data_16228 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 16228 _Entry.Title ; 1H, 13C, and 15N chemical shift assignments for stereo-array labeled (SAIL) ubiquitin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2009-03-27 _Entry.Accession_date 2009-03-27 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.9.13 _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 Teppei Ikeya . . . 16228 2 Mitsuhiro Takeda . . . 16228 3 Hitoshi Yoshida . . . 16228 4 Tsutomu Terauchi . . . 16228 5 Jun-Goo Jee . . . 16228 6 Masatsune Kainosho . . . 16228 7 Peter Guntert . . . 16228 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 16228 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 323 16228 '15N chemical shifts' 80 16228 '1H chemical shifts' 412 16228 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 3 . . 2012-09-19 2009-03-27 update author 'update the chemical shifts' 16228 2 . . 2009-08-10 2009-03-27 update BMRB 'completed entry citation' 16228 1 . . 2009-07-17 2009-03-27 original author 'original release' 16228 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 16228 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 19597942 _Citation.Full_citation . _Citation.Title 'Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR.' _Citation.Journal_name_full . _Citation.Journal_volume 44 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 261 _Citation.Page_last 272 _Citation.Year 2009 _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 Teppei Ikeya . . . 16228 1 2 Mitsuhiro Takeda . . . 16228 1 3 Hitoshi Yoshida . . . 16228 1 4 Tsutomu Terauchi . . . 16228 1 5 Jun-Goo Jee . . . 16228 1 6 Masatsune Kainosho . . . 16228 1 7 Peter Guntert . . . 16228 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'Automated structure determination' 16228 1 CYANA 16228 1 FLYA 16228 1 SAIL 16228 1 ubiquitin 16228 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 16228 _Assembly.ID 1 _Assembly.Name ubiquitin _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 ubiquitin 1 $ubiquitin A . yes native no no . . . 16228 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_ubiquitin _Entity.Sf_category entity _Entity.Sf_framecode ubiquitin _Entity.Entry_ID 16228 _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 . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MQIFVKTLTGKTITLEVESS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLADYN IQKESTLHLVLRLRGG ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 76 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 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 15047 . denatured_ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 2 no BMRB 15410 . Ubi . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 3 no BMRB 15907 . Ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 4 no BMRB 16582 . Ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 5 no BMRB 16626 . Ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 6 no BMRB 17181 . ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 7 no BMRB 17439 . ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 8 no BMRB 17769 . Ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 9 no BMRB 17919 . entity . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 10 no BMRB 18582 . ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 11 no BMRB 18583 . ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 12 no BMRB 18584 . ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 13 no BMRB 18610 . Ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 14 no BMRB 18611 . Ubiquitin_A_state . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 15 no BMRB 18737 . UBIQUITIN . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 16 no BMRB 19406 . entity . . . . . 100.00 152 97.37 98.68 1.40e-43 . . . . 16228 1 17 no BMRB 19412 . entity . . . . . 100.00 152 97.37 98.68 1.40e-43 . . . . 16228 1 18 no BMRB 25070 . Ubiquitin . . . . . 100.00 79 97.37 98.68 1.86e-44 . . . . 16228 1 19 no BMRB 25123 . Ubiquitin . . . . . 94.74 72 97.22 98.61 1.89e-41 . . . . 16228 1 20 no BMRB 26604 . Ubiquitin_(microcrystalline) . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 21 no BMRB 4245 . ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 22 no BMRB 4375 . Ubiquitin . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 23 no PDB 1AAR . "Structure Of A Diubiquitin Conjugate And A Model For Interaction With Ubiquitin Conjugating Enzyme (E2)" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 24 no PDB 1CMX . "Structural Basis For The Specificity Of Ubiquitin C- Terminal Hydrolases" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 25 no PDB 1D3Z . "Ubiquitin Nmr Structure" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 26 no PDB 1F9J . "Structure Of A New Crystal Form Of Tetraubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 27 no PDB 1FXT . "Structure Of A Conjugating Enzyme-Ubiquitin Thiolester Complex" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 28 no PDB 1G6J . "Structure Of Recombinant Human Ubiquitin In Aot Reverse Micelles" . . . . . 98.68 76 97.33 98.67 1.63e-43 . . . . 16228 1 29 no PDB 1GJZ . "Solution Structure Of A Dimeric N-Terminal Fragment Of Human Ubiquitin" . . . . . 67.11 53 98.04 98.04 2.76e-25 . . . . 16228 1 30 no PDB 1NBF . "Crystal Structure Of A Ubp-Family Deubiquitinating Enzyme In Isolation And In Complex With Ubiquitin Aldehyde" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 31 no PDB 1P3Q . "Mechanism Of Ubiquitin Recognition By The Cue Domain Of Vps9" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 32 no PDB 1Q5W . "Ubiquitin Recognition By Npl4 Zinc-Fingers" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 33 no PDB 1S1Q . "Tsg101(Uev) Domain In Complex With Ubiquitin" . . . . . 98.68 76 97.33 98.67 1.63e-43 . . . . 16228 1 34 no PDB 1TBE . "Structure Of Tetraubiquitin Shows How Multiubiquitin Chains Can Be Formed" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 35 no PDB 1UBI . "Synthetic Structural And Biological Studies Of The Ubiquitin System. Part 1" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 36 no PDB 1UBQ . "Structure Of Ubiquitin Refined At 1.8 Angstroms Resolution" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 37 no PDB 1UZX . "A Complex Of The Vps23 Uev With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 38 no PDB 1V80 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 39 no PDB 1V81 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 40 no PDB 1WR6 . "Crystal Structure Of Gga3 Gat Domain In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 41 no PDB 1WRD . "Crystal Structure Of Tom1 Gat Domain In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 42 no PDB 1XD3 . "Crystal Structure Of Uchl3-Ubvme Complex" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 43 no PDB 1XQQ . "Simultaneous Determination Of Protein Structure And Dynamics" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 44 no PDB 1YD8 . "Complex Of Human Gga3 Gat Domain And Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 45 no PDB 1YX5 . "Solution Structure Of S5a Uim-1UBIQUITIN COMPLEX" . . . . . 100.00 98 97.37 98.68 6.66e-45 . . . . 16228 1 46 no PDB 1YX6 . "Solution Structure Of S5a Uim-2UBIQUITIN COMPLEX" . . . . . 100.00 98 97.37 98.68 6.66e-45 . . . . 16228 1 47 no PDB 2AYO . "Structure Of Usp14 Bound To Ubquitin Aldehyde" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 48 no PDB 2BGF . "Nmr Structure Of Lys48-Linked Di-Ubiquitin Using Chemical Shift Perturbation Data Together With Rdcs And 15n- Relaxation Data" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 49 no PDB 2C7M . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 50 no PDB 2C7N . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 51 no PDB 2D3G . "Double Sided Ubiquitin Binding Of Hrs-Uim" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 52 no PDB 2DEN . "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 53 no PDB 2DX5 . "The Complex Structure Between The Mouse Eap45-Glue Domain And Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 54 no PDB 2FID . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 55 no PDB 2FIF . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 56 no PDB 2FUH . "Solution Structure Of The Ubch5cUB NON-Covalent Complex" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 57 no PDB 2G45 . "Co-Crystal Structure Of Znf Ubp Domain From The Deubiquitinating Enzyme Isopeptidase T (Isot) In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 58 no PDB 2GMI . Mms2UBC13~UBIQUITIN . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 59 no PDB 2HD5 . "Usp2 In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 60 no PDB 2HTH . "Structural Basis For Ubiquitin Recognition By The Human Eap45ESCRT-Ii Glue Domain" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 61 no PDB 2IBI . "Covalent Ubiquitin-Usp2 Complex" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 62 no PDB 2J7Q . "Crystal Structure Of The Ubiquitin-Specific Protease Encoded By Murine Cytomegalovirus Tegument Protein M48 In Complex With A U" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 63 no PDB 2JF5 . "Crystal Structure Of Lys63-Linked Di-Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 64 no PDB 2JRI . "Solution Structure Of The Josephin Domain Of Ataxin-3 In Complex With Ubiquitin Molecule." . