . 1 . . . A 42 ARG H . 25070 1 519 . 1 1 45 45 ARG HA H 1 4.464 0.04 . 1 . . . A 42 ARG HA . 25070 1 520 . 1 1 45 45 ARG HB2 H 1 1.888 0.04 . 2 . . . A 42 ARG HB2 . 25070 1 521 . 1 1 45 45 ARG HB3 H 1 1.603 0.04 . 2 . . . A 42 ARG HB3 . 25070 1 522 . 1 1 45 45 ARG HG2 H 1 1.575 0.04 . 2 . . . A 42 ARG HG2 . 25070 1 523 . 1 1 45 45 ARG HG3 H 1 1.308 0.04 . 2 . . . A 42 ARG HG3 . 25070 1 524 . 1 1 45 45 ARG HD2 H 1 3.041 0.04 . 2 . . . A 42 ARG HD2 . 25070 1 525 . 1 1 45 45 ARG HD3 H 1 2.845 0.04 . 2 . . . A 42 ARG HD3 . 25070 1 526 . 1 1 45 45 ARG C C 13 174.052 0.4 . 1 . . . A 42 ARG C . 25070 1 527 . 1 1 45 45 ARG CA C 13 55.288 0.40 . 1 . . . A 42 ARG CA . 25070 1 528 . 1 1 45 45 ARG CB C 13 32.241 0.40 . 1 . . . A 42 ARG CB . 25070 1 529 . 1 1 45 45 ARG CG C 13 26.436 0.40 . 1 . . . A 42 ARG CG . 25070 1 530 . 1 1 45 45 ARG CD C 13 45.434 0.40 . 1 . . . A 42 ARG CD . 25070 1 531 . 1 1 45 45 ARG N N 15 124.860 0.40 . 1 . . . A 42 ARG N . 25070 1 532 . 1 1 46 46 LEU H H 1 8.926 0.04 . 1 . . . A 43 LEU H . 25070 1 533 . 1 1 46 46 LEU HA H 1 5.368 0.04 . 1 . . . A 43 LEU HA . 25070 1 534 . 1 1 46 46 LEU HB2 H 1 1.084 0.04 . 2 . . . A 43 LEU HB2 . 25070 1 535 . 1 1 46 46 LEU HB3 H 1 1.596 0.04 . 2 . . . A 43 LEU HB3 . 25070 1 536 . 1 1 46 46 LEU HG H 1 1.449 0.04 . 1 . . . A 43 LEU HG . 25070 1 537 . 1 1 46 46 LEU HD11 H 1 0.766 0.04 . 1 . . . A 43 LEU HD11 . 25070 1 538 . 1 1 46 46 LEU HD12 H 1 0.766 0.04 . 1 . . . A 43 LEU HD12 . 25070 1 539 . 1 1 46 46 LEU HD13 H 1 0.766 0.04 . 1 . . . A 43 LEU HD13 . 25070 1 540 . 1 1 46 46 LEU HD21 H 1 0.730 0.04 . 1 . . . A 43 LEU HD21 . 25070 1 541 . 1 1 46 46 LEU HD22 H 1 0.730 0.04 . 1 . . . A 43 LEU HD22 . 25070 1 542 . 1 1 46 46 LEU HD23 H 1 0.730 0.04 . 1 . . . A 43 LEU HD23 . 25070 1 543 . 1 1 46 46 LEU C C 13 175.602 0.4 . 1 . . . A 43 LEU C . 25070 1 544 . 1 1 46 46 LEU CA C 13 53.272 0.40 . 1 . . . A 43 LEU CA . 25070 1 545 . 1 1 46 46 LEU CB C 13 45.274 0.40 . 1 . . . A 43 LEU CB . 25070 1 546 . 1 1 46 46 LEU CG C 13 27.010 0.40 . 1 . . . A 43 LEU CG . 25070 1 547 . 1 1 46 46 LEU CD1 C 13 24.232 0.40 . 1 . . . A 43 LEU CD1 . 25070 1 548 . 1 1 46 46 LEU CD2 C 13 26.547 0.40 . 1 . . . A 43 LEU CD2 . 25070 1 549 . 1 1 46 46 LEU N N 15 125.126 0.40 . 1 . . . A 43 LEU N . 25070 1 550 . 1 1 47 47 ILE H H 1 9.229 0.04 . 1 . . . A 44 ILE H . 25070 1 551 . 1 1 47 47 ILE HA H 1 5.112 0.04 . 1 . . . A 44 ILE HA . 25070 1 552 . 1 1 47 47 ILE HB H 1 1.728 0.04 . 1 . . . A 44 ILE HB . 25070 1 553 . 1 1 47 47 ILE HG12 H 1 1.272 0.04 . 2 . . . A 44 ILE HG12 . 25070 1 554 . 1 1 47 47 ILE HG13 H 1 1.146 0.04 . 2 . . . A 44 ILE HG13 . 25070 1 555 . 1 1 47 47 ILE HG21 H 1 0.670 0.04 . 1 . . . A 44 ILE HG21 . 25070 1 556 . 1 1 47 47 ILE HG22 H 1 0.670 0.04 . 1 . . . A 44 ILE HG22 . 25070 1 557 . 1 1 47 47 ILE HG23 H 1 0.670 0.04 . 1 . . . A 44 ILE HG23 . 25070 1 558 . 1 1 47 47 ILE HD11 H 1 0.702 0.04 . 1 . . . A 44 ILE HD11 . 25070 1 559 . 1 1 47 47 ILE HD12 H 1 0.702 0.04 . 1 . . . A 44 ILE HD12 . 25070 1 560 . 1 1 47 47 ILE HD13 H 1 0.702 0.04 . 1 . . . A 44 ILE HD13 . 25070 1 561 . 1 1 47 47 ILE C C 13 175.539 0.4 . 1 . . . A 44 ILE C . 25070 1 562 . 1 1 47 47 ILE CA C 13 58.541 0.40 . 1 . . . A 44 ILE CA . 25070 1 563 . 1 1 47 47 ILE CB C 13 41.357 0.40 . 1 . . . A 44 ILE CB . 25070 1 564 . 1 1 47 47 ILE CG1 C 13 27.973 0.40 . 1 . . . A 44 ILE CG1 . 25070 1 565 . 1 1 47 47 ILE CG2 C 13 17.442 0.40 . 1 . . . A 44 ILE CG2 . 25070 1 566 . 1 1 47 47 ILE CD1 C 13 13.597 0.40 . 1 . . . A 44 ILE CD1 . 25070 1 567 . 1 1 47 47 ILE N N 15 123.154 0.40 . 1 . . . A 44 ILE N . 25070 1 568 . 1 1 48 48 PHE H H 1 8.988 0.04 . 1 . . . A 45 PHE H . 25070 1 569 . 1 1 48 48 PHE HA H 1 4.993 0.04 . 1 . . . A 45 PHE HA . 25070 1 570 . 1 1 48 48 PHE HB2 H 1 3.096 0.04 . 2 . . . A 45 PHE HB2 . 25070 1 571 . 1 1 48 48 PHE HB3 H 1 2.725 0.04 . 2 . . . A 45 PHE HB3 . 25070 1 572 . 1 1 48 48 PHE C C 13 173.984 0.4 . 1 . . . A 45 PHE C . 25070 1 573 . 1 1 48 48 PHE CA C 13 57.392 0.40 . 1 . . . A 45 PHE CA . 25070 1 574 . 1 1 48 48 PHE CB C 13 44.079 0.40 . 1 . . . A 45 PHE CB . 25070 1 575 . 1 1 48 48 PHE N N 15 125.993 0.40 . 1 . . . A 45 PHE N . 25070 1 576 . 1 1 49 49 ALA H H 1 8.777 0.04 . 1 . . . A 46 ALA H . 25070 1 577 . 1 1 49 49 ALA HA H 1 3.676 0.04 . 1 . . . A 46 ALA HA . 25070 1 578 . 1 1 49 49 ALA HB1 H 1 0.836 0.04 . 1 . . . A 46 ALA HB1 . 25070 1 579 . 1 1 49 49 ALA HB2 H 1 0.836 0.04 . 1 . . . A 46 ALA HB2 . 25070 1 580 . 1 1 49 49 ALA HB3 H 1 0.836 0.04 . 1 . . . A 46 ALA HB3 . 25070 1 581 . 1 1 49 49 ALA C C 13 177.431 0.4 . 1 . . . A 46 ALA C . 25070 1 582 . 1 1 49 49 ALA CA C 13 52.448 0.40 . 1 . . . A 46 ALA CA . 25070 1 583 . 1 1 49 49 ALA CB C 13 16.765 0.40 . 1 . . . A 46 ALA CB . 25070 1 584 . 1 1 49 49 ALA N N 15 131.754 0.40 . 1 . . . A 46 ALA N . 25070 1 585 . 1 1 50 50 GLY H H 1 8.496 0.04 . 1 . . . A 47 GLY H . 25070 1 586 . 1 1 50 50 GLY HA2 H 1 3.304 0.04 . 2 . . . A 47 GLY HA2 . 25070 1 587 . 1 1 50 50 GLY HA3 H 1 4.070 0.04 . 2 . . . A 47 GLY HA3 . 25070 1 588 . 1 1 50 50 GLY C C 13 172.195 0.4 . 1 . . . A 47 GLY C . 25070 1 589 . 1 1 50 50 GLY CA C 13 46.215 0.40 . 1 . . . A 47 GLY CA . 25070 1 590 . 1 1 50 50 GLY N N 15 102.476 0.40 . 1 . . . A 47 GLY N . 25070 1 591 . 1 1 51 51 LYS H H 1 7.838 0.04 . 1 . . . A 48 LYS H . 25070 1 592 . 1 1 51 51 LYS HA H 1 4.650 0.04 . 1 . . . A 48 LYS HA . 25070 1 593 . 1 1 51 51 LYS HB2 H 1 1.834 0.04 . 2 . . . A 48 LYS HB2 . 25070 1 594 . 1 1 51 51 LYS HB3 H 1 1.838 0.04 . 2 . . . A 48 LYS HB3 . 25070 1 595 . 1 1 51 51 LYS HG2 H 1 1.511 0.04 . 2 . . . A 48 LYS HG2 . 25070 1 596 . 1 1 51 51 LYS HG3 H 1 1.511 0.04 . 2 . . . A 48 LYS HG3 . 25070 1 597 . 1 1 51 51 LYS HD2 H 1 1.883 0.04 . 2 . . . A 48 LYS HD2 . 25070 1 598 . 1 1 51 51 LYS HD3 H 1 1.830 0.04 . 2 . . . A 48 LYS HD3 . 25070 1 599 . 1 1 51 51 LYS HE2 H 1 3.128 0.04 . 2 . . . A 48 LYS HE2 . 25070 1 600 . 1 1 51 51 LYS HE3 H 1 3.164 0.04 . 2 . . . A 48 LYS HE3 . 25070 1 601 . 1 1 51 51 LYS C C 13 174.462 0.4 . 1 . . . A 48 LYS C . 25070 1 602 . 1 1 51 51 LYS CA C 13 54.347 0.40 . 1 . . . A 48 LYS CA . 25070 1 603 . 1 1 51 51 LYS CB C 13 35.224 0.40 . 1 . . . A 48 LYS CB . 25070 1 604 . 1 1 51 51 LYS CG C 13 24.339 0.40 . 1 . . . A 48 LYS CG . 25070 1 605 . 1 1 51 51 LYS CD C 13 29.193 0.40 . 1 . . . A 48 LYS CD . 25070 1 606 . 1 1 51 51 LYS CE C 13 42.199 0.40 . 1 . . . A 48 LYS CE . 25070 1 607 . 1 1 51 51 LYS N N 15 118.026 0.40 . 1 . . . A 48 LYS N . 25070 1 608 . 1 1 52 52 GLN H H 1 8.794 0.04 . 1 . . . A 49 GLN H . 25070 1 609 . 1 1 52 52 GLN HA H 1 4.781 0.04 . 1 . . . A 49 GLN HA . 25070 1 610 . 1 1 52 52 GLN HB2 H 1 1.999 0.04 . 2 . . . A 49 GLN HB2 . 25070 1 611 . 1 1 52 52 GLN HB3 H 1 1.999 0.04 . 2 . . . A 49 GLN HB3 . 25070 1 612 . 1 1 52 52 GLN HG2 H 1 2.014 0.04 . 2 . . . A 49 GLN HG2 . 25070 1 613 . 1 1 52 52 GLN HG3 H 1 2.223 0.04 . 2 . . . A 49 GLN HG3 . 25070 1 614 . 