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 65 no PDB 2JY6 . "Solution Structure Of The Complex Of Ubiquitin And Ubiquilin 1 Uba Domain" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 66 no PDB 2JZZ . "Solid-State Nmr Structure Of Microcrystalline Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 67 no PDB 2K39 . "Recognition Dynamics Up To Microseconds Revealed From Rdc Derived Ubiquitin Ensemble In Solution" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 68 no PDB 2K6D . "Cin85 Sh3-C Domain In Complex With Ubiquitin" . . . . . 98.68 76 97.33 98.67 9.88e-44 . . . . 16228 1 69 no PDB 2K8B . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Cis Isomer In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 70 no PDB 2K8C . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Trans Isomer In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 71 no PDB 2KDE . "Nmr Structure Of Major S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 72 no PDB 2KDF . "Nmr Structure Of Minor S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 73 no PDB 2KHW . "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" . . . . . 100.00 79 97.37 98.68 1.86e-44 . . . . 16228 1 74 no PDB 2KJH . "Nmr Based Structural Model Of The Ubch8-Ubiquitin Complex" . . . . . 98.68 76 97.33 98.67 9.88e-44 . . . . 16228 1 75 no PDB 2KLG . "Pere Nmr Structure Of Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 76 no PDB 2KN5 . "A Correspondence Between Solution-State Dynamics Of An Individual Protein And The Sequence And Conformational Diversity Of Its " . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 77 no PDB 2KOX . "Nmr Residual Dipolar Couplings Identify Long Range Correlated Motions In The Backbone Of The Protein Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 78 no PDB 2KTF . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 79 no PDB 2KWU . "Solution Structure Of Ubm2 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 80 no PDB 2KWV . "Solution Structure Of Ubm1 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 81 no PDB 2L0F . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 (P692a Mutant) In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 82 no PDB 2L0T . "Solution Structure Of The Complex Of Ubiquitin And The Vhs Domain Of Stam2" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 83 no PDB 2L3Z . "Proton-Detected 4d Dream Solid-State Nmr Structure Of Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 84 no PDB 2LD9 . "Backbone Structure Of Ubiquitin Determined Using Backbone Amide Noes And Backbone N-H And N-C Rdcs" . . . . . 100.00 77 97.37 98.68 2.01e-44 . . . . 16228 1 85 no PDB 2LJ5 . "Description Of The Structural Fluctuations Of Proteins From Structure- Based Calculations Of Residual Dipolar Couplings" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 86 no PDB 2LVO . "Structure Of The Gp78cue Domain Bound To Monubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 87 no PDB 2LVP . "Gp78cue Domain Bound To The Distal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 88 no PDB 2LVQ . "Gp78cue Domain Bound To The Proximal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 89 no PDB 2LZ6 . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 90 no PDB 2MBB . "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" . . . . . 100.00 78 97.37 98.68 1.55e-44 . . . . 16228 1 91 no PDB 2MBH . "Nmr Structure Of Eklf(22-40)/ubiquitin Complex" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 92 no PDB 2MBO . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 0 Mm Nacl" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 93 no PDB 2MBQ . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 150 Mm Nacl" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 94 no PDB 2MCN . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 95 no PDB 2MJ5 . "Structure Of The Uba Domain Of Human Nbr1 In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 96 no PDB 2MJB . "Solution Nmr Structure Of Ubiquitin Refined Against Dipolar Couplings In 4 Media" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 97 no PDB 2MOR . "A Tensor-free Method For The Structural And Dynamical Refinement Of Proteins Using Residual Dipolar Couplings" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 98 no PDB 2MRE . "Nmr Structure Of The Rad18-ubz/ubiquitin Complex" . . . . . 100.00 79 97.37 98.68 1.86e-44 . . . . 16228 1 99 no PDB 2MRO . "Structure Of The Complex Of Ubiquitin And The Uba Domain From Dna- Damage-inducible 1 Protein (ddi1)" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 100 no PDB 2MSG . "Solid-state Nmr Structure Of Ubiquitin" . . . . . 94.74 72 97.22 98.61 1.89e-41 . . . . 16228 1 101 no PDB 2MUR . "Solution Structure Of The Human Faap20 Ubz-ubiquitin Complex" . . . . . 100.00 78 97.37 98.68 1.55e-44 . . . . 16228 1 102 no PDB 2N2K . "Ensemble Structure Of The Closed State Of Lys63-linked Diubiquitin In The Absence Of A Ligand" . . . . . 93.42 71 97.18 98.59 1.55e-40 . . . . 16228 1 103 no PDB 2NR2 . "The Mumo (Minimal Under-Restraining Minimal Over- Restraining) Method For The Determination Of Native States Ensembles Of Prote" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 104 no PDB 2O6V . "Crystal Structure And Solution Nmr Studies Of Lys48-Linked Tetraubiquitin At Neutral Ph" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 105 no PDB 2OJR . "Structure Of Ubiquitin Solved By Sad Using The Lanthanide- Binding Tag" . . . . . 100.00 111 97.37 98.68 6.88e-44 . . . . 16228 1 106 no PDB 2OOB . "Crystal Structure Of The Uba Domain From Cbl-B Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 107 no PDB 2PE9 . "Nmr Based Structure Of The Open Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Tenso" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 108 no PDB 2PEA . "Nmr Based Structure Of The Closed Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Ten" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 109 no PDB 2QHO . "Crystal Structure Of The Uba Domain From Edd Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 110 no PDB 2RR9 . "The Solution Structure Of The K63-Ub2:tuims Complex" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 111 no PDB 2W9N . "Crystal Structure Of Linear Di-Ubiquitin" . . . . . 98.68 152 97.33 98.67 1.23e-42 . . . . 16228 1 112 no PDB 2WDT . "Crystal Structure Of Plasmodium Falciparum Uchl3 In Complex With The Suicide Inhibitor Ubvme" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 113 no PDB 2WWZ . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P212121" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 114 no PDB 2WX0 . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P21" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 115 no PDB 2WX1 . "Tab2 Nzf Domain In Complex With Lys63-Linked Tri-Ubiquitin, P212121" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 116 no PDB 2XBB . "Nedd4 Hect:ub Complex" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 117 no PDB 2XEW . "Crystal Structure Of K11-Linked Diubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 118 no PDB 2XK5 . "Crystal Structure Of K6-Linked Diubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 119 no PDB 2Y5B . "Structure Of Usp21 In Complex With Linear Diubiquitin-Aldehyde" . . . . . 98.68 152 97.33 98.67 9.61e-43 . . . . 16228 1 120 no PDB 2Z59 . "Complex Structures Of Mouse Rpn13 (22-130aa) And Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 121 no PDB 2ZCC . "Ubiquitin Crystallized Under High Pressure" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 122 no PDB 2ZNV . "Crystal Structure Of Human Amsh-Lp Dub Domain In Complex With Lys63-Linked Ubiquitin Dimer" . . . . . 100.00 77 97.37 98.68 1.67e-44 . . . . 16228 1 123 no PDB 2ZVN . "Nemo Cozi Domain Incomplex With Diubiquitin In P212121 Space Group" . . . . . 100.00 154 97.37 98.68 1.53e-43 . . . . 16228 1 124 no PDB 2ZVO . "Nemo Cozi Domain In Complex With Diubiquitin In C2 Space Group" . . . . . 100.00 154 97.37 98.68 1.53e-43 . . . . 16228 1 125 no PDB 3A1Q . "Crystal Structure Of The Mouse Rap80 Uims In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 100.00 77 97.37 98.68 1.67e-44 . . . . 16228 1 126 no PDB 3A33 . "Ubch5b~ubiquitin Conjugate" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 127 no PDB 3A9J . "Crystal Structure Of The Mouse Tab2-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 100.00 77 97.37 98.68 1.67e-44 . . . . 16228 1 128 no PDB 3A9K . "Crystal Structure Of The Mouse Tab3-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 100.00 77 97.37 98.68 1.67e-44 . . . . 16228 1 129 no PDB 3AI5 . "Crystal Structure Of Yeast Enhanced Green Fluorescent Protein- Ubiquitin Fusion Protein" . . . . . 97.37 307 97.30 98.65 3.81e-40 . . . . 16228 1 130 no PDB 3ALB . "Cyclic Lys48-Linked Tetraubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 131 no PDB 3AUL . "Crystal Structure Of Wild-Type Lys48-Linked Diubiquitin In An Open Conformation" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 132 no PDB 3AXC . "Crystal Structure Of Linear Diubiquitin" . . . . . 100.00 154 97.37 98.68 1.53e-43 . . . . 16228 1 133 no PDB 3B08 . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 100.00 152 97.37 98.68 1.40e-43 . . . . 16228 1 134 no PDB 3B0A . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 100.00 152 97.37 98.68 1.40e-43 . . . . 16228 1 135 no PDB 3BY4 . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 136 no PDB 3C0R . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 137 no PDB 3DVG . "Crystal Structure Of K63-Specific Fab Apu.3a8 Bound To K63-Linked Di- Ubiquitin" . . . . . 100.00 80 97.37 98.68 2.00e-44 . . . . 16228 1 138 no PDB 3DVN . "Crystal Structure Of K63-specific Fab Apu2.16 Bound To K63-linked Di- Ubiquitin" . . . . . 100.00 80 97.37 98.68 2.00e-44 . . . . 16228 1 139 no PDB 3EEC . "X-Ray Structure Of Human Ubiquitin Cd(Ii) Adduct" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 140 no PDB 3EFU . "X-Ray Structure Of Human Ubiquitin-Hg(Ii) Adduct" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 141 no PDB 3EHV . "X-Ray Structure Of Human Ubiquitin Zn(Ii) Adduct" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 142 no PDB 3H1U . "Structure Of Ubiquitin In Complex With Cd Ions" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 143 no PDB 3H7P . "Crystal Structure Of K63-Linked Di-Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 144 no PDB 3HM3 . "The Structure And Conformation Of Lys-63 Linked Tetra-Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 145 no PDB 3I3T . "Crystal Structure Of Covalent Ubiquitin-usp21 Complex" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 146 no PDB 3IFW . "Crystal Structure Of The S18y Variant Of Ubiquitin Carboxy T Hydrolase L1 Bound To Ubiquitin Vinylmethylester." . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 147 no PDB 3IHP . "Covalent Ubiquitin-Usp5 Complex" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 148 no PDB 3J60 . "Localization Of The Small Subunit Ribosomal Proteins Into A 5.5 A Cryo-em Map Of Triticum Aestivum Translating 80s Ribosome" . . . . . 100.00 155 98.68 100.00 5.12e-45 . . . . 16228 1 149 no PDB 3JSV . "Crystal Structure Of Mouse Nemo Cozi In Complex With Lys63- Linked Di-Ubiquitin" . . . . . 100.00 77 97.37 98.68 1.67e-44 . . . . 16228 1 150 no PDB 3JVZ . E2~ubiquitin-Hect . . . . . 100.00 81 97.37 98.68 1.84e-44 . . . . 16228 1 151 no PDB 3JW0 . E2~ubiquitin-Hect . . . . . 100.00 81 97.37 98.68 1.84e-44 . . . . 16228 1 152 no PDB 3K9O . "The Crystal Structure Of E2-25k And Ubb+1 Complex" . . . . . 98.68 96 97.33 98.67 2.80e-43 . . . . 16228 1 153 no PDB 3K9P . "The Crystal Structure Of E2-25k And Ubiquitin Complex" . . . . . 100.00 79 97.37 98.68 1.86e-44 . . . . 16228 1 154 no PDB 3KVF . "Crystal Structure Of The I93m Mutant Of Ubiquitin Carboxy Te Hydrolase L1 Bound To Ubiquitin Vinylmethylester" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 155 no PDB 3KW5 . "Crystal Structure Of Ubiquitin Carboxy Terminal Hydrolase L1 Ubiquitin Vinylmethylester" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 156 no PDB 3LDZ . "Crystal Structure Of Human Stam1 Vhs Domain In Complex With Ubiquitin" . . . . . 96.05 73 97.26 98.63 4.88e-42 . . . . 16228 1 157 no PDB 3M3J . "A New Crystal Form Of Lys48-Linked Diubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 158 no PDB 3MHS . "Structure Of The Saga Ubp8SGF11SUS1SGF73 DUB MODULE BOUND Ubiquitin Aldehyde" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 159 no PDB 3N30 . "Crystal Structure Of Cubic Zn3-Hub (Human Ubiquitin) Adduct" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 160 no PDB 3N32 . "The Crystal Structure Of Human Ubiquitin Adduct With Zeise's Salt" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 161 no PDB 3NHE . "High Resolution Structure (1.26a) Of Usp2a In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 162 no PDB 3NOB . "Structure Of K11-linked Di-ubiquitin" . . . . . 100.00 78 97.37 98.68 1.55e-44 . . . . 16228 1 163 no PDB 3NS8 . "Crystal Structure Of An Open Conformation Of Lys48-Linked Diubiquitin At Ph 7.5" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 164 no PDB 3O65 . "Crystal Structure Of A Josephin-Ubiquitin Complex: Evolutionary Restraints On Ataxin-3 Deubiquitinating Activity" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 165 no PDB 3OFI . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 166 no PDB 3OJ3 . "Crystal Structure Of The A20 Znf4 And Ubiquitin Complex" . . . . . 100.00 79 97.37 98.68 1.86e-44 . . . . 16228 1 167 no PDB 3OJ4 . "Crystal Structure Of The A20 Znf4, Ubiquitin And Ubch5a Complex" . . . . . 100.00 79 97.37 98.68 1.86e-44 . . . . 16228 1 168 no PDB 3ONS . "Crystal Structure Of Human Ubiquitin In A New Crystal Form" . . . . . 94.74 72 97.22 98.61 1.89e-41 . . . . 16228 1 169 no PDB 3PHD . "Crystal Structure Of Human Hdac6 In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 170 no PDB 3PHW . "Otu Domain Of Crimean Congo Hemorrhagic Fever Virus In Complex With Ubiquitin" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 171 no PDB 3PRM . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 172 no PDB 3PRP . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 173 no PDB 3PT2 . "Structure Of A Viral Otu Domain Protease Bound To Ubiquitin" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 174 no PDB 3PTF . "X-Ray Structure Of The Non-Covalent Complex Between Ubch5a And Ubiquitin" . . . . . 100.00 79 97.37 98.68 1.86e-44 . . . . 16228 1 175 no PDB 3Q3F . "Engineering Domain-Swapped Binding Interfaces By Mutually Exclusive Folding: Insertion Of Ubiquitin Into Position 103 Of Barnas" . . . . . 98.68 189 97.33 98.67 1.87e-42 . . . . 16228 1 176 no PDB 3RUL . "New Strategy To Analyze Structures Of Glycopeptide-Target Complexes" . . . . . 98.68 79 97.33 98.67 1.11e-43 . . . . 16228 1 177 no PDB 3TBL . "Structure Of Mono-ubiquitinated Pcna: Implications For Dna Polymerase Switching And Okazaki Fragment Maturation" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 178 no PDB 3TMP . "The Catalytic Domain Of Human Deubiquitinase Duba In Complex With Ubiquitin Aldehyde" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 179 no PDB 3U30 . "Crystal Structure Of A Linear-Specific Ubiquitin Fab Bound To Linear Ubiquitin" . . . . . 100.00 172 97.37 98.68 1.49e-43 . . . . 16228 1 180 no PDB 3UGB . "Ubch5c~ubiquitin Conjugate" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 181 no PDB 3VDZ . "Tailoring Encodable Lanthanide-Binding Tags As Mri Contrast Agents: Xq-Dse3-Ubiquitin At 2.4 Angstroms" . . . . . 100.00 111 97.37 98.68 4.91e-44 . . . . 16228 1 182 no PDB 3VFK . "The Structure Of Monodechloro-teicoplanin In Complex With Its Ligand, Using Ubiquitin As A Ligand Carrier" . . . . . 98.68 79 97.33 98.67 1.11e-43 . . . . 16228 1 183 no PDB 3VHT . "Crystal Structure Of Gfp-Wrnip1 Ubz Domain Fusion Protein In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 184 no PDB 3VUW . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form I" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 185 no PDB 3VUX . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form Ii" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 186 no PDB 3VUY . "Crystal Structure Of A20 Zf7 In Complex With Linear Tetraubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 187 no PDB 3WWQ . "Crystal Structure Of Faap20 Ubz Domain In Complex With Lys63-linked Diubiquitin" . . . . . 100.00 77 97.37 98.68 1.67e-44 . . . . 16228 1 188 no PDB 3WXE . "Crystal Structure Of Cyld Usp Domain (c596s) In Complex With Met1- Linked Diubiquitin" . . . . . 94.74 148 97.22 98.61 2.24e-40 . . . . 16228 1 189 no PDB 3WXF . "Crystal Structure Of Cyld Usp Domain (c596s E674q) In Complex With Met1-linked Diubiquitin" . . . . . 94.74 148 97.22 98.61 2.24e-40 . . . . 16228 1 190 no PDB 3WXG . "Crystal Structure Of Cyld Usp Domain (c596a) In Complex With Lys63- Linked Diubiquitin" . . . . . 94.74 72 97.22 98.61 1.89e-41 . . . . 16228 1 191 no PDB 3ZNH . "Crimean Congo Hemorrhagic Fever Virus Otu Domain In Complex With Ubiquitin-propargyl." . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 192 no PDB 3ZNI . "Structure Of Phosphotyr363-cbl-b - Ubch5b-ub - Zap-70 Peptide Complex" . . . . . 100.00 81 97.37 98.68 1.84e-44 . . . . 16228 1 193 no PDB 3ZNZ . "Crystal Structure Of Otulin Otu Domain (c129a) In Complex With Met1-di Ubiquitin" . . . . . 100.00 152 97.37 98.68 1.40e-43 . . . . 16228 1 194 no PDB 4AP4 . "Rnf4 - Ubch5a - Ubiquitin Heterotrimeric Complex" . . . . . 100.00 80 97.37 98.68 1.79e-44 . . . . 16228 1 195 no PDB 4AUQ . "Structure Of Birc7-Ubch5b-Ub Complex." . . . . . 100.00 81 97.37 98.68 1.84e-44 . . . . 16228 1 196 no PDB 4BBN . "Nedd4 Hect-ub:ub Complex" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 197 no PDB 4BOS . "Structure Of Otud2 Otu Domain In Complex With Ubiquitin K11- Linked Peptide" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 198 no PDB 4BOZ . "Structure Of Otud2 Otu Domain In Complex With K11-linked Di Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 199 no PDB 4BVU . "Structure Of Shigella Effector Ospg In Complex With Host Ubch5c-ubiquitin Conjugate" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 200 no PDB 4CXC . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 100.00 156 97.37 98.68 2.46e-44 . . . . 16228 1 201 no PDB 4CXD . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 202 no PDB 4D5L . "Cryo-em Structures Of Ribosomal 80s Complexes With Termination Factors And Cricket Paralysis Virus Ires Reveal The Ires In The " . . . . . 100.00 156 97.37 98.68 2.46e-44 . . . . 16228 1 203 no PDB 4D61 . "Cryo-em Structures Of Ribosomal 80s Complexes With Termination Factors And Cricket Paralysis Virus Ires Reveal The Ires In The " . . . . . 100.00 156 97.37 98.68 2.46e-44 . . . . 16228 1 204 no PDB 4DDG . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 205 no PDB 4DDI . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 206 no PDB 4DHJ . "The Structure Of A Ceotub1 Ubiquitin Aldehyde Ubc13~ub Complex" . . . . . 98.68 76 97.33 98.67 9.88e-44 . . . . 16228 1 207 no PDB 4DHZ . "The Structure Of HCEOTUB1-Ubiquitin Aldehyde-Ubc13~ub" . . . . . 98.68 76 97.33 98.67 9.88e-44 . . . . 16228 1 208 no PDB 4FJV . "Crystal Structure Of Human Otubain2 And Ubiquitin Complex" . . . . . 100.00 86 97.37 98.68 1.76e-44 . . . . 16228 1 209 no PDB 4HXD . "Diversity Of Ubiquitin And Isg15 Specificity Amongst Nairoviruses Viral Ovarian Tumor Domain Proteases" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 210 no PDB 4I6N . "Crystal Structure Of Trichinella Spiralis Uch37 Catalytic Domain Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 97.37 75 97.30 98.65 1.01e-42 . . . . 16228 1 211 no PDB 4IG7 . "Crystal Structure Of Trichinella Spiralis Uch37 Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 212 no PDB 4IUM . "Equine Arteritis Virus Papain-like Protease 2 (plp2) Covalently Bound To Ubiquitin" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 213 no PDB 4JQW . "Crystal Structure Of A Complex Of Nod1 Card And Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 214 no PDB 4K1R . "Crystal Structure Of Schizosaccharomyces Pombe Sst2 Catalytic Domain And Ubiquitin" . . . . . 100.00 81 97.37 98.68 2.01e-44 . . . . 16228 1 215 no PDB 4K7S . "Crystal Structure Of Zn2-hub (human Ubiquitin) Adduct From A Solution 35 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 216 no PDB 4K7U . "Crystal Structure Of Zn2.3-hub (human Ubiquitin) Adduct From A Solution 70 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 217 no PDB 4K7W . "Crystal Structure Of Zn3-hub(human Ubiquitin) Adduct From A Solution 100 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 218 no PDB 4KSK . "Gumby/fam105b In Complex With Ubiquitin" . . . . . 100.00 80 97.37 98.68 1.79e-44 . . . . 16228 1 219 no PDB 4KSL . "Gumby/fam105b In Complex With Linear Di-ubiquitin" . . . . . 100.00 156 97.37 98.68 1.55e-43 . . . . 16228 1 220 no PDB 4KZX . "Rabbit 40s Ribosomal Subunit In Complex With Eif1." . . . . . 100.00 156 97.37 98.68 2.46e-44 . . . . 16228 1 221 no PDB 4KZY . "Rabbit 40s Ribosomal Subunit In Complex With Eif1 And Eif1a." . . . . . 100.00 156 97.37 98.68 2.46e-44 . . . . 16228 1 222 no PDB 4KZZ . "Rabbit 40s Ribosomal Subunit In Complex With Mrna, Initiator Trna And Eif1a" . . . . . 100.00 156 97.37 98.68 2.46e-44 . . . . 16228 1 223 no PDB 4LCD . "Structure Of An Rsp5xubxsna3 Complex: Mechanism Of Ubiquitin Ligation And Lysine Prioritization By A Hect E3" . . . . . 97.37 83 97.30 98.65 4.98e-43 . . . . 16228 1 224 no PDB 4LDT . "The Structure Of H/ceotub1-ubiquitin Aldehyde-ubch5b~ub" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 225 no PDB 4LJO . "Structure Of An Active Ligase (hoip)/ubiquitin Transfer Complex" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 226 no PDB 4LJP . "Structure Of An Active Ligase (hoip-h889a)/ubiquitin Transfer Complex" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 227 no PDB 4M0W . "Crystal Structure Of Sars-cov Papain-like Protease C112s Mutant In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 228 no PDB 4MDK . "Cdc34-ubiquitin-cc0651 Complex" . . . . . 100.00 80 97.37 98.68 1.79e-44 . . . . 16228 1 229 no PDB 4MM3 . "Crystal Structure Of Sars-cov Papain-like Protease Plpro In Complex With Ubiquitin Aldehyde" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 230 no PDB 4MSM . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 E286a Mutant Bound To Ubiquitin" . . . . . 100.00 81 97.37 98.68 2.01e-44 . . . . 16228 1 231 no PDB 4MSQ . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 Catalytic Domain Bound To Ubiquitin" . . . . . 100.00 81 97.37 98.68 2.01e-44 . . . . 16228 1 232 no PDB 4NQK . "Structure Of An Ubiquitin Complex" . . . . . 100.00 79 97.37 98.68 2.42e-44 . . . . 16228 1 233 no PDB 4NQL . "The Crystal Structure Of The Dub Domain Of Amsh Orthologue, Sst2 From S. Pombe, In Complex With Lysine 63-linked Diubiquitin" . . . . . 100.00 77 97.37 98.68 1.67e-44 . . . . 16228 1 234 no PDB 4P4H . "Caught-in-action Signaling Complex Of Rig-i 2card Domain And Mavs Card Domain" . . . . . 100.00 79 97.37 98.68 2.42e-44 . . . . 16228 1 235 no PDB 4PQT . "Insights Into The Mechanism Of Deubiquitination By Jamm Deubiquitinases From Co-crystal Structures Of Enzyme With Substrate And" . . . . . 100.00 81 97.37 98.68 2.01e-44 . . . . 16228 1 236 no PDB 4R62 . "Structure Of Rad6~ub" . . . . . 100.00 78 97.37 98.68 1.68e-44 . . . . 16228 1 237 no PDB 4RF0 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 238 no PDB 4RF1 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 98.68 75 97.33 98.67 1.11e-43 . . . . 16228 1 239 no PDB 4S1Z . "Crystal Structure Of Trabid Nzf1 In Complex With K29 Linked Di- Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 240 no PDB 4S22 . "Crystal Structure Of K29 Linked Di-ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 241 no PDB 4UEL . "Uch-l5 In Complex With Ubiquitin-propargyl Bound To The Rpn13 Deubad Domain" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 242 no PDB 4UF6 . "Uch-l5 In Complex With Ubiquitin-propargyl Bound To An Activating Fragment Of Ino80g" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 243 no PDB 4UN2 . "Crystal Structure Of The Uba Domain Of Dsk2 In Complex With Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 244 no PDB 4UPX . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 245 no PDB 4UQ1 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 246 no PDB 4UQ4 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 100.00 156 97.37 98.68 2.46e-44 . . . . 16228 1 247 no PDB 4UQ5 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 100.00 156 97.37 98.68 2.46e-44 . . . . 16228 1 248 no PDB 4V3K . "Rnf38-ubch5b-ub Complex" . . . . . 100.00 81 97.37 98.68 1.84e-44 . . . . 16228 1 249 no PDB 4V3L . "Rnf38-ub-ubch5b-ub Complex" . . . . . 100.00 81 97.37 98.68 1.84e-44 . . . . 16228 1 250 no PDB 4W20 . "Structure Of The Mammalian 60s Ribosomal Subunit (this Entry Contains The Large Ribosomal Proteins)" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 251 no PDB 4W22 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 252 no PDB 4W23 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Small Ribosomal Subunit)" . . . . . 100.00 156 97.37 98.68 2.46e-44 . . . . 16228 1 253 no PDB 4W25 . "Structure Of The Idle Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 254 no PDB 4W27 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 255 no PDB 4W28 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Small Ribosomal Subunit)" . . . . . 100.00 156 97.37 98.68 2.46e-44 . . . . 16228 1 256 no PDB 4WHV . Rnf8/ubc13c87k~ub . . . . . 100.00 83 97.37 98.68 3.18e-44 . . . . 16228 1 257 no PDB 4WLR . "Crystal Structure Of Much37-hrpn13 Ctd-hub Complex" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 258 no PDB 4WUR . "The Crystal Structure Of The Mers-cov Papain-like Protease (c111s) With Human Ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 259 no PDB 4XKL . "Crystal Structure Of Ndp52 Zf2 In Complex With Mono-ubiquitin" . . . . . 100.00 80 97.37 98.68 2.11e-44 . . . . 16228 1 260 no PDB 4XOF . "Observing The Overall Rocking Motion Of A Protein In A Crystal - Orthorhombic Ubiquitin Crystals Without Zinc." . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 261 no PDB 4XOK . "Observing The Overall Rocking Motion Of A Protein In A Crystal." . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 262 no PDB 4XOL . "Observing The Overall Rocking Motion Of A Protein In A Crystal - Cubic Ubiquitin Crystals." . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 263 no PDB 4XYZ . "Crystal Structure Of K33 Linked Di-ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 264 no PDB 4Y1H . "Crystal Structure Of K33 Linked Tri-ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 265 no PDB 4Z9S . "Non-covalent Assembly Of Monoubiquitin That Mimics K11 Poly-ubiquitin" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 266 no PDB 4ZFR . "Catalytic Domain Of Sst2 F403a Mutant Bound To Ubiquitin" . . . . . 100.00 81 97.37 98.68 2.01e-44 . . . . 16228 1 267 no PDB 4ZFT . "Catalytic Domain Of Sst2 F403w Mutant Bound To Ubiquitin" . . . . . 100.00 81 97.37 98.68 2.01e-44 . . . . 16228 1 268 no PDB 5A5B . "Structure Of The 26s Proteasome-ubp6 Complex" . . . . . 98.68 76 97.33 98.67 1.14e-43 . . . . 16228 1 269 no PDB 5AIT . "A Complex Of Of Rnf4-ring Domain, Ubev2, Ubc13-ub (isopeptide Crosslink)" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 270 no PDB 5AIU . "A Complex Of Rnf4-ring Domain, Ubc13-ub (isopeptide Crosslink)" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 271 no DBJ BAA02154 . "ubiquitin/ribosomal polyprotein [Oryza sativa Japonica Group]" . . . . . 100.00 129 98.68 100.00 2.39e-45 . . . . 16228 1 272 no DBJ BAA03764 . "ubiquitin [Glycine max]" . . . . . 100.00 305 98.68 100.00 1.20e-42 . . . . 16228 1 273 no DBJ BAA03983 . "polyubiquitin [Rattus norvegicus]" . . . . . 100.00 305 97.37 98.68 6.98e-42 . . . . 16228 1 274 no DBJ BAA05085 . "Ubiquitin [Glycine max]" . . . . . 100.00 305 98.68 100.00 1.20e-42 . . . . 16228 1 275 no DBJ BAA05670 . "ubiquitin [Glycine max]" . . . . . 100.00 305 98.68 100.00 1.20e-42 . . . . 16228 1 276 no EMBL CAA10056 . "polyubiquitin [Vicia faba]" . . . . . 100.00 229 98.68 100.00 1.93e-43 . . . . 16228 1 277 no EMBL CAA11268 . "ubiquitin extension protein [Nicotiana tabacum]" . . . . . 100.00 156 98.68 100.00 5.05e-45 . . . . 16228 1 278 no EMBL CAA11269 . "polyubiquitin [Nicotiana tabacum]" . . . . . 100.00 381 98.68 98.68 1.04e-41 . . . . 16228 1 279 no EMBL CAA25706 . "unnamed protein product [Saccharomyces cerevisiae]" . . . . . 50.00 191 97.37 100.00 9.44e-16 . . . . 16228 1 280 no EMBL CAA28495 . "ubiquitin [Homo sapiens]" . . . . . 100.00 229 97.37 98.68 1.21e-42 . . . . 16228 1 281 no GB AAA19247 . "ubiquitin/ribosomal fusion protein [Solanum tuberosum]" . . . . . 100.00 156 98.68 100.00 7.87e-45 . . . . 16228 1 282 no GB AAA28997 . "ubiquitin [Drosophila melanogaster]" . . . . . 100.00 231 97.37 98.68 1.07e-42 . . . . 16228 1 283 no GB AAA28998 . "ubiquitin-hybrid protein precursor [Drosophila melanogaster]" . . . . . 100.00 156 97.37 98.68 3.26e-44 . . . . 16228 1 284 no GB AAA28999 . "ubiquitin, partial [Drosophila melanogaster]" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 285 no GB AAA29001 . "ubiquitin, partial [Drosophila melanogaster]" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 286 no PIR G85036 . "polyubiquitin [imported] - Arabidopsis thaliana" . . . . . 100.00 305 98.68 100.00 1.20e-42 . . . . 16228 1 287 no PIR I50437 . "polyubiquitin 4 - chicken [Gallus gallus]" . . . . . 100.00 305 97.37 98.68 6.98e-42 . . . . 16228 1 288 no PIR I51568 . "polyubiquitin - African clawed frog (fragment)" . . . . . 100.00 167 97.37 98.68 2.34e-43 . . . . 16228 1 289 no PIR I65237 . "ubiquitin / ribosomal protein L40, cytosolic [validated] - rat" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 290 no PIR JS0657 . "ubiquitin / ribosomal protein S27a - maize" . . . . . 100.00 155 98.68 100.00 5.65e-45 . . . . 16228 1 291 no PRF 1101405A . "ubiquitin precursor" . . . . . 50.00 191 97.37 100.00 9.34e-16 . . . . 16228 1 292 no PRF 1207189A . "ubiquitin [Avena sativa]" . . . . . 100.00 76 98.68 100.00 2.55e-45 . . . . 16228 1 293 no PRF 1212243A . "ubiquitin S1" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 294 no PRF 1212243C . "ubiquitin S3" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 295 no PRF 1212243J . "ubiquitin S7(2)" . . . . . 100.00 76 97.37 98.68 1.73e-44 . . . . 16228 1 296 no REF NP_001005123 . "ubiquitin-60S ribosomal protein L40 [Xenopus (Silurana) tropicalis]" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 297 no REF NP_001006688 . "ubiquitin C [Xenopus (Silurana) tropicalis]" . . . . . 100.00 609 97.37 98.68 2.59e-40 . . . . 16228 1 298 no REF NP_001009117 . "polyubiquitin-B [Pan troglodytes]" . . . . . 100.00 229 97.37 98.68 1.21e-42 . . . . 16228 1 299 no REF NP_001009286 . "ubiquitin-60S ribosomal protein L40 [Ovis aries]" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 300 no REF NP_001013290 . "ubiquitin [Danio rerio]" . . . . . 100.00 610 97.37 98.68 2.40e-40 . . . . 16228 1 301 no SP B9DHA6 . "RecName: Full=Ubiquitin-60S ribosomal protein L40-1; Contains: RecName: Full=Ubiquitin; Contains: RecName: Full=60S ribosomal p" . . . . . 100.00 128 98.68 100.00 2.42e-45 . . . . 16228 1 302 no SP P0C273 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 303 no SP P0C275 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 304 no SP P0C276 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 305 no SP P0CG47 . "RecName: Full=Polyubiquitin-B; Contains: RecName: Full=Ubiquitin; Flags: Precursor" . . . . . 100.00 229 97.37 98.68 1.21e-42 . . . . 16228 1 306 no TPD FAA00319 . "TPA: polyubiquitin [Cryptococcus neoformans var. neoformans B-3501A]" . . . . . 100.00 456 97.37 100.00 3.93e-41 . . . . 16228 1 307 no TPE CAI56329 . "TPA: ubiquitin-60S ribosomal L40 fusion protein [Vitis vinifera]" . . . . . 100.00 128 97.37 98.68 2.08e-44 . . . . 16228 1 308 no TPG DAA18802 . "TPA: polyubiquitin [Bos taurus]" . . . . . 100.00 305 97.37 98.68 7.94e-42 . . . . 16228 1 309 no TPG DAA24675 . "TPA: 40S ribosomal protein S27a [Bos taurus]" . . . . . 100.00 156 97.37 98.68 2.46e-44 . . . . 16228 1 310 no TPG DAA28295 . "TPA: ubiquitin and ribosomal protein L40 [Bos taurus]" . . . . . 100.00 128 97.37 98.68 1.11e-44 . . . . 16228 1 311 no TPG DAA39608 . "TPA: Ubiquitin fusion protein [Zea mays]" . . . . . 100.00 129 98.68 100.00 1.92e-45 . . . . 16228 1 312 no TPG DAA44269 . "TPA: Ubiquitin fusion protein [Zea mays]" . . . . . 100.00 129 98.68 100.00 1.92e-45 . . . . 16228 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . MET . 16228 1 2 . GLN . 16228 1 3 . ILE . 16228 1 4 . PHE . 16228 1 5 . VAL . 16228 1 6 . LYS . 16228 1 7 . THR . 16228 1 8 . LEU . 16228 1 9 . THR . 16228 1 10 . GLY . 16228 1 11 . LYS . 16228 1 12 . THR . 16228 1 13 . ILE . 16228 1 14 . THR . 16228 1 15 . LEU . 16228 1 16 . GLU . 16228 1 17 . VAL . 16228 1 18 . GLU . 16228 1 19 . SER . 16228 1 20 . SER . 16228 1 21 . ASP . 16228 1 22 . THR . 16228 1 23 . ILE . 16228 1 24 . GLU . 16228 1 25 . ASN . 16228 1 26 . VAL . 16228 1 27 . LYS . 16228 1 28 . ALA . 16228 1 29 . LYS . 16228 1 30 . ILE . 16228 1 31 . GLN . 16228 1 32 . ASP . 16228 1 33 . LYS . 16228 1 34 . GLU . 16228 1 35 . GLY . 16228 1 36 . ILE . 16228 1 37 . PRO . 16228 1 38 . PRO . 16228 1 39 . ASP . 16228 1 40 . GLN . 16228 1 41 . GLN . 16228 1 42 . ARG . 16228 1 43 . LEU . 16228 1 44 . ILE . 16228 1 45 . PHE . 16228 1 46 . ALA . 16228 1 47 . GLY . 16228 1 48 . LYS . 16228 1 49 . GLN . 16228 1 50 . LEU . 16228 1 51 . GLU . 16228 1 52 . ASP . 16228 1 53 . GLY . 16228 1 54 . ARG . 16228 1 55 . THR . 16228 1 56 . LEU . 16228 1 57 . ALA . 16228 1 58 . ASP . 16228 1 59 . TYR . 16228 1 60 . ASN . 16228 1 61 . ILE . 16228 1 62 . GLN . 16228 1 63 . LYS . 16228 1 64 . GLU . 16228 1 65 . SER . 16228 1 66 . THR . 16228 1 67 . LEU . 16228 1 68 . HIS . 16228 1 69 . LEU . 16228 1 70 . VAL . 16228 1 71 . LEU . 16228 1 72 . ARG . 16228 1 73 . LEU . 16228 1 74 . ARG . 16228 1 75 . GLY . 16228 1 76 . GLY . 16228 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 16228 1 . GLN 2 2 16228 1 . ILE 3 3 16228 1 . PHE 4 4 16228 1 . VAL 5 5 16228 1 . LYS 6 6 16228 1 . THR 7 7 16228 1 . LEU 8 8 16228 1 . THR 9 9 16228 1 . GLY 10 10 16228 1 . LYS 11 11 16228 1 . THR 12 12 16228 1 . ILE 13 13 16228 1 . THR 14 14 16228 1 . LEU 15 15 16228 1 . GLU 16 16 16228 1 . VAL 17 17 16228 1 . GLU 18 18 16228 1 . SER 19 19 16228 1 . SER 20 20 16228 1 . ASP 21 21 16228 1 . THR 22 22 16228 1 . ILE 23 23 16228 1 . GLU 24 24 16228 1 . ASN 25 25 16228 1 . VAL 26 26 16228 1 . LYS 27 27 16228 1 . ALA 28 28 16228 1 . LYS 29 29 16228 1 . ILE 30 30 16228 1 . GLN 31 31 16228 1 . ASP 32 32 16228 1 . LYS 33 33 16228 1 . GLU 34 34 16228 1 . GLY 35 35 16228 1 . ILE 36 36 16228 1 . PRO 37 37 16228 1 . PRO 38 38 16228 1 . ASP 39 39 16228 1 . GLN 40 40 16228 1 . GLN 41 41 16228 1 . ARG 42 42 16228 1 . LEU 43 43 16228 1 . ILE 44 44 16228 1 . PHE 45 45 16228 1 . ALA 46 46 16228 1 . GLY 47 47 16228 1 . LYS 48 48 16228 1 . GLN 49 49 16228 1 . LEU 50 50 16228 1 . GLU 51 51 16228 1 . ASP 52 52 16228 1 . GLY 53 53 16228 1 . ARG 54 54 16228 1 . THR 55 55 16228 1 . LEU 56 56 16228 1 . ALA 57 57 16228 1 . ASP 58 58 16228 1 . TYR 59 59 16228 1 . ASN 60 60 16228 1 . ILE 61 61 16228 1 . GLN 62 62 16228 1 . LYS 63 63 16228 1 . GLU 64 64 16228 1 . SER 65 65 16228 1 . THR 66 66 16228 1 . LEU 67 67 16228 1 . HIS 68 68 16228 1 . LEU 69 69 16228 1 . VAL 70 70 16228 1 . LEU 71 71 16228 1 . ARG 72 72 16228 1 . LEU 73 73 16228 1 . ARG 74 74 16228 1 . GLY 75 75 16228 1 . GLY 76 76 16228 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 16228 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $ubiquitin . 3077 organism . 'Chlorella vulgaris' 'Chlorella vulgaris' . . Eukaryota Viridiplantae Chlorella vulgaris K-73122 . . . . . . . . . . . . . . . . . . . . 16228 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 16228 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $ubiquitin . 'cell free synthesis' 'Escherichia coli' . . 562 Escherichia coli . . . . . . . . . . . . . . . . N.N. . . . . . . 16228 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 16228 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 ubiquitin 'Stereo-array isotope labeling (SAIL)' . . 1 $ubiquitin . . 0.1 . . mM . . . . 16228 1 2 'sodium phosphate' 'natural abundance' . . . . . . 10 . . mM . . . . 16228 1 3 'sodium azide' 'natural abundance' . . . . . . 0.01 . . % . . . . 16228 1 4 H2O 'natural abundance' . . . . . . 90 . . % . . . . 16228 1 5 D2O 'natural abundance' . . . . . . 10 . . % . . . . 16228 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 16228 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.06 . M 16228 1 pH 6.6 . pH 16228 1 pressure 1 . atm 16228 1 temperature 310 . K 16228 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 16228 _Software.ID 1 _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' . . 16228 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 16228 1 stop_ save_ save_ANSIG _Software.Sf_category software _Software.Sf_framecode ANSIG _Software.Entry_ID 16228 _Software.ID 2 _Software.Name ANSIG _Software.Version 3.3 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Kraulis . . 16228 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 16228 2 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 16228 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 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 16228 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker DRX . 