1 1 52 52 GLN C C 13 175.644 0.4 . 1 . . . A 49 GLN C . 25070 1 615 . 1 1 52 52 GLN CA C 13 54.761 0.40 . 1 . . . A 49 GLN CA . 25070 1 616 . 1 1 52 52 GLN CB C 13 30.450 0.40 . 1 . . . A 49 GLN CB . 25070 1 617 . 1 1 52 52 GLN CG C 13 35.335 0.40 . 1 . . . A 49 GLN CG . 25070 1 618 . 1 1 52 52 GLN N N 15 121.979 0.40 . 1 . . . A 49 GLN N . 25070 1 619 . 1 1 53 53 LEU H H 1 8.578 0.04 . 1 . . . A 50 LEU H . 25070 1 620 . 1 1 53 53 LEU HA H 1 3.995 0.04 . 1 . . . A 50 LEU HA . 25070 1 621 . 1 1 53 53 LEU HB2 H 1 1.435 0.04 . 2 . . . A 50 LEU HB2 . 25070 1 622 . 1 1 53 53 LEU HB3 H 1 1.009 0.04 . 2 . . . A 50 LEU HB3 . 25070 1 623 . 1 1 53 53 LEU HG H 1 1.386 0.04 . 1 . . . A 50 LEU HG . 25070 1 624 . 1 1 53 53 LEU HD11 H 1 0.497 0.04 . 1 . . . A 50 LEU HD11 . 25070 1 625 . 1 1 53 53 LEU HD12 H 1 0.497 0.04 . 1 . . . A 50 LEU HD12 . 25070 1 626 . 1 1 53 53 LEU HD13 H 1 0.497 0.04 . 1 . . . A 50 LEU HD13 . 25070 1 627 . 1 1 53 53 LEU HD21 H 1 -0.181 0.04 . 1 . . . A 50 LEU HD21 . 25070 1 628 . 1 1 53 53 LEU HD22 H 1 -0.181 0.04 . 1 . . . A 50 LEU HD22 . 25070 1 629 . 1 1 53 53 LEU HD23 H 1 -0.181 0.04 . 1 . . . A 50 LEU HD23 . 25070 1 630 . 1 1 53 53 LEU C C 13 176.618 0.4 . 1 . . . A 50 LEU C . 25070 1 631 . 1 1 53 53 LEU CA C 13 54.698 0.40 . 1 . . . A 50 LEU CA . 25070 1 632 . 1 1 53 53 LEU CB C 13 41.067 0.40 . 1 . . . A 50 LEU CB . 25070 1 633 . 1 1 53 53 LEU CG C 13 25.893 0.40 . 1 . . . A 50 LEU CG . 25070 1 634 . 1 1 53 53 LEU CD1 C 13 25.947 0.40 . 1 . . . A 50 LEU CD1 . 25070 1 635 . 1 1 53 53 LEU CD2 C 13 19.364 0.40 . 1 . . . A 50 LEU CD2 . 25070 1 636 . 1 1 53 53 LEU N N 15 126.623 0.40 . 1 . . . A 50 LEU N . 25070 1 637 . 1 1 54 54 GLU H H 1 8.413 0.04 . 1 . . . A 51 GLU H . 25070 1 638 . 1 1 54 54 GLU HA H 1 4.498 0.04 . 1 . . . A 51 GLU HA . 25070 1 639 . 1 1 54 54 GLU HB2 H 1 2.197 0.04 . 2 . . . A 51 GLU HB2 . 25070 1 640 . 1 1 54 54 GLU HB3 H 1 1.933 0.04 . 2 . . . A 51 GLU HB3 . 25070 1 641 . 1 1 54 54 GLU HG2 H 1 2.439 0.04 . 2 . . . A 51 GLU HG2 . 25070 1 642 . 1 1 54 54 GLU HG3 H 1 2.354 0.04 . 2 . . . A 51 GLU HG3 . 25070 1 643 . 1 1 54 54 GLU C C 13 175.448 0.4 . 1 . . . A 51 GLU C . 25070 1 644 . 1 1 54 54 GLU CA C 13 55.734 0.40 . 1 . . . A 51 GLU CA . 25070 1 645 . 1 1 54 54 GLU CB C 13 32.008 0.40 . 1 . . . A 51 GLU CB . 25070 1 646 . 1 1 54 54 GLU CG C 13 36.295 0.40 . 1 . . . A 51 GLU CG . 25070 1 647 . 1 1 54 54 GLU N N 15 123.491 0.40 . 1 . . . A 51 GLU N . 25070 1 648 . 1 1 55 55 ASP H H 1 8.177 0.04 . 1 . . . A 52 ASP H . 25070 1 649 . 1 1 55 55 ASP HA H 1 4.338 0.04 . 1 . . . A 52 ASP HA . 25070 1 650 . 1 1 55 55 ASP HB2 H 1 2.582 0.04 . 2 . . . A 52 ASP HB2 . 25070 1 651 . 1 1 55 55 ASP HB3 H 1 2.495 0.04 . 2 . . . A 52 ASP HB3 . 25070 1 652 . 1 1 55 55 ASP CA C 13 56.735 0.40 . 1 . . . A 52 ASP CA . 25070 1 653 . 1 1 55 55 ASP CB C 13 40.710 0.40 . 1 . . . A 52 ASP CB . 25070 1 654 . 1 1 55 55 ASP N N 15 120.516 0.40 . 1 . . . A 52 ASP N . 25070 1 655 . 1 1 56 56 GLY HA2 H 1 4.037 0.04 . 2 . . . A 53 GLY HA2 . 25070 1 656 . 1 1 56 56 GLY HA3 H 1 4.008 0.04 . 2 . . . A 53 GLY HA3 . 25070 1 657 . 1 1 56 56 GLY C C 13 174.769 0.4 . 1 . . . A 53 GLY C . 25070 1 658 . 1 1 56 56 GLY CA C 13 45.178 0.40 . 1 . . . A 53 GLY CA . 25070 1 659 . 1 1 57 57 ARG H H 1 7.469 0.04 . 1 . . . A 54 ARG H . 25070 1 660 . 1 1 57 57 ARG HA H 1 4.691 0.04 . 1 . . . A 54 ARG HA . 25070 1 661 . 1 1 57 57 ARG HB2 H 1 2.042 0.04 . 2 . . . A 54 ARG HB2 . 25070 1 662 . 1 1 57 57 ARG HB3 H 1 2.215 0.04 . 2 . . . A 54 ARG HB3 . 25070 1 663 . 1 1 57 57 ARG HG2 H 1 1.798 0.04 . 2 . . . A 54 ARG HG2 . 25070 1 664 . 1 1 57 57 ARG HG3 H 1 1.590 0.04 . 2 . . . A 54 ARG HG3 . 25070 1 665 . 1 1 57 57 ARG HD2 H 1 3.107 0.04 . 2 . . . A 54 ARG HD2 . 25070 1 666 . 1 1 57 57 ARG HD3 H 1 3.042 0.04 . 2 . . . A 54 ARG HD3 . 25070 1 667 . 1 1 57 57 ARG C C 13 175.346 0.4 . 1 . . . A 54 ARG C . 25070 1 668 . 1 1 57 57 ARG CA C 13 54.363 0.40 . 1 . . . A 54 ARG CA . 25070 1 669 . 1 1 57 57 ARG CB C 13 32.727 0.40 . 1 . . . A 54 ARG CB . 25070 1 670 . 1 1 57 57 ARG CG C 13 27.489 0.40 . 1 . . . A 54 ARG CG . 25070 1 671 . 1 1 57 57 ARG CD C 13 43.141 0.40 . 1 . . . A 54 ARG CD . 25070 1 672 . 1 1 57 57 ARG N N 15 119.448 0.40 . 1 . . . A 54 ARG N . 25070 1 673 . 1 1 58 58 THR H H 1 8.861 0.04 . 1 . . . A 55 THR H . 25070 1 674 . 1 1 58 58 THR HA H 1 5.214 0.04 . 1 . . . A 55 THR HA . 25070 1 675 . 1 1 58 58 THR HB H 1 4.492 0.04 . 1 . . . A 55 THR HB . 25070 1 676 . 1 1 58 58 THR HG21 H 1 1.099 0.04 . 1 . . . A 55 THR HG21 . 25070 1 677 . 1 1 58 58 THR HG22 H 1 1.099 0.04 . 1 . . . A 55 THR HG22 . 25070 1 678 . 1 1 58 58 THR HG23 H 1 1.099 0.04 . 1 . . . A 55 THR HG23 . 25070 1 679 . 1 1 58 58 THR C C 13 176.503 0.4 . 1 . . . A 55 THR C . 25070 1 680 . 1 1 58 58 THR CA C 13 59.748 0.40 . 1 . . . A 55 THR CA . 25070 1 681 . 1 1 58 58 THR CB C 13 72.442 0.40 . 1 . . . A 55 THR CB . 25070 1 682 . 1 1 58 58 THR CG2 C 13 22.103 0.40 . 1 . . . A 55 THR CG2 . 25070 1 683 . 1 1 58 58 THR N N 15 108.975 0.40 . 1 . . . A 55 THR N . 25070 1 684 . 1 1 59 59 LEU H H 1 8.210 0.04 . 1 . . . A 56 LEU H . 25070 1 685 . 1 1 59 59 LEU HA H 1 4.027 0.04 . 1 . . . A 56 LEU HA . 25070 1 686 . 1 1 59 59 LEU HB2 H 1 1.154 0.04 . 2 . . . A 56 LEU HB2 . 25070 1 687 . 1 1 59 59 LEU HB3 H 1 2.078 0.04 . 2 . . . A 56 LEU HB3 . 25070 1 688 . 1 1 59 59 LEU HG H 1 1.712 0.04 . 1 . . . A 56 LEU HG . 25070 1 689 . 1 1 59 59 LEU HD11 H 1 0.591 0.04 . 1 . . . A 56 LEU HD11 . 25070 1 690 . 1 1 59 59 LEU HD12 H 1 0.591 0.04 . 1 . . . A 56 LEU HD12 . 25070 1 691 . 1 1 59 59 LEU HD13 H 1 0.591 0.04 . 1 . . . A 56 LEU HD13 . 25070 1 692 . 1 1 59 59 LEU HD21 H 1 0.738 0.04 . 1 . . . A 56 LEU HD21 . 25070 1 693 . 1 1 59 59 LEU HD22 H 1 0.738 0.04 . 1 . . . A 56 LEU HD22 . 25070 1 694 . 1 1 59 59 LEU HD23 H 1 0.738 0.04 . 1 . . . A 56 LEU HD23 . 25070 1 695 . 1 1 59 59 LEU C C 13 180.695 0.4 . 1 . . . A 56 LEU C . 25070 1 696 . 1 1 59 59 LEU CA C 13 58.627 0.40 . 1 . . . A 56 LEU CA . 25070 1 697 . 1 1 59 59 LEU CB C 13 40.250 0.40 . 1 . . . A 56 LEU CB . 25070 1 698 . 1 1 59 59 LEU CG C 13 26.540 0.40 . 1 . . . A 56 LEU CG . 25070 1 699 . 1 1 59 59 LEU CD1 C 13 23.041 0.40 . 1 . . . A 56 LEU CD1 . 25070 1 700 . 1 1 59 59 LEU CD2 C 13 26.908 0.40 . 1 . . . A 56 LEU CD2 . 25070 1 701 . 1 1 59 59 LEU N N 15 117.898 0.40 . 1 . . . A 56 LEU N . 25070 1 702 . 1 1 60 60 SER H H 1 8.346 0.04 . 1 . . . A 57 SER H . 25070 1 703 . 1 1 60 60 SER HA H 1 4.228 0.04 . 1 . . . A 57 SER HA . 25070 1 704 . 1 1 60 60 SER HB2 H 1 3.725 0.04 . 2 . . . A 57 SER HB2 . 25070 1 705 . 1 1 60 60 SER HB3 H 1 3.815 0.04 . 2 . . . A 57 SER HB3 . 25070 1 706 . 1 1 60 60 SER C C 13 178.231 0.4 . 1 . . . A 57 SER C . 25070 1 707 . 1 1 60 60 SER CA C 13 61.123 0.40 . 1 . . . A 57 SER CA . 25070 1 708 . 1 1 60 60 SER CB C 13 62.379 0.40 . 1 . . . A 57 SER CB . 25070 1 709 . 1 1 60 60 SER N N 15 113.360 0.40 . 