600 . . . 16228 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 16228 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 2 '2D 1H-13C HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 3 HB(CBCG)HE no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 4 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 5 '3D C(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 6 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 7 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 8 '3D HBHA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 9 '3D H(CCO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 10 '3D HCCH-COSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 11 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 12 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 1 13 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16228 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 16228 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.251449530 . . . . . . . . . 16228 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 16228 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.101329118 . . . . . . . . . 16228 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 16228 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 16228 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 MET HA H 1 4.132 0.020 . 1 . . . . 1 MET HA . 16228 1 2 . 1 1 1 1 MET HB2 H 1 1.930 0.020 . 1 . . . . 1 MET HB2 . 16228 1 3 . 1 1 1 1 MET HG2 H 1 2.403 0.020 . 1 . . . . 1 MET HG2 . 16228 1 4 . 1 1 1 1 MET C C 13 170.502 0.400 . 1 . . . . 1 MET C . 16228 1 5 . 1 1 1 1 MET CA C 13 54.442 0.400 . 1 . . . . 1 MET CA . 16228 1 6 . 1 1 1 1 MET CB C 13 32.763 0.400 . 1 . . . . 1 MET CB . 16228 1 7 . 1 1 1 1 MET CG C 13 30.120 0.400 . 1 . . . . 1 MET CG . 16228 1 8 . 1 1 2 2 GLN H H 1 8.845 0.020 . 1 . . . . 2 GLN H . 16228 1 9 . 1 1 2 2 GLN HA H 1 5.194 0.020 . 1 . . . . 2 GLN HA . 16228 1 10 . 1 1 2 2 GLN HB2 H 1 1.752 0.020 . 1 . . . . 2 GLN HB2 . 16228 1 11 . 1 1 2 2 GLN HE21 H 1 7.645 0.020 . 2 . . . . 2 GLN HE21 . 16228 1 12 . 1 1 2 2 GLN HE22 H 1 6.658 0.020 . 2 . . . . 2 GLN HE22 . 16228 1 13 . 1 1 2 2 GLN HG2 H 1 1.976 0.020 . 1 . . . . 2 GLN HG2 . 16228 1 14 . 1 1 2 2 GLN C C 13 175.822 0.400 . 1 . . . . 2 GLN C . 16228 1 15 . 1 1 2 2 GLN CA C 13 54.885 0.400 . 1 . . . . 2 GLN CA . 16228 1 16 . 1 1 2 2 GLN CB C 13 30.065 0.400 . 1 . . . . 2 GLN CB . 16228 1 17 . 1 1 2 2 GLN CG C 13 34.301 0.400 . 1 . . . . 2 GLN CG . 16228 1 18 . 1 1 2 2 GLN N N 15 122.813 0.400 . 1 . . . . 2 GLN N . 16228 1 19 . 1 1 2 2 GLN NE2 N 15 111.909 0.400 . 1 . . . . 2 GLN NE2 . 16228 1 20 . 1 1 3 3 ILE H H 1 8.252 0.020 . 1 . . . . 3 ILE H . 16228 1 21 . 1 1 3 3 ILE HA H 1 4.064 0.020 . 1 . . . . 3 ILE HA . 16228 1 22 . 1 1 3 3 ILE HB H 1 1.666 0.020 . 1 . . . . 3 ILE HB . 16228 1 23 . 1 1 3 3 ILE HD11 H 1 0.464 0.020 . 1 . . . . 3 ILE HD11 . 16228 1 24 . 1 1 3 3 ILE HD12 H 1 0.464 0.020 . 1 . . . . 3 ILE HD12 . 16228 1 25 . 1 1 3 3 ILE HD13 H 1 0.464 0.020 . 1 . . . . 3 ILE HD13 . 16228 1 26 . 1 1 3 3 ILE HG12 H 1 0.718 0.020 . 1 . . . . 3 ILE HG12 . 16228 1 27 . 1 1 3 3 ILE HG21 H 1 0.511 0.020 . 1 . . . . 3 ILE HG21 . 16228 1 28 . 1 1 3 3 ILE HG22 H 1 0.511 0.020 . 1 . . . . 3 ILE HG22 . 16228 1 29 . 1 1 3 3 ILE HG23 H 1 0.511 0.020 . 1 . . . . 3 ILE HG23 . 16228 1 30 . 1 1 3 3 ILE C C 13 172.294 0.400 . 1 . . . . 3 ILE C . 16228 1 31 . 1 1 3 3 ILE CA C 13 59.443 0.400 . 1 . . . . 3 ILE CA . 16228 1 32 . 1 1 3 3 ILE CB C 13 41.689 0.400 . 1 . . . . 3 ILE CB . 16228 1 33 . 1 1 3 3 ILE CD1 C 13 13.387 0.400 . 1 . . . . 3 ILE CD1 . 16228 1 34 . 1 1 3 3 ILE CG1 C 13 24.550 0.400 . 1 . . . . 3 ILE CG1 . 16228 1 35 . 1 1 3 3 ILE CG2 C 13 17.081 0.400 . 1 . . . . 3 ILE CG2 . 16228 1 36 . 1 1 3 3 ILE N N 15 115.378 0.400 . 1 . . . . 3 ILE N . 16228 1 37 . 1 1 4 4 PHE H H 1 8.540 0.020 . 1 . . . . 4 PHE H . 16228 1 38 . 1 1 4 4 PHE HA H 1 5.570 0.020 . 1 . . . . 4 PHE HA . 16228 1 39 . 1 1 4 4 PHE HB3 H 1 2.779 0.020 . 1 . . . . 4 PHE HB3 . 16228 1 40 . 1 1 4 4 PHE HE1 H 1 7.169 0.020 . 1 . . . . 4 PHE HE1 . 16228 1 41 . 1 1 4 4 PHE HE2 H 1 7.169 0.020 . 1 . . . . 4 PHE HE2 . 16228 1 42 . 1 1 4 4 PHE C C 13 175.045 0.400 . 1 . . . . 4 PHE C . 16228 1 43 . 1 1 4 4 PHE CA C 13 55.010 0.400 . 1 . . . . 4 PHE CA . 16228 1 44 . 1 1 4 4 PHE CB C 13 40.756 0.400 . 1 . . . . 4 PHE CB . 16228 1 45 . 1 1 4 4 PHE CE1 C 13 130.844 0.400 . 1 . . . . 4 PHE CE1 . 16228 1 46 . 1 1 4 4 PHE CE2 C 13 130.844 0.400 . 1 . . . . 4 PHE CE2 . 16228 1 47 . 1 1 4 4 PHE N N 15 118.612 0.400 . 1 . . . . 4 PHE N . 16228 1 48 . 1 1 5 5 VAL H H 1 9.223 0.020 . 1 . . . . 5 VAL H . 16228 1 49 . 1 1 5 5 VAL HA H 1 4.764 0.020 . 1 . . . . 5 VAL HA . 16228 1 50 . 1 1 5 5 VAL HB H 1 1.784 0.020 . 1 . . . . 5 VAL HB . 16228 1 51 . 1 1 5 5 VAL HG21 H 1 0.607 0.020 . 1 . . . . 5 VAL HG21 . 16228 1 52 . 1 1 5 5 VAL HG22 H 1 0.607 0.020 . 1 . . . . 5 VAL HG22 . 16228 1 53 . 1 1 5 5 VAL HG23 H 1 0.607 0.020 . 1 . . . . 5 VAL HG23 . 16228 1 54 . 1 1 5 5 VAL C C 13 174.725 0.400 . 1 . . . . 5 VAL C . 16228 1 55 . 1 1 5 5 VAL CA C 13 60.284 0.400 . 1 . . . . 5 VAL CA . 16228 1 56 . 1 1 5 5 VAL CB C 13 33.804 0.400 . 1 . . . . 5 VAL CB . 16228 1 57 . 1 1 5 5 VAL CG2 C 13 20.079 0.400 . 1 . . . . 5 VAL CG2 . 16228 1 58 . 1 1 5 5 VAL N N 15 121.208 0.400 . 1 . . . . 5 VAL N . 16228 1 59 . 1 1 6 6 LYS H H 1 8.913 0.020 . 1 . . . . 6 LYS H . 16228 1 60 . 1 1 6 6 LYS HA H 1 5.187 0.020 . 1 . . . . 6 LYS HA . 16228 1 61 . 1 1 6 6 LYS HB3 H 1 1.593 0.020 . 1 . . . . 6 LYS HB3 . 16228 1 62 . 1 1 6 6 LYS HD3 H 1 1.485 0.020 . 1 . . . . 6 LYS HD3 . 16228 1 63 . 1 1 6 6 LYS HE2 H 1 2.798 0.020 . 1 . . . . 6 LYS HE2 . 16228 1 64 . 1 1 6 6 LYS HG3 H 1 1.159 0.020 . 1 . . . . 6 LYS HG3 . 16228 1 65 . 1 1 6 6 LYS C C 13 176.996 0.400 . 1 . . . . 6 LYS C . 16228 1 66 . 1 1 6 6 LYS CA C 13 54.499 0.400 . 1 . . . . 6 LYS CA . 16228 1 67 . 1 1 6 6 LYS CB C 13 33.751 0.400 . 1 . . . . 6 LYS CB . 16228 1 68 . 1 1 6 6 LYS CD C 13 28.667 0.400 . 1 . . . . 6 LYS CD . 16228 1 69 . 1 1 6 6 LYS CE C 13 41.559 0.400 . 1 . . . . 6 LYS CE . 16228 1 70 . 1 1 6 6 LYS CG C 13 24.346 0.400 . 1 . . . . 6 LYS CG . 16228 1 71 . 1 1 6 6 LYS N N 15 127.955 0.400 . 1 . . . . 6 LYS N . 16228 1 72 . 1 1 7 7 THR H H 1 8.679 0.020 . 1 . . . . 7 THR H . 16228 1 73 . 1 1 7 7 THR HA H 1 4.854 0.020 . 1 . . . . 7 THR HA . 16228 1 74 . 1 1 7 7 THR HB H 1 4.698 0.020 . 1 . . . . 7 THR HB . 16228 1 75 . 1 1 7 7 THR HG21 H 1 1.057 0.020 . 1 . . . . 7 THR HG21 . 16228 1 76 . 1 1 7 7 THR HG22 H 1 1.057 0.020 . 1 . . . . 7 THR HG22 . 16228 1 77 . 1 1 7 7 THR HG23 H 1 1.057 0.020 . 1 . . . . 7 THR HG23 . 16228 1 78 . 1 1 7 7 THR C C 13 176.813 0.400 . 1 . . . . 7 THR C . 16228 1 79 . 1 1 7 7 THR CA C 13 60.350 0.400 . 1 . . . . 7 THR CA . 16228 1 80 . 1 1 7 7 THR CB C 13 70.480 0.400 . 1 . . . . 7 THR CB . 16228 1 81 . 1 1 7 7 THR CG2 C 13 20.920 0.400 . 1 . . . . 7 THR CG2 . 16228 1 82 . 1 1 7 7 THR N N 15 115.451 0.400 . 1 . . . . 7 THR N . 16228 1 83 . 1 1 8 8 LEU H H 1 9.032 0.020 . 1 . . . . 8 LEU H . 16228 1 84 . 1 1 8 8 LEU HA H 1 4.216 0.020 . 1 . . . . 8 LEU HA . 16228 1 85 . 1 1 8 8 LEU HB3 H 1 1.654 0.020 . 1 . . . . 8 LEU HB3 . 16228 1 86 . 1 1 8 8 LEU HD11 H 1 0.928 0.020 . 1 . . . . 8 LEU HD11 . 16228 1 87 . 1 1 8 8 LEU HD12 H 1 0.928 0.020 . 1 . . . . 8 LEU HD12 . 16228 1 88 . 1 1 8 8 LEU HD13 H 1 0.928 0.020 . 1 . . . . 8 LEU HD13 . 16228 1 89 . 1 1 8 8 LEU HG H 1 1.770 0.020 . 1 . . . . 8 LEU HG . 16228 1 90 . 1 1 8 8 LEU C C 13 178.734 0.400 . 1 . . . . 8 LEU C . 16228 1 91 . 1 1 8 8 LEU CA C 13 57.381 0.400 . 1 . . . . 8 LEU CA . 16228 1 92 . 1 1 8 8 LEU CB C 13 41.482 0.400 . 1 . . . . 8 LEU CB . 16228 1 93 . 1 1 8 8 LEU CD1 C 13 24.671 0.400 . 1 . . . . 8 LEU CD1 . 16228 1 94 . 1 1 8 8 LEU CG C 13 26.900 0.400 . 1 . . . . 8 LEU CG . 16228 1 95 . 1 1 8 8 LEU N N 15 121.183 0.400 . 1 . . . . 8 LEU N . 16228 1 96 . 1 1 9 9 THR H H 1 7.571 0.020 . 1 . . . . 9 THR H . 16228 1 97 . 1 1 9 9 THR HA H 1 4.340 0.020 . 1 . . . . 9 THR HA . 16228 1 98 . 1 1 9 9 THR HB H 1 4.497 0.020 . 1 . . . . 9 THR HB . 16228 1 99 . 1 1 9 9 THR HG21 H 1 1.151 0.020 . 1 . . . . 9 THR HG21 . 16228 1 100 . 1 1 9 9 THR HG22 H 1 1.151 0.020 . 1 . . . . 9 THR HG22 . 16228 1 101 . 1 1 9 9 THR HG23 H 1 1.151 0.020 . 1 . . . . 9 THR HG23 . 16228 1 102 . 1 1 9 9 THR C C 13 175.401 0.400 . 1 . . . . 9 THR C . 16228 1 103 . 1 1 9 9 THR CA C 13 61.365 0.400 . 1 . . . . 9 THR CA . 16228 1 104 . 1 1 9 9 THR CB C 13 68.964 0.400 . 1 . . . . 9 THR CB . 16228 1 105 . 1 1 9 9 THR CG2 C 13 21.360 0.400 . 1 . . . . 9 THR CG2 . 16228 1 106 . 1 1 9 9 THR N N 15 105.862 0.400 . 1 . . . . 9 THR N . 16228 1 107 . 1 1 10 10 GLY H H 1 7.763 0.020 . 1 . . . . 10 GLY H . 16228 1 108 . 1 1 10 10 GLY HA2 H 1 3.510 0.020 . 1 . . . . 10 GLY HA2 . 16228 1 109 . 1 1 10 10 GLY C C 13 173.855 0.400 . 1 . . . . 10 GLY C . 16228 1 110 . 1 1 10 10 GLY CA C 13 45.113 0.400 . 1 . . . . 10 GLY CA . 16228 1 111 . 1 1 10 10 GLY N N 15 109.118 0.400 . 1 . . . . 10 GLY N . 16228 1 112 . 1 1 11 11 LYS H H 1 7.213 0.020 . 1 . . . . 11 LYS H . 16228 1 113 . 1 1 11 11 LYS HA H 1 4.269 0.020 . 1 . . . . 11 LYS HA . 16228 1 114 . 1 1 11 11 LYS HB3 H 1 1.688 0.020 . 1 . . . . 11 LYS HB3 . 16228 1 115 . 1 1 11 11 LYS HD3 H 1 1.496 0.020 . 1 . . . . 11 LYS HD3 . 16228 1 116 . 1 1 11 11 LYS HE2 H 1 2.806 0.020 . 1 . . . . 11 LYS HE2 . 16228 1 117 . 1 1 11 11 LYS HG3 H 1 1.294 0.020 . 1 . . . . 11 LYS HG3 . 16228 1 118 . 1 1 11 11 LYS C C 13 175.657 0.400 . 1 . . . . 11 LYS C . 16228 1 119 . 1 1 11 11 LYS CA C 13 56.194 0.400 . 1 . . . . 11 LYS CA . 16228 1 120 . 1 1 11 11 LYS CB C 13 32.932 0.400 . 1 . . . . 11 LYS CB . 16228 1 121 . 1 1 11 11 LYS CD C 13 28.820 0.400 . 1 . . . . 11 LYS CD . 16228 1 122 . 1 1 11 11 LYS CE C 13 41.555 0.400 . 1 . . . . 11 LYS CE . 16228 1 123 . 1 1 11 11 LYS CG C 13 24.468 0.400 . 1 . . . . 11 LYS CG . 16228 1 124 . 1 1 11 11 LYS N N 15 121.919 0.400 . 1 . . . . 11 LYS N . 16228 1 125 . 1 1 12 12 THR H H 1 8.554 0.020 . 1 . . . . 12 THR H . 16228 1 126 . 1 1 12 12 THR HA H 1 4.990 0.020 . 1 . . . . 12 THR HA . 16228 1 127 . 1 1 12 12 THR HB H 1 3.853 0.020 . 1 . . . . 12 THR HB . 16228 1 128 . 1 1 12 12 THR HG21 H 1 0.958 0.020 . 1 . . . . 12 THR HG21 . 16228 1 129 . 1 1 12 12 THR HG22 H 1 0.958 0.020 . 1 . . . . 12 THR HG22 . 16228 1 130 . 1 1 12 12 THR HG23 H 1 0.958 0.020 . 1 . . . . 12 THR HG23 . 16228 1 131 . 1 1 12 12 THR C C 13 174.220 0.400 . 1 . . . . 12 THR C . 16228 1 132 . 1 1 12 12 THR CA C 13 62.264 0.400 . 1 . . . . 12 THR CA . 16228 1 133 . 1 1 12 12 THR CB C 13 69.640 0.400 . 1 . . . . 12 THR CB . 16228 1 134 . 1 1 12 12 THR CG2 C 13 21.394 0.400 . 1 . . . . 12 THR CG2 . 16228 1 135 . 1 1 12 12 THR N N 15 120.566 0.400 . 1 . . . . 12 THR N . 16228 1 136 . 1 1 13 13 ILE H H 1 9.493 0.020 . 1 . . . . 13 ILE H . 16228 1 137 . 1 1 13 13 ILE HA H 1 4.441 0.020 . 1 . . . . 13 ILE HA . 16228 1 138 . 1 1 13 13 ILE HB H 1 1.778 0.020 . 1 . . . . 13 ILE HB . 16228 1 139 . 1 1 13 13 ILE HD11 H 1 0.600 0.020 . 1 . . . . 13 ILE HD11 . 16228 1 140 . 1 1 13 13 ILE HD12 H 1 0.600 0.020 . 1 . . . . 13 ILE HD12 . 16228 1 141 . 1 1 13 13 ILE HD13 H 1 0.600 0.020 . 1 . . . . 13 ILE HD13 . 16228 1 142 . 1 1 13 13 ILE HG12 H 1 0.997 0.020 . 1 . . . . 13 ILE HG12 . 16228 1 143 . 1 1 13 13 ILE HG21 H 1 0.764 0.020 . 1 . . . . 13 ILE HG21 . 16228 1 144 . 1 1 13 13 ILE HG22 H 1 0.764 0.020 . 1 . . . . 13 ILE HG22 . 16228 1 145 . 1 1 13 13 ILE HG23 H 1 0.764 0.020 . 1 . . . . 13 ILE HG23 . 16228 1 146 . 1 1 13 13 ILE C C 13 175.069 0.400 . 1 . . . . 13 ILE C . 16228 1 147 . 1 1 13 13 ILE CA C 13 59.934 0.400 . 1 . . . . 13 ILE CA . 16228 1 148 . 1 1 13 13 ILE CB C 13 40.438 0.400 . 1 . . . . 13 ILE CB . 16228 1 149 . 1 1 13 13 ILE CD1 C 13 13.677 0.400 . 1 . . . . 13 ILE CD1 . 16228 1 150 . 1 1 13 13 ILE CG1 C 13 26.308 0.400 . 1 . . . . 13 ILE CG1 . 16228 1 151 . 1 1 13 13 ILE CG2 C 13 17.137 0.400 . 1 . . . . 13 ILE CG2 . 16228 1 152 . 1 1 13 13 ILE N N 15 127.547 0.400 . 1 . . . . 13 ILE N . 16228 1 153 . 1 1 14 14 THR H H 1 8.646 0.020 . 1 . . . . 14 THR H . 16228 1 154 . 1 1 14 14 THR HA H 1 4.898 0.020 . 1 . . . . 14 THR HA . 16228 1 155 . 1 1 14 14 THR HB H 1 3.951 0.020 . 1 . . . . 14 THR HB . 16228 1 156 . 1 1 14 14 THR HG21 H 1 1.025 0.020 . 1 . . . . 14 THR HG21 . 16228 1 157 . 1 1 14 14 THR HG22 H 1 1.025 0.020 . 1 . . . . 14 THR HG22 . 16228 1 158 . 1 1 14 14 THR HG23 H 1 1.025 0.020 . 1 . . . . 14 THR HG23 . 16228 1 159 . 1 1 14 14 THR C C 13 173.611 0.400 . 1 . . . . 14 THR C . 16228 1 160 . 1 1 14 14 THR CA C 13 61.953 0.400 . 1 . . . . 14 THR CA . 16228 1 161 . 1 1 14 14 THR CB C 13 69.519 0.400 . 1 . . . . 14 THR CB . 16228 1 162 . 1 1 14 14 THR CG2 C 13 21.296 0.400 . 1 . . . . 14 THR CG2 . 16228 1 163 . 1 1 14 14 THR N N 15 121.434 0.400 . 1 . . . . 14 THR N . 16228 1 164 . 1 1 15 15 LEU H H 1 8.691 0.020 . 1 . . . . 15 LEU H . 16228 1 165 . 1 1 15 15 LEU HA H 1 4.661 0.020 . 1 . . . . 15 LEU HA . 16228 1 166 . 1 1 15 15 LEU HB3 H 1 1.107 0.020 . 1 . . . . 15 LEU HB3 . 16228 1 167 . 1 1 15 15 LEU HD11 H 1 0.583 0.020 . 1 . . . . 15 LEU HD11 . 16228 1 168 . 1 1 15 15 LEU HD12 H 1 0.583 0.020 . 1 . . . . 15 LEU HD12 . 16228 1 169 . 1 1 15 15 LEU HD13 H 1 0.583 0.020 . 1 . . . . 15 LEU HD13 . 16228 1 170 . 1 1 15 15 LEU HG H 1 1.308 0.020 . 1 . . . . 15 LEU HG . 16228 1 171 . 1 1 15 15 LEU C C 13 174.423 0.400 . 1 . . . . 15 LEU C . 16228 1 172 . 1 1 15 15 LEU CA C 13 52.680 0.400 . 1 . . . . 15 LEU CA . 16228 1 173 . 1 1 15 15 LEU CB C 13 46.289 0.400 . 1 . . . . 15 LEU CB . 16228 1 174 . 1 1 15 15 LEU CD1 C 13 26.183 0.400 . 1 . . . . 15 LEU CD1 . 16228 1 175 . 1 1 15 15 LEU CG C 13 26.231 0.400 . 1 . . . . 15 LEU CG . 16228 1 176 . 1 1 15 15 LEU N N 15 125.098 0.400 . 1 . . . . 15 LEU N . 16228 1 177 . 1 1 16 16 GLU H H 1 8.052 0.020 . 1 . . . . 16 GLU H . 16228 1 178 . 1 1 16 16 GLU HA H 1 4.805 0.020 . 1 . . . . 16 GLU HA . 16228 1 179 . 1 1 16 16 GLU HB2 H 1 1.731 0.020 . 1 . . . . 16 GLU HB2 . 16228 1 180 . 1 1 16 16 GLU HG2 H 1 2.135 0.020 . 1 . . . . 16 GLU HG2 . 16228 1 181 . 1 1 16 16 GLU C C 13 175.723 0.400 . 1 . . . . 16 GLU C . 16228 1 182 . 1 1 16 16 GLU CA C 13 54.777 0.400 . 1 . . . . 16 GLU CA . 16228 1 183 . 1 1 16 16 GLU CB C 13 29.377 0.400 . 1 . . . . 16 GLU CB . 16228 1 184 . 1 1 16 16 GLU CG C 13 35.148 0.400 . 1 . . . . 16 GLU CG . 16228 1 185 . 1 1 16 16 GLU N N 15 122.395 0.400 . 1 . . . . 16 GLU N . 16228 1 186 . 1 1 17 17 VAL H H 1 8.872 0.020 . 1 . . . . 17 VAL H . 16228 1 187 . 1 1 17 17 VAL HA H 1 4.611 0.020 . 1 . . . . 17 VAL HA . 16228 1 188 . 1 1 17 17 VAL HB H 1 2.246 0.020 . 1 . . . . 17 VAL HB . 16228 1 189 . 1 1 17 17 VAL HG21 H 1 0.317 0.020 . 1 . . . . 17 VAL HG21 . 16228 1 190 . 1 1 17 17 VAL HG22 H 1 0.317 0.020 . 1 . . . . 17 VAL HG22 . 16228 1 191 . 1 1 17 17 VAL HG23 H 1 0.317 0.020 . 1 . . . . 17 VAL HG23 . 16228 1 192 . 1 1 17 17 VAL C C 13 174.005 0.400 . 1 . . . . 17 VAL C . 16228 1 193 . 1 1 17 17 VAL CA C 13 58.470 0.400 . 1 . . . . 17 VAL CA . 16228 1 194 . 1 1 17 17 VAL CB C 13 35.961 0.400 . 1 . . . . 17 VAL CB . 16228 1 195 . 1 1 17 17 VAL CG2 C 13 18.712 0.400 . 1 . . . . 17 VAL CG2 . 16228 1 196 . 1 1 17 17 VAL N N 15 117.658 0.400 . 1 . . . . 17 VAL N . 16228 1 197 . 1 1 18 18 GLU H H 1 8.539 0.020 . 1 . . . . 18 GLU H . 16228 1 198 . 1 1 18 18 GLU HA H 1 4.777 0.020 . 1 . . . . 18 GLU HA . 16228 1 199 . 1 1 18 18 GLU HB2 H 1 1.579 0.020 . 1 . . . . 18 GLU HB2 . 16228 1 200 . 1 1 18 18 GLU HG2 H 1 2.131 0.020 . 1 . . . . 18 GLU HG2 . 16228 1 201 . 1 1 18 18 GLU C C 13 178.051 0.400 . 1 . . . . 18 GLU C . 16228 1 202 . 1 1 18 18 GLU CA C 13 53.612 0.400 . 1 . . . . 18 GLU CA . 16228 1 203 . 1 1 18 18 GLU CB C 13 31.877 0.400 . 1 . . . . 18 GLU CB . 16228 1 204 . 1 1 18 18 GLU CG C 13 35.133 0.400 . 1 . . . . 18 GLU CG . 16228 1 205 . 1 1 18 18 GLU N N 15 118.737 0.400 . 1 . . . . 18 GLU N . 16228 1 206 . 1 1 19 19 SER H H 1 9.231 0.020 . 1 . . . . 19 SER H . 16228 1 207 . 1 1 19 19 SER HA H 1 3.873 0.020 . 1 . . . . 19 SER HA . 16228 1 208 . 1 1 19 19 SER HB3 H 1 3.801 0.020 . 1 . . . . 19 SER HB3 . 16228 1 209 . 1 1 19 19 SER C C 13 172.934 0.400 . 1 . . . . 19 SER C . 16228 1 210 . 1 1 19 19 SER CA C 13 62.048 0.400 . 1 . . . . 19 SER CA . 16228 1 211 . 1 1 19 19 SER CB C 13 62.256 0.400 . 1 . . . . 19 SER CB . 16228 1 212 . 1 1 19 19 SER N N 15 117.883 0.400 . 1 . . . . 19 SER N . 16228 1 213 . 1 1 20 20 SER H H 1 7.206 0.020 . 1 . . . . 20 SER H . 16228 1 214 . 1 1 20 20 SER HA H 1 4.296 0.020 . 1 . . . . 20 SER HA . 16228 1 215 . 1 1 20 20 SER HB3 H 1 3.669 0.020 . 1 . . . . 20 SER HB3 . 16228 1 216 . 1 1 20 20 SER C C 13 174.493 0.400 . 1 . . . . 20 SER C . 16228 1 217 . 1 1 20 20 SER CA C 13 57.173 0.400 . 1 . . . . 20 SER CA . 16228 1 218 . 1 1 20 20 SER CB C 13 63.197 0.400 . 1 . . . . 20 SER CB . 16228 1 219 . 1 1 20 20 SER N N 15 108.227 0.400 . 1 . . . . 20 SER N . 16228 1 220 . 1 1 21 21 ASP H H 1 7.807 0.020 . 1 . . . . 21 ASP H . 16228 1 221 . 1 1 21 21 ASP HA H 1 4.599 0.020 . 1 . . . . 21 ASP HA . 16228 1 222 . 1 1 21 21 ASP HB2 H 1 2.437 0.020 . 1 . . . . 21 ASP HB2 . 16228 1 223 . 1 1 21 21 ASP C C 13 176.149 0.400 . 1 . . . . 21 ASP C . 16228 1 224 . 1 1 21 21 ASP CA C 13 55.742 0.400 . 1 . . . . 21 ASP CA . 16228 1 225 . 1 1 21 21 ASP CB C 13 40.539 0.400 . 1 . . . . 21 ASP CB . 16228 1 226 . 1 1 21 21 ASP N N 15 123.497 0.400 . 1 . . . . 21 ASP N . 16228 1 227 . 1 1 22 22 THR H H 1 7.815 0.020 . 1 . . . . 22 THR H . 16228 1 228 . 1 1 22 22 THR HA H 1 4.841 0.020 . 1 . . . . 22 THR HA . 16228 1 229 . 1 1 22 22 THR HB H 1 4.726 0.020 . 1 . . . . 22 THR HB . 16228 1 230 . 1 1 22 22 THR HG21 H 1 1.157 0.020 . 1 . . . . 22 THR HG21 . 16228 1 231 . 1 1 22 22 THR HG22 H 1 1.157 0.020 . 1 . . . . 22 THR HG22 . 16228 1 232 . 1 1 22 22 THR HG23 H 1 1.157 0.020 . 1 . . . . 22 THR HG23 . 16228 1 233 . 1 1 22 22 THR C C 13 176.649 0.400 . 1 . . . . 22 THR C . 16228 1 234 . 1 1 22 22 THR CA C 13 59.592 0.400 . 1 . . . . 22 THR CA . 16228 1 235 . 1 1 22 22 THR CB C 13 71.133 0.400 . 1 . . . . 22 THR CB . 16228 1 236 . 1 1 22 22 THR CG2 C 13 21.752 0.400 . 1 . . . . 22 THR CG2 . 16228 1 237 . 1 1 22 22 THR N N 15 108.940 0.400 . 1 . . . . 22 THR N . 16228 1 238 . 1 1 23 23 ILE H H 1 8.461 0.020 . 1 . . . . 23 ILE H . 16228 1 239 . 1 1 23 23 ILE HA H 1 3.548 0.020 . 1 . . . . 23 ILE HA . 16228 1 240 . 1 1 23 23 ILE HB H 1 2.364 0.020 . 1 . . . . 23 ILE HB . 16228 1 241 . 1 1 23 23 ILE HD11 H 1 0.453 0.020 . 1 . . . . 23 ILE HD11 . 16228 1 242 . 1 1 23 23 ILE HD12 H 1 0.453 0.020 . 1 . . . . 23 ILE HD12 . 16228 1 243 . 1 1 23 23 ILE HD13 H 1 0.453 0.020 . 1 . . . . 23 ILE HD13 . 16228 1 244 . 1 1 23 23 ILE HG12 H 1 1.778 0.020 . 1 . . . . 23 ILE HG12 . 16228 1 245 . 1 1 23 23 ILE HG21 H 1 0.671 0.020 . 1 . . . . 23 ILE HG21 . 16228 1 246 . 1 1 23 23 ILE HG22 H 1 0.671 0.020 . 1 . . . . 23 ILE HG22 . 16228 1 247 . 