1 . . . A 57 SER N . 25070 1 710 . 1 1 61 61 ASP H H 1 7.934 0.04 . 1 . . . A 58 ASP H . 25070 1 711 . 1 1 61 61 ASP HA H 1 4.257 0.04 . 1 . . . A 58 ASP HA . 25070 1 712 . 1 1 61 61 ASP HB2 H 1 2.991 0.04 . 2 . . . A 58 ASP HB2 . 25070 1 713 . 1 1 61 61 ASP HB3 H 1 2.265 0.04 . 2 . . . A 58 ASP HB3 . 25070 1 714 . 1 1 61 61 ASP C C 13 177.422 0.4 . 1 . . . A 58 ASP C . 25070 1 715 . 1 1 61 61 ASP CA C 13 57.406 0.40 . 1 . . . A 58 ASP CA . 25070 1 716 . 1 1 61 61 ASP CB C 13 40.387 0.40 . 1 . . . A 58 ASP CB . 25070 1 717 . 1 1 61 61 ASP N N 15 124.637 0.40 . 1 . . . A 58 ASP N . 25070 1 718 . 1 1 62 62 TYR H H 1 7.251 0.04 . 1 . . . A 59 TYR H . 25070 1 719 . 1 1 62 62 TYR HA H 1 4.630 0.04 . 1 . . . A 59 TYR HA . 25070 1 720 . 1 1 62 62 TYR HB2 H 1 3.475 0.04 . 2 . . . A 59 TYR HB2 . 25070 1 721 . 1 1 62 62 TYR HB3 H 1 2.512 0.04 . 2 . . . A 59 TYR HB3 . 25070 1 722 . 1 1 62 62 TYR C C 13 174.684 0.4 . 1 . . . A 59 TYR C . 25070 1 723 . 1 1 62 62 TYR CA C 13 58.393 0.40 . 1 . . . A 59 TYR CA . 25070 1 724 . 1 1 62 62 TYR CB C 13 40.033 0.40 . 1 . . . A 59 TYR CB . 25070 1 725 . 1 1 62 62 TYR N N 15 115.716 0.40 . 1 . . . A 59 TYR N . 25070 1 726 . 1 1 63 63 ASN H H 1 8.158 0.04 . 1 . . . A 60 ASN H . 25070 1 727 . 1 1 63 63 ASN HA H 1 4.335 0.04 . 1 . . . A 60 ASN HA . 25070 1 728 . 1 1 63 63 ASN HB2 H 1 3.304 0.04 . 2 . . . A 60 ASN HB2 . 25070 1 729 . 1 1 63 63 ASN HB3 H 1 2.788 0.04 . 2 . . . A 60 ASN HB3 . 25070 1 730 . 1 1 63 63 ASN HD21 H 1 7.572 0.04 . 1 . . . A 60 ASN HD21 . 25070 1 731 . 1 1 63 63 ASN HD22 H 1 6.827 0.04 . 2 . . . A 60 ASN HD22 . 25070 1 732 . 1 1 63 63 ASN C C 13 174.293 0.4 . 1 . . . A 60 ASN C . 25070 1 733 . 1 1 63 63 ASN CA C 13 54.207 0.40 . 1 . . . A 60 ASN CA . 25070 1 734 . 1 1 63 63 ASN CB C 13 37.415 0.40 . 1 . . . A 60 ASN CB . 25070 1 735 . 1 1 63 63 ASN N N 15 115.950 0.40 . 1 . . . A 60 ASN N . 25070 1 736 . 1 1 63 63 ASN ND2 N 15 111.244 0.04 . 1 . . . A 60 ASN ND2 . 25070 1 737 . 1 1 64 64 ILE H H 1 7.288 0.04 . 1 . . . A 61 ILE H . 25070 1 738 . 1 1 64 64 ILE HA H 1 3.345 0.04 . 1 . . . A 61 ILE HA . 25070 1 739 . 1 1 64 64 ILE HB H 1 1.350 0.04 . 1 . . . A 61 ILE HB . 25070 1 740 . 1 1 64 64 ILE HG12 H 1 -0.502 0.04 . 2 . . . A 61 ILE HG12 . 25070 1 741 . 1 1 64 64 ILE HG13 H 1 1.097 0.04 . 2 . . . A 61 ILE HG13 . 25070 1 742 . 1 1 64 64 ILE HG21 H 1 0.449 0.04 . 1 . . . A 61 ILE HG21 . 25070 1 743 . 1 1 64 64 ILE HG22 H 1 0.449 0.04 . 1 . . . A 61 ILE HG22 . 25070 1 744 . 1 1 64 64 ILE HG23 H 1 0.449 0.04 . 1 . . . A 61 ILE HG23 . 25070 1 745 . 1 1 64 64 ILE HD11 H 1 0.403 0.04 . 1 . . . A 61 ILE HD11 . 25070 1 746 . 1 1 64 64 ILE HD12 H 1 0.403 0.04 . 1 . . . A 61 ILE HD12 . 25070 1 747 . 1 1 64 64 ILE HD13 H 1 0.403 0.04 . 1 . . . A 61 ILE HD13 . 25070 1 748 . 1 1 64 64 ILE C C 13 174.354 0.4 . 1 . . . A 61 ILE C . 25070 1 749 . 1 1 64 64 ILE CA C 13 62.785 0.40 . 1 . . . A 61 ILE CA . 25070 1 750 . 1 1 64 64 ILE CB C 13 36.807 0.40 . 1 . . . A 61 ILE CB . 25070 1 751 . 1 1 64 64 ILE CG1 C 13 28.594 0.40 . 1 . . . A 61 ILE CG1 . 25070 1 752 . 1 1 64 64 ILE CG2 C 13 17.467 0.40 . 1 . . . A 61 ILE CG2 . 25070 1 753 . 1 1 64 64 ILE CD1 C 13 14.674 0.40 . 1 . . . A 61 ILE CD1 . 25070 1 754 . 1 1 64 64 ILE N N 15 119.182 0.40 . 1 . . . A 61 ILE N . 25070 1 755 . 1 1 65 65 GLN H H 1 7.639 0.04 . 1 . . . A 62 GLN H . 25070 1 756 . 1 1 65 65 GLN HA H 1 4.473 0.04 . 1 . . . A 62 GLN HA . 25070 1 757 . 1 1 65 65 GLN HB2 H 1 2.214 0.04 . 2 . . . A 62 GLN HB2 . 25070 1 758 . 1 1 65 65 GLN HB3 H 1 1.844 0.04 . 2 . . . A 62 GLN HB3 . 25070 1 759 . 1 1 65 65 GLN HG2 H 1 2.322 0.04 . 2 . . . A 62 GLN HG2 . 25070 1 760 . 1 1 65 65 GLN HG3 H 1 2.264 0.04 . 2 . . . A 62 GLN HG3 . 25070 1 761 . 1 1 65 65 GLN HE21 H 1 6.820 0.04 . 1 . . . A 62 GLN HE21 . 25070 1 762 . 1 1 65 65 GLN HE22 H 1 7.295 0.04 . 2 . . . A 62 GLN HE22 . 25070 1 763 . 1 1 65 65 GLN C C 13 175.499 0.4 . 1 . . . A 62 GLN C . 25070 1 764 . 1 1 65 65 GLN CA C 13 53.560 0.40 . 1 . . . A 62 GLN CA . 25070 1 765 . 1 1 65 65 GLN CB C 13 31.788 0.40 . 1 . . . A 62 GLN CB . 25070 1 766 . 1 1 65 65 GLN CG C 13 33.559 0.40 . 1 . . . A 62 GLN CG . 25070 1 767 . 1 1 65 65 GLN N N 15 125.061 0.40 . 1 . . . A 62 GLN N . 25070 1 768 . 1 1 65 65 GLN NE2 N 15 112.030 0.04 . 1 . . . A 62 GLN NE2 . 25070 1 769 . 1 1 66 66 LYS H H 1 8.435 0.04 . 1 . . . A 63 LYS H . 25070 1 770 . 1 1 66 66 LYS HA H 1 3.925 0.04 . 1 . . . A 63 LYS HA . 25070 1 771 . 1 1 66 66 LYS HB2 H 1 2.013 0.04 . 2 . . . A 63 LYS HB2 . 25070 1 772 . 1 1 66 66 LYS HB3 H 1 1.850 0.04 . 2 . . . A 63 LYS HB3 . 25070 1 773 . 1 1 66 66 LYS HG2 H 1 1.497 0.04 . 2 . . . A 63 LYS HG2 . 25070 1 774 . 1 1 66 66 LYS HG3 H 1 1.464 0.04 . 2 . . . A 63 LYS HG3 . 25070 1 775 . 1 1 66 66 LYS HD2 H 1 1.720 0.04 . 2 . . . A 63 LYS HD2 . 25070 1 776 . 1 1 66 66 LYS HD3 H 1 1.720 0.04 . 2 . . . A 63 LYS HD3 . 25070 1 777 . 1 1 66 66 LYS HE2 H 1 3.012 0.04 . 2 . . . A 63 LYS HE2 . 25070 1 778 . 1 1 66 66 LYS HE3 H 1 3.012 0.04 . 2 . . . A 63 LYS HE3 . 25070 1 779 . 1 1 66 66 LYS C C 13 176.002 0.4 . 1 . . . A 63 LYS C . 25070 1 780 . 1 1 66 66 LYS CA C 13 58.170 0.40 . 1 . . . A 63 LYS CA . 25070 1 781 . 1 1 66 66 LYS CB C 13 32.554 0.40 . 1 . . . A 63 LYS CB . 25070 1 782 . 1 1 66 66 LYS CG C 13 24.277 0.40 . 1 . . . A 63 LYS CG . 25070 1 783 . 1 1 66 66 LYS CD C 13 29.748 0.40 . 1 . . . A 63 LYS CD . 25070 1 784 . 1 1 66 66 LYS CE C 13 42.282 0.40 . 1 . . . A 63 LYS CE . 25070 1 785 . 1 1 66 66 LYS N N 15 120.334 0.40 . 1 . . . A 63 LYS N . 25070 1 786 . 1 1 67 67 GLU H H 1 9.287 0.04 . 1 . . . A 64 GLU H . 25070 1 787 . 1 1 67 67 GLU HA H 1 3.320 0.04 . 1 . . . A 64 GLU HA . 25070 1 788 . 1 1 67 67 GLU HB2 H 1 2.503 0.04 . 2 . . . A 64 GLU HB2 . 25070 1 789 . 1 1 67 67 GLU HB3 H 1 2.370 0.04 . 2 . . . A 64 GLU HB3 . 25070 1 790 . 1 1 67 67 GLU HG2 H 1 2.228 0.04 . 2 . . . A 64 GLU HG2 . 25070 1 791 . 1 1 67 67 GLU HG3 H 1 2.197 0.04 . 2 . . . A 64 GLU HG3 . 25070 1 792 . 1 1 67 67 GLU C C 13 175.195 0.4 . 1 . . . A 64 GLU C . 25070 1 793 . 1 1 67 67 GLU CA C 13 58.469 0.40 . 1 . . . A 64 GLU CA . 25070 1 794 . 1 1 67 67 GLU CB C 13 26.047 0.40 . 1 . . . A 64 GLU CB . 25070 1 795 . 1 1 67 67 GLU CG C 13 37.458 0.40 . 1 . . . A 64 GLU CG . 25070 1 796 . 1 1 67 67 GLU N N 15 115.237 0.40 . 1 . . . A 64 GLU N . 25070 1 797 . 1 1 68 68 SER H H 1 7.759 0.04 . 1 . . . A 65 SER H . 25070 1 798 . 1 1 68 68 SER HA H 1 4.580 0.04 . 1 . . . A 65 SER HA . 25070 1 799 . 1 1 68 68 SER HB2 H 1 3.868 0.04 . 2 . . . A 65 SER HB2 . 25070 1 800 . 1 1 68 68 SER HB3 H 1 3.618 0.04 . 2 . . . A 65 SER HB3 . 25070 1 801 . 1 1 68 68 SER C C 13 171.967 0.4 . 1 . . . A 65 SER C . 25070 1 802 . 1 1 68 68 SER CA C 13 61.101 0.40 . 1 . . . A 65 SER CA . 25070 1 803 . 1 1 68 68 SER CB C 13 64.915 0.40 . 1 . . . A 65 SER CB . 25070 1 804 . 1 1 68 68 SER N N 15 115.316 0.40 . 1 . . . A 65 SER N . 25070 1 805 . 1 1 69 69 THR H H 1 8.676 0.04 . 1 . . . A 66 THR H . 25070 1 806 . 1 1 69 69 THR HA H 1 5.248 0.04 . 1 . . . A 66 THR HA . 25070 1 807 . 1 1 69 69 THR HB H 1 3.994 0.04 . 1 . . . A 66 THR HB . 25070 1 808 . 1 1 69 69 THR HG21 H 1 0.840 0.04 . 1 . . . A 66 THR HG21 . 25070 1 809 . 1 1 69 69 THR HG22 H 1 0.840 0.04 . 1 . . . A 66 THR HG22 . 25070 1 810 . 1 1 69 69 THR HG23 H 1 0.840 0.04 . 1 . . . A 66 THR HG23 . 25070 1 811 . 1 1 69 69 THR C C 13 173.440 0.4 . 1 . . . A 66 THR C . 25070 1 812 . 1 1 69 69 THR CA C 13 62.453 0.40 . 1 . . . A 66 THR CA . 25070 1 813 . 1 1 69 69 THR CB C 13 70.381 0.40 . 1 . . . A 66 THR CB . 25070 1 814 . 1 1 69 69 THR CG2 C 13 21.103 0.40 . 1 . . . A 66 THR CG2 . 25070 1 815 . 1 1 69 69 THR N N 15 117.579 0.40 . 1 . . . A 66 THR N . 25070 1 816 . 1 1 70 70 LEU H H 1 9.337 0.04 . 1 . . . A 67 LEU H . 25070 1 817 . 1 1 70 70 LEU HA H 1 4.984 0.04 . 1 . . . A 67 LEU HA . 25070 1 818 . 1 1 70 70 LEU HB2 H 1 1.583 0.04 . 2 . . . A 67 LEU HB2 . 25070 1 819 . 1 1 70 70 LEU HB3 H 1 1.583 0.04 . 2 . . . A 67 LEU HB3 . 25070 1 820 . 1 1 70 70 LEU HG H 1 1.704 0.04 . 1 . . . A 67 LEU HG . 25070 1 821 . 1 1 70 70 LEU HD11 H 1 0.566 0.04 . 1 . . . A 67 LEU HD11 . 25070 1 822 . 1 1 70 70 LEU HD12 H 1 0.566 0.04 . 1 . . . A 67 LEU HD12 . 25070 1 823 . 1 1 70 70 LEU HD13 H 1 0.566 0.04 . 1 . . . A 67 LEU HD13 . 25070 1 824 . 1 1 70 70 LEU HD21 H 1 0.634 0.04 . 1 . . . A 67 LEU HD21 . 25070 1 825 . 1 1 70 70 LEU HD22 H 1 0.634 0.04 . 1 . . . A 67 LEU HD22 . 25070 1 826 . 1 1 70 70 LEU HD23 H 1 0.634 0.04 . 1 . . . A 67 LEU HD23 . 25070 1 827 . 1 1 70 70 LEU C C 13 175.134 0.4 . 1 . . . A 67 LEU C . 25070 1 828 . 1 1 70 70 LEU CA C 13 53.969 0.40 . 1 . . . A 67 LEU CA . 25070 1 829 . 1 1 70 70 LEU CB C 13 44.366 0.40 . 1 . . . A 67 LEU CB . 25070 1 830 . 1 1 70 70 LEU CG C 13 29.731 0.40 . 1 . . . A 67 LEU CG . 25070 1 831 . 1 1 70 70 LEU CD1 C 13 25.556 0.40 . 1 . . . A 67 LEU CD1 . 25070 1 832 . 1 1 70 70 LEU CD2 C 13 24.717 0.40 . 1 . . . A 67 LEU CD2 . 25070 1 833 . 1 1 70 70 LEU N N 15 127.831 0.40 . 1 . . . A 67 LEU N . 25070 1 834 . 1 1 71 71 HIS H H 1 9.125 0.04 . 1 . . . A 68 HIS H . 25070 1 835 . 1 1 71 71 HIS HA H 1 5.332 0.04 . 1 . . . A 68 HIS HA . 25070 1 836 . 1 1 71 71 HIS HB2 H 1 2.870 0.04 . 2 . . . A 68 HIS HB2 . 25070 1 837 . 1 1 71 71 HIS HB3 H 1 2.827 0.04 . 2 . . . A 68 HIS HB3 . 25070 1 838 . 1 1 71 71 HIS CA C 13 56.481 0.40 . 1 . . . A 68 HIS CA . 25070 1 839 . 1 1 71 71 HIS CB C 13 32.569 0.40 . 1 . . . A 68 HIS CB . 25070 1 840 . 1 1 71 71 HIS N N 15 119.168 0.40 . 1 . . . A 68 HIS N . 25070 1 841 . 1 1 72 72 LEU H H 1 8.516 0.04 . 1 . . . A 69 LEU H . 25070 1 842 . 1 1 72 72 LEU HA H 1 5.091 0.04 . 1 . . . A 69 LEU HA . 25070 1 843 . 1 1 72 72 LEU HB2 H 1 1.414 0.04 . 2 . . . A 69 LEU HB2 . 25070 1 844 . 1 1 72 72 LEU HB3 H 1 1.022 0.04 . 2 . . . A 69 LEU HB3 . 25070 1 845 . 1 1 72 72 LEU HG H 1 1.250 0.04 . 1 . . . A 69 LEU HG . 25070 1 846 . 1 1 72 72 LEU HD11 H 1 0.753 0.04 . 1 . . . A 69 LEU HD11 . 25070 1 847 . 1 1 72 72 LEU HD12 H 1 0.753 0.04 . 1 . . . A 69 LEU HD12 . 25070 1 848 . 1 1 72 72 LEU HD13 H 1 0.753 0.04 . 1 . . . A 69 LEU HD13 . 25070 1 849 . 1 1 72 72 LEU HD21 H 1 0.653 0.04 . 1 . . . A 69 LEU HD21 . 25070 1 850 . 1 1 72 72 LEU HD22 H 1 0.653 0.04 . 1 . . . A 69 LEU HD22 . 25070 1 851 . 1 1 72 72 LEU HD23 H 1 0.653 0.04 . 1 . . . A 69 LEU HD23 . 25070 1 852 . 1 1 72 72 LEU C C 13 174.275 0.4 . 1 . . . A 69 LEU C . 25070 1 853 . 1 1 72 72 LEU CA C 13 53.534 0.40 . 1 . . . A 69 LEU CA . 25070 1 854 . 1 1 72 72 LEU CB C 13 44.574 0.40 . 1 . . . A 69 LEU CB . 25070 1 855 . 1 1 72 72 LEU CG C 13 27.640 0.40 . 1 . . . A 69 LEU CG . 25070 1 856 . 1 1 72 72 LEU CD1 C 13 23.311 0.40 . 1 . . . A 69 LEU CD1 . 25070 1 857 . 1 1 72 72 LEU CD2 C 13 26.026 0.40 . 1 . . . A 69 LEU CD2 . 25070 1 858 . 1 1 72 72 LEU N N 15 124.015 0.40 . 1 . . . A 69 LEU N . 25070 1 859 . 1 1 73 73 VAL H H 1 9.221 0.04 . 1 . . . A 70 VAL H . 25070 1 860 . 1 1 73 73 VAL HA H 1 4.118 0.04 . 1 . . . A 70 VAL HA . 25070 1 861 . 1 1 73 73 VAL HB H 1 1.863 0.04 . 1 . . . A 70 VAL HB . 25070 1 862 . 1 1 73 73 VAL HG11 H 1 0.892 0.04 . 1 . . . A 70 VAL HG11 . 25070 1 863 . 1 1 73 73 VAL HG12 H 1 0.892 0.04 . 1 . . . A 70 VAL HG12 . 25070 1 864 . 1 1 73 73 VAL HG13 H 1 0.892 0.04 . 1 . . . A 70 VAL HG13 . 25070 1 865 . 1 1 73 73 VAL HG21 H 1 0.909 0.04 . 1 . . . A 70 VAL HG21 . 25070 1 866 . 1 1 73 73 VAL HG22 H 1 0.909 0.04 . 1 . . . A 70 VAL HG22 . 25070 1 867 . 1 1 73 73 VAL HG23 H 1 0.909 0.04 . 1 . . . A 70 VAL HG23 . 25070 1 868 . 1 1 73 73 VAL C C 13 173.580 0.4 . 1 . . . A 70 VAL C . 25070 1 869 . 1 1 73 73 VAL CA C 13 61.357 0.40 . 1 . . . A 70 VAL CA . 25070 1 870 . 1 1 73 73 VAL CB C 13 34.702 0.40 . 1 . . . A 70 VAL CB . 25070 1 871 . 1 1 73 73 VAL CG1 C 13 21.507 0.40 . 1 . . . A 70 VAL CG1 . 25070 1 872 . 1 1 73 73 VAL CG2 C 13 21.506 0.40 . 1 . . . A 70 VAL CG2 . 25070 1 873 . 1 1 73 73 VAL N N 15 129.337 0.40 . 1 . . . A 70 VAL N . 25070 1 874 . 1 1 74 74 LEU H H 1 8.465 0.04 . 1 . . . A 71 LEU H . 25070 1 875 . 1 1 74 74 LEU HA H 1 5.112 0.04 . 1 . . . A 71 LEU HA . 25070 1 876 . 1 1 74 74 LEU HB2 H 1 1.705 0.04 . 2 . . . A 71 LEU HB2 . 25070 1 877 . 1 1 74 74 LEU HB3 H 1 1.462 0.04 . 2 . . . A 71 LEU HB3 . 25070 1 878 . 1 1 74 74 LEU HG H 1 1.654 0.04 . 1 . . . A 71 LEU HG . 25070 1 879 . 1 1 74 74 LEU HD11 H 1 0.801 0.04 . 1 . . . A 71 LEU HD11 . 25070 1 880 . 1 1 74 74 LEU HD12 H 1 0.801 0.04 . 1 . . . A 71 LEU HD12 . 25070 1 881 . 1 1 74 74 LEU HD13 H 1 0.801 0.04 . 1 . . . A 71 LEU HD13 . 25070 1 882 . 1 1 74 74 LEU HD21 H 1 0.924 0.04 . 1 . . . A 71 LEU HD21 . 25070 1 883 . 1 1 74 74 LEU HD22 H 1 0.924 0.04 . 1 . . . A 71 LEU HD22 . 25070 1 884 . 1 1 74 74 LEU HD23 H 1 0.924 0.04 . 1 . . . A 71 LEU HD23 . 25070 1 885 . 1 1 74 74 LEU C C 13 177.924 0.4 . 1 . . . A 71 LEU C . 25070 1 886 . 1 1 74 74 LEU CA C 13 53.799 0.40 . 1 . . . A 71 LEU CA . 25070 1 887 . 1 1 74 74 LEU CB C 13 42.032 0.40 . 1 . . . A 71 LEU CB . 25070 1 888 . 1 1 74 74 LEU CG C 13 28.023 0.40 . 1 . . . A 71 LEU CG . 25070 1 889 . 1 1 74 74 LEU CD1 C 13 24.382 0.40 . 1 . . . A 71 LEU CD1 . 25070 1 890 . 1 1 74 74 LEU CD2 C 13 24.938 0.40 . 1 . . . A 71 LEU CD2 . 25070 1 891 . 1 1 74 74 LEU N N 15 126.166 0.40 . 1 . . . A 71 LEU N . 25070 1 892 . 1 1 75 75 ARG H H 1 8.975 0.04 . 1 . . . A 72 ARG H . 25070 1 893 . 1 1 75 75 ARG HA H 1 4.315 0.04 . 1 . . . A 72 ARG HA . 25070 1 894 . 1 1 75 75 ARG HB2 H 1 1.501 0.04 . 2 . . . A 72 ARG HB2 . 25070 1 895 . 1 1 75 75 ARG HB3 H 1 1.744 0.04 . 2 . . . A 72 ARG HB3 . 25070 1 896 . 1 1 75 75 ARG HG2 H 1 1.454 0.04 . 2 . . . A 72 ARG HG2 . 25070 1 897 . 1 1 75 75 ARG HG3 H 1 1.454 0.04 . 2 . . . A 72 ARG HG3 . 25070 1 898 . 1 1 75 75 ARG HD2 H 1 3.091 0.04 . 2 . . . A 72 ARG HD2 . 25070 1 899 . 1 1 75 75 ARG HD3 H 1 3.091 0.04 . 2 . . . A 72 ARG HD3 . 25070 1 900 . 1 1 75 75 ARG C C 13 175.200 0.4 . 1 . . . A 72 ARG C . 25070 1 901 . 1 1 75 75 ARG CA C 13 56.108 0.40 . 1 . . . A 72 ARG CA . 25070 1 902 . 1 1 75 75 ARG CB C 13 31.412 0.40 . 1 . . . A 72 ARG CB . 25070 1 903 . 1 1 75 75 ARG CG C 13 27.709 0.40 . 1 . . . A 72 ARG CG . 25070 1 904 . 1 1 75 75 ARG CD C 13 43.752 0.40 . 1 . . . A 72 ARG CD . 25070 1 905 . 1 1 75 75 ARG N N 15 124.879 0.40 . 1 . . . A 72 ARG N . 25070 1 906 . 1 1 76 76 LEU H H 1 8.168 0.04 . 1 . . . A 73 LEU H . 25070 1 907 . 1 1 76 76 LEU HA H 1 4.360 0.04 . 1 . . . A 73 LEU HA . 25070 1 908 . 1 1 76 76 LEU HB2 H 1 1.607 0.04 . 2 . . . A 73 LEU HB2 . 25070 1 909 . 1 1 76 76 LEU HB3 H 1 1.536 0.04 . 2 . . . A 73 LEU HB3 . 25070 1 910 . 1 1 76 76 LEU HG H 1 1.592 0.04 . 1 . . . A 73 LEU HG . 25070 1 911 . 1 1 76 76 LEU HD11 H 1 0.850 0.04 . 1 . . . A 73 LEU HD11 . 25070 1 912 . 1 1 76 76 LEU HD12 H 1 0.850 0.04 . 1 . . . A 73 LEU HD12 . 25070 1 913 . 1 1 76 76 LEU HD13 H 1 0.850 0.04 . 1 . . . A 73 LEU HD13 . 25070 1 914 . 1 1 76 76 LEU HD21 H 1 0.913 0.04 . 1 . . . A 73 LEU HD21 . 25070 1 915 . 1 1 76 76 LEU HD22 H 1 0.913 0.04 . 1 . . . A 73 LEU HD22 . 25070 1 916 . 1 1 76 76 LEU HD23 H 1 0.913 0.04 . 1 . . . A 73 LEU HD23 . 25070 1 917 . 1 1 76 76 LEU C C 13 177.545 0.4 . 1 . . . A 73 LEU C . 25070 1 918 . 1 1 76 76 LEU CA C 13 54.862 0.40 . 1 . . . A 73 LEU CA . 25070 1 919 . 1 1 76 76 LEU CB C 13 42.349 0.40 . 1 . . . A 73 LEU CB . 25070 1 920 . 1 1 76 76 LEU CG C 13 27.317 0.40 . 1 . . . A 73 LEU CG . 25070 1 921 . 1 1 76 76 LEU CD1 C 13 23.372 0.40 . 1 . . . A 73 LEU CD1 . 25070 1 922 . 1 1 76 76 LEU CD2 C 13 24.999 0.40 . 1 . . . A 73 LEU CD2 . 25070 1 923 . 1 1 76 76 LEU N N 15 123.827 0.40 . 1 . . . A 73 LEU N . 25070 1 924 . 1 1 77 77 ARG H H 1 8.502 0.04 . 1 . . . A 74 ARG H . 25070 1 925 . 1 1 77 77 ARG HA H 1 4.256 0.04 . 1 . . . A 74 ARG HA . 25070 1 926 . 1 1 77 77 ARG HB2 H 1 1.743 0.04 . 2 . . . A 74 ARG HB2 . 25070 1 927 . 1 1 77 77 ARG HB3 H 1 1.816 0.04 . 2 . . . A 74 ARG HB3 . 25070 1 928 . 1 1 77 77 ARG HG2 H 1 1.579 0.04 . 2 . . . A 74 ARG HG2 . 25070 1 929 . 1 1 77 77 ARG HG3 H 1 1.628 0.04 . 2 . . . A 74 ARG HG3 . 25070 1 930 . 1 1 77 77 ARG HD2 H 1 3.164 0.04 . 2 . . . A 74 ARG HD2 . 25070 1 931 . 1 1 77 77 ARG HD3 H 1 3.164 0.04 . 2 . . . A 74 ARG HD3 . 25070 1 932 . 1 1 77 77 ARG C C 13 176.848 0.4 . 1 . . . A 74 ARG C . 25070 1 933 . 1 1 77 77 ARG CA C 13 56.534 0.40 . 1 . . . A 74 ARG CA . 25070 1 934 . 1 1 77 77 ARG CB C 13 30.710 0.40 . 1 . . . A 74 ARG CB . 25070 1 935 . 1 1 77 77 ARG CG C 13 27.100 0.40 . 1 . . . A 74 ARG CG . 25070 1 936 . 1 1 77 77 ARG CD C 13 43.309 0.40 . 1 . . . A 74 ARG CD . 25070 1 937 . 1 1 77 77 ARG N N 15 122.614 0.40 . 1 . . . A 74 ARG N . 25070 1 938 . 1 1 78 78 GLY H H 1 8.506 0.04 . 1 . . . A 75 GLY H . 25070 1 939 . 1 1 78 78 GLY HA2 H 1 3.940 0.04 . 2 . . . A 75 GLY HA2 . 25070 1 940 . 1 1 78 78 GLY HA3 H 1 3.940 0.04 . 2 . . . A 75 GLY HA3 . 25070 1 941 . 1 1 78 78 GLY C C 13 173.625 0.4 . 1 . . . A 75 GLY C . 25070 1 942 . 1 1 78 78 GLY CA C 13 45.276 0.40 . 1 . . . A 75 GLY CA . 25070 1 943 . 1 1 78 78 GLY N N 15 111.362 0.40 . 1 . . . A 75 GLY N . 25070 1 944 . 1 1 79 79 GLY H H 1 7.938 0.04 . 1 . . . A 76 GLY H . 25070 1 945 . 1 1 79 79 GLY N N 15 115.178 0.40 . 1 . . . A 76 GLY N . 25070 1 946 . 2 2 4 4 GLN H H 1 8.471 0.04 . 1 . . . . 198 GLN H . 25070 1 947 . 2 2 4 4 GLN HA H 1 4.366 0.04 . 1 . . . . 198 GLN HA . 25070 1 948 . 2 2 4 4 GLN HB2 H 1 2.049 0.04 . 2 . . . . 198 GLN HB2 . 25070 1 949 . 2 2 4 4 GLN HB3 H 1 1.969 0.04 . 2 . . . . 198 GLN HB3 . 25070 1 950 . 2 2 4 4 GLN HG2 H 1 2.339 0.04 . 2 . . . . 198 GLN HG2 . 25070 1 951 . 2 2 4 4 GLN HG3 H 1 2.339 0.04 . 2 . . . . 198 GLN HG3 . 25070 1 952 . 2 2 4 4 GLN HE21 H 1 7.509 0.04 . 1 . . . . 198 GLN HE21 . 25070 1 953 . 2 2 4 4 GLN HE22 H 1 6.872 0.04 . 2 . . . . 198 GLN HE22 . 25070 1 954 . 2 2 4 4 GLN C C 13 175.756 0.4 . 1 . . . . 198 GLN C . 25070 1 955 . 2 2 4 4 GLN CA C 13 55.730 0.40 . 1 . . . . 198 GLN CA . 25070 1 956 . 2 2 4 4 GLN CB C 13 29.582 0.40 . 1 . . . . 198 GLN CB . 25070 1 957 . 2 2 4 4 GLN CG C 13 33.822 0.40 . 1 . . . . 198 GLN CG . 25070 1 958 . 2 2 4 4 GLN N N 15 122.569 0.40 . 1 . . . . 198 GLN N . 25070 1 959 . 2 2 4 4 GLN NE2 N 15 112.315 0.04 . 1 . . . . 198 GLN NE2 . 25070 1 960 . 2 2 5 5 VAL H H 1 8.319 0.04 . 1 . . . . 199 VAL H . 25070 1 961 . 2 2 5 5 VAL HA H 1 4.194 0.04 . 1 . . . . 199 VAL HA . 25070 1 962 . 2 2 5 5 VAL HB H 1 2.079 0.04 . 1 . . . . 199 VAL HB . 25070 1 963 . 2 2 5 5 VAL HG11 H 1 0.946 0.04 . 1 . . . . 199 VAL HG1 . 25070 1 964 . 2 2 5 5 VAL HG12 H 1 0.946 0.04 . 1 . . . . 199 VAL HG1 . 25070 1 965 . 2 2 5 5 VAL HG13 H 1 0.946 0.04 . 1 . . . . 199 VAL HG1 . 25070 1 966 . 2 2 5 5 VAL HG21 H 1 0.946 0.04 . 1 . . . . 199 VAL HG2 . 25070 1 967 . 2 2 5 5 VAL HG22 H 1 0.946 0.04 . 1 . . . . 199 VAL HG2 . 25070 1 968 . 2 2 5 5 VAL HG23 H 1 0.946 0.04 . 1 . . . . 199 VAL HG2 . 25070 1 969 . 2 2 5 5 VAL C C 13 175.972 0.4 . 1 . . . . 199 VAL C . 25070 1 970 . 2 2 5 5 VAL CA C 13 62.116 0.40 . 1 . . . . 199 VAL CA . 25070 1 971 . 2 2 5 5 VAL CB C 13 32.936 0.40 . 1 . . . . 199 VAL CB . 25070 1 972 . 2 2 5 5 VAL CG1 C 13 20.675 0.40 . 1 . . . . 199 VAL CG1 . 25070 1 973 . 2 2 5 5 VAL CG2 C 13 20.675 0.40 . 1 . . . . 199 VAL CG2 . 25070 1 974 . 2 2 5 5 VAL N N 15 122.497 0.40 . 1 . . . . 199 VAL N . 25070 1 975 . 2 2 6 6 THR H H 1 8.544 0.04 . 1 . . . . 200 THR H . 25070 1 976 . 2 2 6 6 THR HA H 1 4.266 0.04 . 1 . . . . 200 THR HA . 25070 1 977 . 2 2 6 6 THR HB H 1 4.102 0.04 . 1 . . . . 200 THR HB . 25070 1 978 . 2 2 6 6 THR HG21 H 1 1.167 0.04 . 1 . . . . 200 THR HG2 . 25070 1 979 . 2 2 6 6 THR HG22 H 1 1.167 0.04 . 1 . . . . 200 THR HG2 . 25070 1 980 . 2 2 6 6 THR HG23 H 1 1.167 0.04 . 1 . . . . 200 THR HG2 . 25070 1 981 . 2 2 6 6 THR C C 13 174.141 0.4 . 1 . . . . 200 THR C . 25070 1 982 . 2 2 6 6 THR CA C 13 62.854 0.40 . 1 . . . . 200 THR CA . 25070 1 983 . 2 2 6 6 THR CB C 13 69.548 0.40 . 1 . . . . 200 THR CB . 25070 1 984 . 2 2 6 6 THR CG2 C 13 22.077 0.40 . 1 . . . . 200 THR CG2 . 25070 1 985 . 2 2 6 6 THR N N 15 121.902 0.40 . 1 . . . . 200 THR N . 25070 1 986 . 2 2 7 7 LYS H H 1 8.658 0.04 . 1 . . . . 201 LYS H . 25070 1 987 . 2 2 7 7 LYS HA H 1 4.824 0.04 . 1 . . . . 201 LYS HA . 25070 1 988 . 2 2 7 7 LYS HB2 H 1 1.555 0.04 . 2 . . . . 201 LYS HB2 . 25070 1 989 . 2 2 7 7 LYS HB3 H 1 1.618 0.04 . 2 . . . . 201 LYS HB3 . 25070 1 990 . 2 2 7 7 LYS HG2 H 1 0.951 0.04 . 2 . . . . 201 LYS HG2 . 25070 1 991 . 2 2 7 7 LYS HG3 H 1 1.448 0.04 . 2 . . . . 201 LYS HG3 . 25070 1 992 . 2 2 7 7 LYS HD2 H 1 1.474 0.04 . 2 . . . . 201 LYS HD2 . 25070 1 993 . 2 2 7 7 LYS HD3 H 1 1.474 0.04 . 2 . . . . 201 LYS HD3 . 25070 1 994 . 2 2 7 7 LYS HE2 H 1 2.801 0.04 . 2 . . . . 201 LYS HE2 . 25070 1 995 . 2 2 7 7 LYS HE3 H 1 2.788 0.04 . 2 . . . . 201 LYS HE3 . 25070 1 996 . 2 2 7 7 LYS C C 13 175.287 0.4 . 1 . . . . 201 LYS C . 25070 1 997 . 2 2 7 7 LYS CA C 13 55.287 0.40 . 1 . . . . 201 LYS CA . 25070 1 998 . 2 2 7 7 LYS CB C 13 34.871 0.40 . 1 . . . . 201 LYS CB . 25070 1 999 . 2 2 7 7 LYS CG C 13 25.347 0.40 . 1 . . . . 201 LYS CG . 25070 1 1000 . 2 2 7 7 LYS CD C 13 29.064 0.40 . 1 . . . . 201 LYS CD . 25070 1 1001 . 2 2 7 7 LYS CE C 13 42.139 0.40 . 1 . . . . 201 LYS CE . 25070 1 1002 . 2 2 7 7 LYS N N 15 126.406 0.40 . 1 . . . . 201 LYS N . 25070 1 1003 . 2 2 8 8 VAL H H 1 9.049 0.04 . 1 . . . . 202 VAL H . 25070 1 1004 . 2 2 8 8 VAL HA H 1 4.562 0.04 . 1 . . . . 202 VAL HA . 25070 1 1005 . 2 2 8 8 VAL HB H 1 2.130 0.04 . 1 . . . . 202 VAL HB . 25070 1 1006 . 2 2 8 8 VAL HG11 H 1 0.683 0.04 . 1 . . . . 202 VAL HG1 . 25070 1 1007 . 2 2 8 8 VAL HG12 H 1 0.683 0.04 . 1 . . . . 202 VAL HG1 . 25070 1 1008 . 2 2 8 8 VAL HG13 H 1 0.683 0.04 . 1 . . . . 202 VAL HG1 . 25070 1 1009 . 2 2 8 8 VAL HG21 H 1 0.785 0.04 . 1 . . . . 202 VAL HG2 . 25070 1 1010 . 2 2 8 8 VAL HG22 H 1 0.785 0.04 . 1 . . . . 202 VAL HG2 . 25070 1 1011 . 2 2 8 8 VAL HG23 H 1 0.785 0.04 . 1 . . . . 202 VAL HG2 . 25070 1 1012 . 2 2 8 8 VAL C C 13 172.829 0.4 . 1 . . . . 202 VAL C . 25070 1 1013 . 2 2 8 8 VAL CA C 13 58.397 0.40 . 1 . . . . 202 VAL CA . 25070 1 1014 . 2 2 8 8 VAL CB C 13 35.361 0.40 . 1 . . . . 202 VAL CB . 25070 1 1015 . 2 2 8 8 VAL CG1 C 13 18.271 0.40 . 1 . . . . 202 VAL CG1 . 25070 1 1016 . 2 2 8 8 VAL CG2 C 13 22.081 0.40 . 1 . . . . 202 VAL CG2 . 25070 1 1017 . 2 2 8 8 VAL N N 15 115.133 0.40 . 1 . . . . 202 VAL N . 25070 1 1018 . 2 2 9 9 ASP H H 1 8.241 0.04 . 1 . . . . 203 ASP H . 25070 1 1019 . 2 2 9 9 ASP HA H 1 5.196 0.04 . 1 . . . . 203 ASP HA . 25070 1 1020 . 2 2 9 9 ASP HB2 H 1 2.071 0.04 . 2 . . . . 203 ASP HB2 . 25070 1 1021 . 2 2 9 9 ASP HB3 H 1 2.319 0.04 . 2 . . . . 203 ASP HB3 . 25070 1 1022 . 2 2 9 9 ASP C C 13 176.176 0.4 . 1 . . . . 203 ASP C . 25070 1 1023 . 2 2 9 9 ASP CA C 13 52.027 0.40 . 1 . . . . 203 ASP CA . 25070 1 1024 . 2 2 9 9 ASP CB C 13 41.041 0.40 . 1 . . . . 203 ASP CB . 25070 1 1025 . 2 2 9 9 ASP N N 15 120.131 0.40 . 1 . . . . 203 ASP N . 25070 1 1026 . 2 2 10 10 CYS H H 1 8.959 0.04 . 1 . . . . 204 CYS H . 25070 1 1027 . 2 2 10 10 CYS HA H 1 4.288 0.04 . 1 . . . . 204 CYS HA . 25070 1 1028 . 2 2 10 10 CYS HB2 H 1 2.410 0.04 . 2 . . . . 204 CYS HB2 . 25070 1 1029 . 2 2 10 10 CYS HB3 H 1 3.112 0.04 . 2 . . . . 204 CYS HB3 . 25070 1 1030 . 2 2 10 10 CYS CA C 13 57.180 0.40 . 1 . . . . 204 CYS CA . 25070 1 1031 . 2 2 10 10 CYS CB C 13 30.632 0.40 . 1 . . . . 204 CYS CB . 25070 1 1032 . 2 2 10 10 CYS N N 15 126.182 0.40 . 1 . . . . 204 CYS N . 25070 1 1033 . 2 2 11 11 PRO HA H 1 4.151 0.04 . 1 . . . . 205 PRO HA . 25070 1 1034 . 2 2 11 11 PRO HB2 H 1 1.275 0.04 . 2 . . . . 205 PRO HB2 . 25070 1 1035 . 2 2 11 11 PRO HB3 H 1 1.596 0.04 . 2 . . . . 205 PRO HB3 . 25070 1 1036 . 2 2 11 11 PRO HG2 H 1 1.679 0.04 . 2 . . . . 205 PRO HG2 . 25070 1 1037 . 2 2 11 11 PRO HG3 H 1 1.679 0.04 . 2 . . . . 205 PRO HG3 . 25070 1 1038 . 2 2 11 11 PRO HD2 H 1 4.135 0.04 . 2 . . . . 205 PRO HD2 . 25070 1 1039 . 2 2 11 11 PRO HD3 H 1 3.836 0.04 . 2 . . . . 205 PRO HD3 . 25070 1 1040 . 2 2 11 11 PRO C C 13 175.274 0.4 . 1 . . . . 205 PRO C . 25070 1 1041 . 2 2 11 11 PRO CA C 13 63.745 0.40 . 1 . . . . 205 PRO CA . 25070 1 1042 . 2 2 11 11 PRO CB C 13 31.217 0.40 . 1 . . . . 205 PRO CB . 25070 1 1043 . 2 2 11 11 PRO CG C 13 26.816 0.40 . 1 . . . . 205 PRO CG . 25070 1 1044 . 2 2 11 11 PRO CD C 13 50.506 0.40 . 1 . . . . 205 PRO CD . 25070 1 1045 . 2 2 12 12 VAL H H 1 9.503 0.04 . 1 . . . . 206 VAL H . 25070 1 1046 . 2 2 12 12 VAL HA H 1 3.819 0.04 . 1 . . . . 206 VAL HA . 25070 1 1047 . 2 2 12 12 VAL HB H 1 2.514 0.04 . 1 . . . . 206 VAL HB . 25070 1 1048 . 2 2 12 12 VAL HG11 H 1 0.810 0.04 . 1 . . . . 206 VAL HG1 . 25070 1 1049 . 2 2 12 12 VAL HG12 H 1 0.810 0.04 . 1 . . . . 206 VAL HG1 . 25070 1 1050 . 2 2 12 12 VAL HG13 H 1 0.810 0.04 . 1 . . . . 206 VAL HG1 . 25070 1 1051 . 2 2 12 12 VAL HG21 H 1 0.656 0.04 . 1 . . . . 206 VAL HG2 . 25070 1 1052 . 2 2 12 12 VAL HG22 H 1 0.656 0.04 . 1 . . . . 206 VAL HG2 . 25070 1 1053 . 2 2 12 12 VAL HG23 H 1 0.656 0.04 . 1 . . . . 206 VAL HG2 . 25070 1 1054 . 2 2 12 12 VAL C C 13 176.797 0.4 . 1 . . . . 206 VAL C . 25070 1 1055 . 2 2 12 12 VAL CA C 13 64.952 0.40 . 1 . . . . 206 VAL CA . 25070 1 1056 . 2 2 12 12 VAL CB C 13 32.282 0.40 . 1 . . . . 206 VAL CB . 25070 1 1057 . 2 2 12 12 VAL CG1 C 13 22.277 0.40 . 1 . . . . 206 VAL CG1 . 25070 1 1058 . 2 2 12 12 VAL CG2 C 13 22.053 0.40 . 1 . . . . 206 VAL CG2 . 25070 1 1059 . 2 2 12 12 VAL N N 15 124.265 0.40 . 1 . . . . 206 VAL N . 25070 1 1060 . 2 2 13 13 CYS H H 1 8.421 0.04 . 1 . . . . 207 CYS H . 25070 1 1061 . 2 2 13 13 CYS HA H 1 4.879 0.04 . 1 . . . . 207 CYS HA . 25070 1 1062 . 2 2 13 13 CYS HB2 H 1 2.499 0.04 . 2 . . . . 207 CYS HB2 . 25070 1 1063 . 2 2 13 13 CYS HB3 H 1 3.207 0.04 . 2 . . . . 207 CYS HB3 . 25070 1 1064 . 2 2 13 13 CYS C C 13 177.094 0.4 . 1 . . . . 207 CYS C . 25070 1 1065 . 2 2 13 13 CYS CA C 13 58.752 0.40 . 1 . . . . 207 CYS CA . 25070 1 1066 . 2 2 13 13 CYS CB C 13 32.508 0.40 . 1 . . . . 207 CYS CB . 25070 1 1067 . 2 2 13 13 CYS N N 15 118.345 0.40 . 1 . . . . 207 CYS N . 25070 1 1068 . 2 2 14 14 GLY H H 1 7.822 0.04 . 1 . . . . 208 GLY H . 25070 1 1069 . 2 2 14 14 GLY HA2 H 1 3.717 0.04 . 2 . . . . 208 GLY HA2 . 25070 1 1070 . 2 2 14 14 GLY HA3 H 1 4.089 0.04 . 2 . . . . 208 GLY HA3 . 25070 1 1071 . 2 2 14 14 GLY C C 13 173.543 0.4 . 1 . . . . 208 GLY C . 25070 1 1072 . 2 2 14 14 GLY CA C 13 46.117 0.40 . 1 . . . . 208 GLY CA . 25070 1 1073 . 2 2 14 14 GLY N N 15 113.039 0.40 . 1 . . . . 208 GLY N . 25070 1 1074 . 2 2 15 15 VAL H H 1 8.170 0.04 . 1 . . . . 209 VAL H . 25070 1 1075 . 2 2 15 15 VAL HA H 1 3.931 0.04 . 1 . . . . 209 VAL HA . 25070 1 1076 . 2 2 15 15 VAL HB H 1 2.035 0.04 . 1 . . . . 209 VAL HB . 25070 1 1077 . 2 2 15 15 VAL HG11 H 1 0.858 0.04 . 1 . . . . 209 VAL HG1 . 25070 1 1078 . 2 2 15 15 VAL HG12 H 1 0.858 0.04 . 1 . . . . 209 VAL HG1 . 25070 1 1079 . 2 2 15 15 VAL HG13 H 1 0.858 0.04 . 1 . . . . 209 VAL HG1 . 25070 1 1080 . 2 2 15 15 VAL HG21 H 1 0.707 0.04 . 1 . . . . 209 VAL HG2 . 25070 1 1081 . 2 2 15 15 VAL HG22 H 1 0.707 0.04 . 1 . . . . 209 VAL HG2 . 25070 1 1082 . 2 2 15 15 VAL HG23 H 1 0.707 0.04 . 1 . . . . 209 VAL HG2 . 25070 1 1083 . 2 2 15 15 VAL C C 13 173.147 0.4 . 1 . . . . 209 VAL C . 25070 1 1084 . 2 2 15 15 VAL CA C 13 63.236 0.40 . 1 . . . . 209 VAL CA . 25070 1 1085 . 2 2 15 15 VAL CB C 13 31.910 0.40 . 1 . . . . 209 VAL CB . 25070 1 1086 . 2 2 15 15 VAL CG1 C 13 22.044 0.40 . 1 . . . . 209 VAL CG1 . 25070 1 1087 . 2 2 15 15 VAL CG2 C 13 21.082 0.40 . 1 . . . . 209 VAL CG2 . 25070 1 1088 . 2 2 15 15 VAL N N 15 122.128 0.40 . 1 . . . . 209 VAL N . 25070 1 1089 . 2 2 16 16 ASN H H 1 8.157 0.04 . 1 . . . . 210 ASN H . 25070 1 1090 . 2 2 16 16 ASN HA H 1 5.305 0.04 . 1 . . . . 210 ASN HA . 25070 1 1091 . 2 2 16 16 ASN HB2 H 1 2.507 0.04 . 2 . . . . 210 ASN HB2 . 25070 1 1092 . 2 2 16 16 ASN HB3 H 1 2.741 0.04 . 2 . . . . 210 ASN HB3 . 25070 1 1093 . 2 2 16 16 ASN HD21 H 1 7.790 0.04 . 1 . . . . 210 ASN HD21 . 25070 1 1094 . 2 2 16 16 ASN HD22 H 1 6.384 0.04 . 2 . . . . 210 ASN HD22 . 25070 1 1095 . 2 2 16 16 ASN C C 13 174.827 0.4 . 1 . . . . 210 ASN C . 25070 1 1096 . 2 2 16 16 ASN CA C 13 53.727 0.40 . 1 . . . . 210 ASN CA . 25070 1 1097 . 2 2 16 16 ASN CB C 13 41.088 0.40 . 1 . . . . 210 ASN CB . 25070 1 1098 . 2 2 16 16 ASN N N 15 125.100 0.40 . 1 . . . . 210 ASN N . 25070 1 1099 . 2 2 16 16 ASN ND2 N 15 111.169 0.04 . 1 . . . . 210 ASN ND2 . 25070 1 1100 . 2 2 17 17 ILE H H 1 9.296 0.04 . 1 . . . . 211 ILE H . 25070 1 1101 . 2 2 17 17 ILE HA H 1 4.800 0.04 . 1 . . . . 211 ILE HA . 25070 1 1102 . 2 2 17 17 ILE HB H 1 1.697 0.04 . 1 . . . . 211 ILE HB . 25070 1 1103 . 2 2 17 17 ILE HG12 H 1 1.034 0.04 . 2 . . . . 211 ILE HG12 . 25070 1 1104 . 2 2 17 17 ILE HG13 H 1 1.034 0.04 . 2 . . . . 211 ILE HG13 . 25070 1 1105 . 2 2 17 17 ILE HG21 H 1 0.737 0.04 . 1 . . . . 211 ILE HG2 . 25070 1 1106 . 2 2 17 17 ILE HG22 H 1 0.737 0.04 . 1 . . . . 211 ILE HG2 . 25070 1 1107 . 2 2 17 17 ILE HG23 H 1 0.737 0.04 . 1 . . . . 211 ILE HG2 . 25070 1 1108 . 2 2 17 17 ILE HD11 H 1 0.379 0.04 . 1 . . . . 211 ILE HD1 . 25070 1 1109 . 2 2 17 17 ILE HD12 H 1 0.379 0.04 . 1 . . . . 211 ILE HD1 . 25070 1 1110 . 2 2 17 17 ILE HD13 H 1 0.379 0.04 . 1 . . . . 211 ILE HD1 . 25070 1 1111 . 2 2 17 17 ILE CA C 13 57.771 0.40 . 1 . . . . 211 ILE CA . 25070 1 1112 . 2 2 17 17 ILE CB C 13 41.806 0.40 . 1 . . . . 211 ILE CB . 25070 1 1113 . 2 2 17 17 ILE CG1 C 13 25.322 0.40 . 1 . . . . 211 ILE CG1 . 25070 1 1114 . 2 2 17 17 ILE CG2 C 13 17.662 0.40 . 1 . . . . 211 ILE CG2 . 25070 1 1115 . 2 2 17 17 ILE CD1 C 13 13.015 0.40 . 1 . . . . 211 ILE CD1 . 25070 1 1116 . 2 2 17 17 ILE N N 15 124.695 0.40 . 1 . . . . 211 ILE N . 25070 1 1117 . 2 2 18 18 PRO HA H 1 4.493 0.04 . 1 . . . . 212 PRO HA . 25070 1 1118 . 2 2 18 18 PRO HB2 H 1 2.230 0.04 . 2 . . . . 212 PRO HB2 . 25070 1 1119 . 2 2 18 18 PRO HB3 H 1 1.624 0.04 . 2 . . . . 212 PRO HB3 . 25070 1 1120 . 2 2 18 18 PRO HG2 H 1 1.693 0.04 . 2 . . . . 212 PRO HG2 . 25070 1 1121 . 2 2 18 18 PRO HG3 H 1 1.857 0.04 . 2 . . . . 212 PRO HG3 . 25070 1 1122 . 2 2 18 18 PRO HD2 H 1 3.408 0.04 . 2 . . . . 212 PRO HD2 . 25070 1 1123 . 2 2 18 18 PRO HD3 H 1 3.772 0.04 . 2 . . . . 212 PRO HD3 . 25070 1 1124 . 2 2 18 18 PRO C C 13 178.137 0.4 . 1 . . . . 212 PRO C . 25070 1 1125 . 2 2 18 18 PRO CA C 13 63.370 0.40 . 1 . . . . 212 PRO CA . 25070 1 1126 . 2 2 18 18 PRO CB C 13 31.943 0.40 . 1 . . . . 212 PRO CB . 25070 1 1127 . 2 2 18 18 PRO CG C 13 28.476 0.40 . 1 . . . . 212 PRO CG . 25070 1 1128 . 2 2 18 18 PRO CD C 13 50.915 0.40 . 1 . . . . 212 PRO CD . 25070 1 1129 . 2 2 19 19 GLU H H 1 8.964 0.04 . 1 . . . . 213 GLU H . 25070 1 1130 . 2 2 19 19 GLU HA H 1 3.758 0.04 . 1 . . . . 213 GLU HA . 25070 1 1131 . 2 2 19 19 GLU HB2 H 1 2.015 0.04 . 2 . . . . 213 GLU HB2 . 25070 1 1132 . 2 2 19 19 GLU HB3 H 1 1.875 0.04 . 2 . . . . 213 GLU HB3 . 25070 1 1133 . 2 2 19 19 GLU HG2 H 1 2.278 0.04 . 2 . . . . 213 GLU HG2 . 25070 1 1134 . 2 2 19 19 GLU HG3 H 1 2.167 0.04 . 2 . . . . 213 GLU HG3 . 25070 1 1135 . 2 2 19 19 GLU C C 13 178.381 0.4 . 1 . . . . 213 GLU C . 25070 1 1136 . 2 2 19 19 GLU CA C 13 59.968 0.40 . 1 . . . . 213 GLU CA . 25070 1 1137 . 2 2 19 19 GLU CB C 13 29.493 0.40 . 1 . . . . 213 GLU CB . 25070 1 1138 . 2 2 19 19 GLU CG C 13 35.968 0.40 . 1 . . . . 213 GLU CG . 25070 1 1139 . 2 2 19 19 GLU N N 15 126.299 0.40 . 1 . . . . 213 GLU N . 25070 1 1140 . 2 2 20 20 SER H H 1 8.312 0.04 . 1 . . . . 214 SER H . 25070 1 1141 . 2 2 20 20 SER HA H 1 4.215 0.04 . 1 . . . . 214 SER HA . 25070 1 1142 . 2 2 20 20 SER HB2 H 1 4.019 0.04 . 2 . . . . 214 SER HB2 . 25070 1 1143 . 2 2 20 20 SER HB3 H 1 3.930 0.04 . 2 . . . . 214 SER HB3 . 25070 1 1144 . 2 2 20 20 SER C C 13 175.479 0.4 . 1 . . . . 214 SER C . 25070 1 1145 . 2 2 20 20 SER CA C 13 60.183 0.40 . 1 . . . . 214 SER CA . 25070 1 1146 . 2 2 20 20 SER CB C 13 62.620 0.40 . 1 . . . . 214 SER CB . 25070 1 1147 . 2 2 20 20 SER N N 15 112.128 0.40 . 1 . . . . 214 SER N . 25070 1 1148 . 2 2 21 21 HIS H H 1 8.109 0.04 . 1 . . . . 215 HIS H . 25070 1 1149 . 2 2 21 21 HIS HA H 1 4.987 0.04 . 1 . . . . 215 HIS HA . 25070 1 1150 . 2 2 21 21 HIS HB2 H 1 3.397 0.04 . 2 . . . . 215 HIS HB2 . 25070 1 1151 . 2 2 21 21 HIS HB3 H 1 2.984 0.04 . 2 . . . . 215 HIS HB3 . 25070 1 1152 . 2 2 21 21 HIS C C 13 176.980 0.4 . 1 . . . . 215 HIS C . 25070 1 1153 . 2 2 21 21 HIS CA C 13 55.335 0.40 . 1 . . . . 215 HIS CA . 25070 1 1154 . 2 2 21 21 HIS CB C 13 32.531 0.40 . 1 . . . . 215 HIS CB . 25070 1 1155 . 2 2 21 21 HIS N N 15 120.226 0.40 . 1 . . . . 215 HIS N . 25070 1 1156 . 2 2 22 22 ILE H H 1 7.576 0.04 . 1 . . . . 216 ILE H . 25070 1 1157 . 2 2 22 22 ILE HA H 1 4.141 0.04 . 1 . . . . 216 ILE HA . 25070 1 1158 . 2 2 22 22 ILE HB H 1 1.784 0.04 . 1 . . . . 216 ILE HB . 25070 1 1159 . 2 2 22 22 ILE HG12 H 1 1.330 0.04 . 2 . . . . 216 ILE HG12 . 25070 1 1160 . 2 2 22 22 ILE HG13 H 1 1.452 0.04 . 2 . . . . 216 ILE HG13 . 25070 1 1161 . 2 2 22 22 ILE HG21 H 1 1.142 0.04 . 1 . . . . 216 ILE HG2 . 25070 1 1162 . 2 2 22 22 ILE HG22 H 1 1.142 0.04 . 1 . . . . 216 ILE HG2 . 25070 1 1163 . 2 2 22 22 ILE HG23 H 1 1.142 0.04 . 1 . . . . 216 ILE HG2 . 25070 1 1164 . 2 2 22 22 ILE HD11 H 1 0.929 0.04 . 1 . . . . 216 ILE HD1 . 25070 1 1165 . 2 2 22 22 ILE HD12 H 1 0.929 0.04 . 1 . . . . 216 ILE HD1 . 25070 1 1166 . 2 2 22 22 ILE HD13 H 1 0.929 0.04 . 1 . . . . 216 ILE HD1 . 25070 1 1167 . 2 2 22 22 ILE C C 13 175.534 0.4 . 1 . . . . 216 ILE C . 25070 1 1168 . 2 2 22 22 ILE CA C 13 62.250 0.40 . 1 . . . . 216 ILE CA . 25070 1 1169 . 2 2 22 22 ILE CB C 13 38.160 0.40 . 1 . . . . 216 ILE CB . 25070 1 1170 . 2 2 22 22 ILE CG1 C 13 29.594 0.40 . 1 . . . . 216 ILE CG1 . 25070 1 1171 . 2 2 22 22 ILE CG2 C 13 19.172 0.40 . 1 . . . . 216 ILE CG2 . 25070 1 1172 . 2 2 22 22 ILE CD1 C 13 13.693 0.40 . 1 . . . . 216 ILE CD1 . 25070 1 1173 . 2 2 22 22 ILE N N 15 119.955 0.40 . 1 . . . . 216 ILE N . 25070 1 1174 . 2 2 23 23 ASN H H 1 8.467 0.04 . 1 . . . . 217 ASN H . 25070 1 1175 . 2 2 23 23 ASN HA H 1 4.292 0.04 . 1 . . . . 217 ASN HA . 25070 1 1176 . 2 2 23 23 ASN HB2 H 1 2.526 0.04 . 2 . . . . 217 ASN HB2 . 25070 1 1177 . 2 2 23 23 ASN HB3 H 1 2.771 0.04 . 2 . . . . 217 ASN HB3 . 25070 1 1178 . 2 2 23 23 ASN C C 13 176.857 0.4 . 1 . . . . 217 ASN C . 25070 1 1179 . 2 2 23 23 ASN CA C 13 58.829 0.40 . 1 . . . . 217 ASN CA . 25070 1 1180 . 2 2 23 23 ASN CB C 13 38.707 0.40 . 1 . . . . 217 ASN CB . 25070 1 1181 . 2 2 23 23 ASN N N 15 121.785 0.40 . 1 . . . . 217 ASN N . 25070 1 1182 . 2 2 24 24 LYS H H 1 8.044 0.04 . 1 . . . . 218 LYS H . 25070 1 1183 . 2 2 24 24 LYS HA H 1 4.125 0.04 . 1 . . . . 218 LYS HA . 25070 1 1184 . 2 2 24 24 LYS HB2 H 1 1.767 0.04 . 2 . . . . 218 LYS HB2 . 25070 1 1185 . 2 2 24 24 LYS HB3 H 1 1.811 0.04 . 2 . . . . 218 LYS HB3 . 25070 1 1186 . 2 2 24 24 LYS HG2 H 1 1.476 0.04 . 2 . . . . 218 LYS HG2 . 25070 1 1187 . 2 2 24 24 LYS HG3 H 1 1.476 0.04 . 2 . . . . 218 LYS HG3 . 25070 1 1188 . 2 2 24 24 LYS HD2 H 1 1.696 0.04 . 2 . . . . 218 LYS HD2 . 25070 1 1189 . 2 2 24 24 LYS HD3 H 1 1.696 0.04 . 2 . . . . 218 LYS HD3 . 25070 1 1190 . 2 2 24 24 LYS HE2 H 1 2.959 0.04 . 2 . . . . 218 LYS HE2 . 25070 1 1191 . 2 2 24 24 LYS HE3 H 1 2.959 0.04 . 2 . . . . 218 LYS HE3 . 25070 1 1192 . 2 2 24 24 LYS C C 13 179.720 0.4 . 1 . . . . 218 LYS C . 25070 1 1193 . 2 2 24 24 LYS CA C 13 58.495 0.40 . 1 . . . . 218 LYS CA . 25070 1 1194 . 2 2 24 24 LYS CB C 13 31.780 0.40 . 1 . . . . 218 LYS CB . 25070 1 1195 . 2 2 24 24 LYS CG C 13 24.755 0.40 . 1 . . . . 218 LYS CG . 25070 1 1196 . 2 2 24 24 LYS CD C 13 29.106 0.40 . 1 . . . . 218 LYS CD . 25070 1 1197 . 2 2 24 24 LYS CE C 13 42.146 0.40 . 1 . . . . 218 LYS CE . 25070 1 1198 . 2 2 24 24 LYS N N 15 120.745 0.40 . 1 . . . . 218 LYS N . 25070 1 1199 . 2 2 25 25 HIS H H 1 8.417 0.04 . 1 . . . . 219 HIS H . 25070 1 1200 . 2 2 25 25 HIS HA H 1 4.189 0.04 . 1 . . . . 219 HIS HA . 25070 1 1201 . 2 2 25 25 HIS HB2 H 1 3.150 0.04 . 2 . . . . 219 HIS HB2 . 25070 1 1202 . 2 2 25 25 HIS HB3 H 1 3.237 0.04 . 2 . . . . 219 HIS HB3 . 25070 1 1203 . 2 2 25 25 HIS C C 13 177.912 0.4 . 1 . . . . 219 HIS C . 25070 1 1204 . 2 2 25 25 HIS CA C 13 60.119 0.40 . 1 . . . . 219 HIS CA . 25070 1 1205 . 2 2 25 25 HIS CB C 13 28.517 0.40 . 1 . . . . 219 HIS CB . 25070 1 1206 . 2 2 25 25 HIS N N 15 118.175 0.40 . 1 . . . . 219 HIS N . 25070 1 1207 . 2 2 26 26 LEU H H 1 8.832 0.04 . 1 . . . . 220 LEU H . 25070 1 1208 . 2 2 26 26 LEU HA H 1 3.781 0.04 . 1 . . . . 220 LEU HA . 25070 1 1209 . 2 2 26 26 LEU HB2 H 1 1.361 0.04 . 2 . . . . 220 LEU HB2 . 25070 1 1210 . 2 2 26 26 LEU HB3 H 1 2.033 0.04 . 2 . . . . 220 LEU HB3 . 25070 1 1211 . 2 2 26 26 LEU HG H 1 1.959 0.04 . 1 . . . . 220 LEU HG . 25070 1 1212 . 2 2 26 26 LEU HD11 H 1 0.824 0.04 . 1 . . . . 220 LEU HD1 . 25070 1 1213 . 2 2 26 26 LEU HD12 H 1 0.824 0.04 . 1 . . . . 220 LEU HD1 . 25070 1 1214 . 2 2 26 26 LEU HD13 H 1 0.824 0.04 . 1 . . . . 220 LEU HD1 . 25070 1 1215 . 2 2 26 26 LEU HD21 H 1 0.932 0.04 . 1 . . . . 220 LEU HD2 . 25070 1 1216 . 2 2 26 26 LEU HD22 H 1 0.932 0.04 . 1 . . . . 220 LEU HD2 . 25070 1 1217 . 2 2 26 26 LEU HD23 H 1 0.932 0.04 . 1 . . . . 220 LEU HD2 . 25070 1 1218 . 2 2 26 26 LEU C C 13 177.346 0.4 . 1 . . . . 220 LEU C . 25070 1 1219 . 2 2 26 26 LEU CA C 13 57.981 0.40 . 1 . . . . 220 LEU CA . 25070 1 1220 . 2 2 26 26 LEU CB C 13 41.436 0.40 . 1 . . . . 220 LEU CB . 25070 1 1221 . 2 2 26 26 LEU CG C 13 27.298 0.40 . 1 . . . . 220 LEU CG . 25070 1 1222 . 2 2 26 26 LEU CD1 C 13 27.421 0.40 . 1 . . . . 220 LEU CD1 . 25070 1 1223 . 2 2 26 26 LEU CD2 C 13 24.774 0.40 . 1 . . . . 220 LEU CD2 . 25070 1 1224 . 2 2 26 26 LEU N N 15 120.394 0.40 . 1 . . . . 220 LEU N . 25070 1 1225 . 2 2 27 27 ASP H H 1 7.695 0.04 . 1 . . . . 221 ASP H . 25070 1 1226 . 2 2 27 27 ASP HA H 1 4.239 0.04 . 1 . . . . 221 ASP HA . 25070 1 1227 . 2 2 27 27 ASP HB2 H 1 2.885 0.04 . 2 . . . . 221 ASP HB2 . 25070 1 1228 . 2 2 27 27 ASP HB3 H 1 2.651 0.04 . 2 . . . . 221 ASP HB3 . 25070 1 1229 . 2 2 27 27 ASP C C 13 178.430 0.4 . 1 . . . . 221 ASP C . 25070 1 1230 . 2 2 27 27 ASP CA C 13 57.433 0.40 . 1 . . . . 221 ASP CA . 25070 1 1231 . 2 2 27 27 ASP CB C 13 39.548 0.40 . 1 . . . . 221 ASP CB . 25070 1 1232 . 2 2 27 27 ASP N N 15 117.206 0.40 . 1 . . . . 221 ASP N . 25070 1 1233 . 2 2 28 28 SER H H 1 7.084 0.04 . 1 . . . . 222 SER H . 25070 1 1234 . 2 2 28 28 SER HA H 1 4.490 0.04 . 1 . . . . 222 SER HA . 25070 1 1235 . 2 2 28 28 SER HB2 H 1 3.826 0.04 . 2 . . . . 222 SER HB2 . 25070 1 1236 . 2 2 28 28 SER HB3 H 1 3.826 0.04 . 2 . . . . 222 SER HB3 . 25070 1 1237 . 2 2 28 28 SER C C 13 174.480 0.4 . 1 . . . . 222 SER C . 25070 1 1238 . 2 2 28 28 SER CA C 13 59.899 0.40 . 1 . . . . 222 SER CA . 25070 1 1239 . 2 2 28 28 SER CB C 13 63.779 0.40 . 1 . . . . 222 SER CB . 25070 1 1240 . 2 2 28 28 SER N N 15 112.049 0.40 . 1 . . . . 222 SER N . 25070 1 1241 . 2 2 29 29 CYS H H 1 8.394 0.04 . 1 . . . . 223 CYS H . 25070 1 1242 . 2 2 29 29 CYS HA H 1 3.796 0.04 . 1 . . . . 223 CYS HA . 25070 1 1243 . 2 2 29 29 CYS HB2 H 1 2.509 0.04 . 2 . . . . 223 CYS HB2 . 25070 1 1244 . 2 2 29 29 CYS HB3 H 1 2.013 0.04 . 2 . . . . 223 CYS HB3 . 25070 1 1245 . 2 2 29 29 CYS C C 13 177.193 0.4 . 1 . . . . 223 CYS C . 25070 1 1246 . 2 2 29 29 CYS CA C 13 63.304 0.40 . 1 . . . . 223 CYS CA . 25070 1 1247 . 2 2 29 29 CYS CB C 13 30.791 0.40 . 1 . . . . 223 CYS CB . 25070 1 1248 . 2 2 29 29 CYS N N 15 127.419 0.40 . 1 . . . . 223 CYS N . 25070 1 1249 . 2 2 30 30 LEU H H 1 8.173 0.04 . 1 . . . . 224 LEU H . 25070 1 1250 . 2 2 30 30 LEU HA H 1 4.104 0.04 . 1 . . . . 224 LEU HA . 25070 1 1251 . 2 2 30 30 LEU HB2 H 1 1.506 0.04 . 2 . . . . 224 LEU HB2 . 25070 1 1252 . 2 2 30 30 LEU HB3 H 1 1.775 0.04 . 2 . . . . 224 LEU HB3 . 25070 1 1253 . 2 2 30 30 LEU HG H 1 1.677 0.04 . 1 . . . . 224 LEU HG . 25070 1 1254 . 2 2 30 30 LEU HD11 H 1 0.738 0.04 . 1 . . . . 224 LEU HD1 . 25070 1 1255 . 2 2 30 30 LEU HD12 H 1 0.738 0.04 . 1 . . . . 224 LEU HD1 . 25070 1 1256 . 2 2 30 30 LEU HD13 H 1 0.738 0.04 . 1 . . . . 224 LEU HD1 . 25070 1 1257 . 2 2 30 30 LEU HD21 H 1 0.796 0.04 . 1 . . . . 224 LEU HD2 . 25070 1 1258 . 2 2 30 30 LEU HD22 H 1 0.796 0.04 . 1 . . . . 224 LEU HD2 . 25070 1 1259 . 2 2 30 30 LEU HD23 H 1 0.796 0.04 . 1 . . . . 224 LEU HD2 . 25070 1 1260 . 2 2 30 30 LEU C C 13 177.683 0.4 . 1 . . . . 224 LEU C . 25070 1 1261 . 2 2 30 30 LEU CA C 13 55.666 0.40 . 1 . . . . 224 LEU CA . 25070 1 1262 . 2 2 30 30 LEU CB C 13 42.305 0.40 . 1 . . . . 224 LEU CB . 25070 1 1263 . 2 2 30 30 LEU CG C 13 26.947 0.40 . 1 . . . . 224 LEU CG . 25070 1 1264 . 2 2 30 30 LEU CD1 C 13 24.061 0.40 . 1 . . . . 224 LEU CD1 . 25070 1 1265 . 2 2 30 30 LEU CD2 C 13 26.857 0.40 . 1 . . . . 224 LEU CD2 . 25070 1 1266 . 2 2 30 30 LEU N N 15 114.322 0.40 . 1 . . . . 224 LEU N . 25070 1 1267 . 2 2 31 31 SER H H 1 7.858 0.04 . 1 . . . . 225 SER H . 25070 1 1268 . 2 2 31 31 SER HA H 1 4.419 0.04 . 1 . . . . 225 SER HA . 25070 1 1269 . 2 2 31 31 SER HB2 H 1 3.808 0.04 . 2 . . . . 225 SER HB2 . 25070 1 1270 . 2 2 31 31 SER HB3 H 1 3.808 0.04 . 2 . . . . 225 SER HB3 . 25070 1 1271 . 2 2 31 31 SER C C 13 173.360 0.4 . 1 . . . . 225 SER C . 25070 1 1272 . 2 2 31 31 SER CA C 13 58.244 0.40 . 1 . . . . 225 SER CA . 25070 1 1273 . 2 2 31 31 SER CB C 13 63.837 0.40 . 1 . . . . 225 SER CB . 25070 1 1274 . 2 2 31 31 SER N N 15 114.496 0.40 . 1 . . . . 225 SER N . 25070 1 1275 . 2 2 32 32 ARG H H 1 8.098 0.04 . 1 . . . . 226 ARG H . 25070 1 1276 . 2 2 32 32 ARG N N 15 125.493 0.40 . 1 . . . . 226 ARG N . 25070 1 stop_ save_