1 1 23 23 ILE HG23 H 1 0.671 0.020 . 1 . . . . 23 ILE HG23 . 16228 1 248 . 1 1 23 23 ILE C C 13 178.757 0.400 . 1 . . . . 23 ILE C . 16228 1 249 . 1 1 23 23 ILE CA C 13 62.318 0.400 . 1 . . . . 23 ILE CA . 16228 1 250 . 1 1 23 23 ILE CB C 13 34.336 0.400 . 1 . . . . 23 ILE CB . 16228 1 251 . 1 1 23 23 ILE CD1 C 13 8.608 0.400 . 1 . . . . 23 ILE CD1 . 16228 1 252 . 1 1 23 23 ILE CG1 C 13 27.267 0.400 . 1 . . . . 23 ILE CG1 . 16228 1 253 . 1 1 23 23 ILE CG2 C 13 17.462 0.400 . 1 . . . . 23 ILE CG2 . 16228 1 254 . 1 1 23 23 ILE N N 15 121.239 0.400 . 1 . . . . 23 ILE N . 16228 1 255 . 1 1 24 24 GLU H H 1 10.041 0.020 . 1 . . . . 24 GLU H . 16228 1 256 . 1 1 24 24 GLU HA H 1 3.803 0.020 . 1 . . . . 24 GLU HA . 16228 1 257 . 1 1 24 24 GLU HB2 H 1 1.915 0.020 . 1 . . . . 24 GLU HB2 . 16228 1 258 . 1 1 24 24 GLU HG2 H 1 2.292 0.020 . 1 . . . . 24 GLU HG2 . 16228 1 259 . 1 1 24 24 GLU C C 13 178.928 0.400 . 1 . . . . 24 GLU C . 16228 1 260 . 1 1 24 24 GLU CA C 13 60.612 0.400 . 1 . . . . 24 GLU CA . 16228 1 261 . 1 1 24 24 GLU CB C 13 28.262 0.400 . 1 . . . . 24 GLU CB . 16228 1 262 . 1 1 24 24 GLU CG C 13 35.840 0.400 . 1 . . . . 24 GLU CG . 16228 1 263 . 1 1 24 24 GLU N N 15 121.174 0.400 . 1 . . . . 24 GLU N . 16228 1 264 . 1 1 25 25 ASN H H 1 7.881 0.020 . 1 . . . . 25 ASN H . 16228 1 265 . 1 1 25 25 ASN HA H 1 4.462 0.020 . 1 . . . . 25 ASN HA . 16228 1 266 . 1 1 25 25 ASN HB2 H 1 3.126 0.020 . 1 . . . . 25 ASN HB2 . 16228 1 267 . 1 1 25 25 ASN HD21 H 1 7.773 0.020 . 2 . . . . 25 ASN HD21 . 16228 1 268 . 1 1 25 25 ASN HD22 H 1 6.821 0.020 . 2 . . . . 25 ASN HD22 . 16228 1 269 . 1 1 25 25 ASN C C 13 178.200 0.400 . 1 . . . . 25 ASN C . 16228 1 270 . 1 1 25 25 ASN CA C 13 55.910 0.400 . 1 . . . . 25 ASN CA . 16228 1 271 . 1 1 25 25 ASN CB C 13 38.288 0.400 . 1 . . . . 25 ASN CB . 16228 1 272 . 1 1 25 25 ASN N N 15 121.430 0.400 . 1 . . . . 25 ASN N . 16228 1 273 . 1 1 25 25 ASN ND2 N 15 109.874 0.400 . 1 . . . . 25 ASN ND2 . 16228 1 274 . 1 1 26 26 VAL H H 1 8.051 0.020 . 1 . . . . 26 VAL H . 16228 1 275 . 1 1 26 26 VAL HA H 1 3.316 0.020 . 1 . . . . 26 VAL HA . 16228 1 276 . 1 1 26 26 VAL HB H 1 2.237 0.020 . 1 . . . . 26 VAL HB . 16228 1 277 . 1 1 26 26 VAL HG21 H 1 0.850 0.020 . 1 . . . . 26 VAL HG21 . 16228 1 278 . 1 1 26 26 VAL HG22 H 1 0.850 0.020 . 1 . . . . 26 VAL HG22 . 16228 1 279 . 1 1 26 26 VAL HG23 H 1 0.850 0.020 . 1 . . . . 26 VAL HG23 . 16228 1 280 . 1 1 26 26 VAL C C 13 177.838 0.400 . 1 . . . . 26 VAL C . 16228 1 281 . 1 1 26 26 VAL CA C 13 67.556 0.400 . 1 . . . . 26 VAL CA . 16228 1 282 . 1 1 26 26 VAL CB C 13 30.323 0.400 . 1 . . . . 26 VAL CB . 16228 1 283 . 1 1 26 26 VAL CG2 C 13 22.793 0.400 . 1 . . . . 26 VAL CG2 . 16228 1 284 . 1 1 26 26 VAL N N 15 122.089 0.400 . 1 . . . . 26 VAL N . 16228 1 285 . 1 1 27 27 LYS H H 1 8.493 0.020 . 1 . . . . 27 LYS H . 16228 1 286 . 1 1 27 27 LYS HA H 1 4.495 0.020 . 1 . . . . 27 LYS HA . 16228 1 287 . 1 1 27 27 LYS HB3 H 1 1.339 0.020 . 1 . . . . 27 LYS HB3 . 16228 1 288 . 1 1 27 27 LYS HD3 H 1 1.592 0.020 . 1 . . . . 27 LYS HD3 . 16228 1 289 . 1 1 27 27 LYS HE2 H 1 2.546 0.020 . 1 . . . . 27 LYS HE2 . 16228 1 290 . 1 1 27 27 LYS HG3 H 1 1.458 0.020 . 1 . . . . 27 LYS HG3 . 16228 1 291 . 1 1 27 27 LYS C C 13 180.396 0.400 . 1 . . . . 27 LYS C . 16228 1 292 . 1 1 27 27 LYS CA C 13 59.075 0.400 . 1 . . . . 27 LYS CA . 16228 1 293 . 1 1 27 27 LYS CB C 13 33.177 0.400 . 1 . . . . 27 LYS CB . 16228 1 294 . 1 1 27 27 LYS CD C 13 29.814 0.400 . 1 . . . . 27 LYS CD . 16228 1 295 . 1 1 27 27 LYS CE C 13 41.943 0.400 . 1 . . . . 27 LYS CE . 16228 1 296 . 1 1 27 27 LYS CG C 13 25.405 0.400 . 1 . . . . 27 LYS CG . 16228 1 297 . 1 1 27 27 LYS N N 15 118.889 0.400 . 1 . . . . 27 LYS N . 16228 1 298 . 1 1 28 28 ALA H H 1 7.924 0.020 . 1 . . . . 28 ALA H . 16228 1 299 . 1 1 28 28 ALA HA H 1 4.073 0.020 . 1 . . . . 28 ALA HA . 16228 1 300 . 1 1 28 28 ALA HB1 H 1 1.526 0.020 . 1 . . . . 28 ALA HB1 . 16228 1 301 . 1 1 28 28 ALA HB2 H 1 1.526 0.020 . 1 . . . . 28 ALA HB2 . 16228 1 302 . 1 1 28 28 ALA HB3 H 1 1.526 0.020 . 1 . . . . 28 ALA HB3 . 16228 1 303 . 1 1 28 28 ALA C C 13 180.149 0.400 . 1 . . . . 28 ALA C . 16228 1 304 . 1 1 28 28 ALA CA C 13 55.218 0.400 . 1 . . . . 28 ALA CA . 16228 1 305 . 1 1 28 28 ALA CB C 13 17.218 0.400 . 1 . . . . 28 ALA CB . 16228 1 306 . 1 1 28 28 ALA N N 15 123.395 0.400 . 1 . . . . 28 ALA N . 16228 1 307 . 1 1 29 29 LYS H H 1 7.801 0.020 . 1 . . . . 29 LYS H . 16228 1 308 . 1 1 29 29 LYS HA H 1 4.119 0.020 . 1 . . . . 29 LYS HA . 16228 1 309 . 1 1 29 29 LYS HB3 H 1 1.833 0.020 . 1 . . . . 29 LYS HB3 . 16228 1 310 . 1 1 29 29 LYS HD3 H 1 1.676 0.020 . 1 . . . . 29 LYS HD3 . 16228 1 311 . 1 1 29 29 LYS HE2 H 1 2.885 0.020 . 1 . . . . 29 LYS HE2 . 16228 1 312 . 1 1 29 29 LYS HG3 H 1 1.682 0.020 . 1 . . . . 29 LYS HG3 . 16228 1 313 . 1 1 29 29 LYS C C 13 180.202 0.400 . 1 . . . . 29 LYS C . 16228 1 314 . 1 1 29 29 LYS CA C 13 59.642 0.400 . 1 . . . . 29 LYS CA . 16228 1 315 . 1 1 29 29 LYS CB C 13 32.791 0.400 . 1 . . . . 29 LYS CB . 16228 1 316 . 1 1 29 29 LYS CD C 13 29.500 0.400 . 1 . . . . 29 LYS CD . 16228 1 317 . 1 1 29 29 LYS CE C 13 42.078 0.400 . 1 . . . . 29 LYS CE . 16228 1 318 . 1 1 29 29 LYS CG C 13 25.880 0.400 . 1 . . . . 29 LYS CG . 16228 1 319 . 1 1 29 29 LYS N N 15 120.260 0.400 . 1 . . . . 29 LYS N . 16228 1 320 . 1 1 30 30 ILE H H 1 8.216 0.020 . 1 . . . . 30 ILE H . 16228 1 321 . 1 1 30 30 ILE HA H 1 3.420 0.020 . 1 . . . . 30 ILE HA . 16228 1 322 . 1 1 30 30 ILE HB H 1 2.256 0.020 . 1 . . . . 30 ILE HB . 16228 1 323 . 1 1 30 30 ILE HD11 H 1 0.768 0.020 . 1 . . . . 30 ILE HD11 . 16228 1 324 . 1 1 30 30 ILE HD12 H 1 0.768 0.020 . 1 . . . . 30 ILE HD12 . 16228 1 325 . 1 1 30 30 ILE HD13 H 1 0.768 0.020 . 1 . . . . 30 ILE HD13 . 16228 1 326 . 1 1 30 30 ILE HG12 H 1 0.565 0.020 . 1 . . . . 30 ILE HG12 . 16228 1 327 . 1 1 30 30 ILE HG21 H 1 0.577 0.020 . 1 . . . . 30 ILE HG21 . 16228 1 328 . 1 1 30 30 ILE HG22 H 1 0.577 0.020 . 1 . . . . 30 ILE HG22 . 16228 1 329 . 1 1 30 30 ILE HG23 H 1 0.577 0.020 . 1 . . . . 30 ILE HG23 . 16228 1 330 . 1 1 30 30 ILE C C 13 178.107 0.400 . 1 . . . . 30 ILE C . 16228 1 331 . 1 1 30 30 ILE CA C 13 66.054 0.400 . 1 . . . . 30 ILE CA . 16228 1 332 . 1 1 30 30 ILE CB C 13 36.470 0.400 . 1 . . . . 30 ILE CB . 16228 1 333 . 1 1 30 30 ILE CD1 C 13 14.477 0.400 . 1 . . . . 30 ILE CD1 . 16228 1 334 . 1 1 30 30 ILE CG1 C 13 30.526 0.400 . 1 . . . . 30 ILE CG1 . 16228 1 335 . 1 1 30 30 ILE CG2 C 13 16.540 0.400 . 1 . . . . 30 ILE CG2 . 16228 1 336 . 1 1 30 30 ILE N N 15 121.299 0.400 . 1 . . . . 30 ILE N . 16228 1 337 . 1 1 31 31 GLN H H 1 8.492 0.020 . 1 . . . . 31 GLN H . 16228 1 338 . 1 1 31 31 GLN HA H 1 3.739 0.020 . 1 . . . . 31 GLN HA . 16228 1 339 . 1 1 31 31 GLN HB2 H 1 1.878 0.020 . 1 . . . . 31 GLN HB2 . 16228 1 340 . 1 1 31 31 GLN HE21 H 1 7.578 0.020 . 2 . . . . 31 GLN HE21 . 16228 1 341 . 1 1 31 31 GLN HE22 H 1 6.740 0.020 . 2 . . . . 31 GLN HE22 . 16228 1 342 . 1 1 31 31 GLN HG2 H 1 2.182 0.020 . 1 . . . . 31 GLN HG2 . 16228 1 343 . 1 1 31 31 GLN C C 13 178.714 0.400 . 1 . . . . 31 GLN C . 16228 1 344 . 1 1 31 31 GLN CA C 13 59.919 0.400 . 1 . . . . 31 GLN CA . 16228 1 345 . 1 1 31 31 GLN CB C 13 27.327 0.400 . 1 . . . . 31 GLN CB . 16228 1 346 . 1 1 31 31 GLN CG C 13 33.372 0.400 . 1 . . . . 31 GLN CG . 16228 1 347 . 1 1 31 31 GLN N N 15 123.486 0.400 . 1 . . . . 31 GLN N . 16228 1 348 . 1 1 31 31 GLN NE2 N 15 109.994 0.400 . 1 . . . . 31 GLN NE2 . 16228 1 349 . 1 1 32 32 ASP H H 1 7.946 0.020 . 1 . . . . 32 ASP H . 16228 1 350 . 1 1 32 32 ASP HA H 1 4.254 0.020 . 1 . . . . 32 ASP HA . 16228 1 351 . 1 1 32 32 ASP HB2 H 1 2.746 0.020 . 1 . . . . 32 ASP HB2 . 16228 1 352 . 1 1 32 32 ASP C C 13 177.198 0.400 . 1 . . . . 32 ASP C . 16228 1 353 . 1 1 32 32 ASP CA C 13 57.382 0.400 . 1 . . . . 32 ASP CA . 16228 1 354 . 1 1 32 32 ASP CB C 13 40.891 0.400 . 1 . . . . 32 ASP CB . 16228 1 355 . 1 1 32 32 ASP N N 15 119.741 0.400 . 1 . . . . 32 ASP N . 16228 1 356 . 1 1 33 33 LYS H H 1 7.367 0.020 . 1 . . . . 33 LYS H . 16228 1 357 . 1 1 33 33 LYS HA H 1 4.229 0.020 . 1 . . . . 33 LYS HA . 16228 1 358 . 1 1 33 33 LYS HB3 H 1 1.915 0.020 . 1 . . . . 33 LYS HB3 . 16228 1 359 . 1 1 33 33 LYS HD3 H 1 1.627 0.020 . 1 . . . . 33 LYS HD3 . 16228 1 360 . 1 1 33 33 LYS HE2 H 1 3.016 0.020 . 1 . . . . 33 LYS HE2 . 16228 1 361 . 1 1 33 33 LYS HG3 H 1 1.477 0.020 . 1 . . . . 33 LYS HG3 . 16228 1 362 . 1 1 33 33 LYS C C 13 177.717 0.400 . 1 . . . . 33 LYS C . 16228 1 363 . 1 1 33 33 LYS CA C 13 57.864 0.400 . 1 . . . . 33 LYS CA . 16228 1 364 . 1 1 33 33 LYS CB C 13 33.485 0.400 . 1 . . . . 33 LYS CB . 16228 1 365 . 1 1 33 33 LYS CD C 13 28.230 0.400 . 1 . . . . 33 LYS CD . 16228 1 366 . 1 1 33 33 LYS CE C 13 41.821 0.400 . 1 . . . . 33 LYS CE . 16228 1 367 . 1 1 33 33 LYS CG C 13 24.659 0.400 . 1 . . . . 33 LYS CG . 16228 1 368 . 1 1 33 33 LYS N N 15 115.402 0.400 . 1 . . . . 33 LYS N . 16228 1 369 . 1 1 34 34 GLU H H 1 8.659 0.020 . 1 . . . . 34 GLU H . 16228 1 370 . 1 1 34 34 GLU HA H 1 4.490 0.020 . 1 . . . . 34 GLU HA . 16228 1 371 . 1 1 34 34 GLU HB2 H 1 1.586 0.020 . 1 . . . . 34 GLU HB2 . 16228 1 372 . 1 1 34 34 GLU HG2 H 1 1.966 0.020 . 1 . . . . 34 GLU HG2 . 16228 1 373 . 1 1 34 34 GLU C C 13 177.826 0.400 . 1 . . . . 34 GLU C . 16228 1 374 . 1 1 34 34 GLU CA C 13 55.209 0.400 . 1 . . . . 34 GLU CA . 16228 1 375 . 1 1 34 34 GLU CB C 13 32.966 0.400 . 1 . . . . 34 GLU CB . 16228 1 376 . 1 1 34 34 GLU CG C 13 36.045 0.400 . 1 . . . . 34 GLU CG . 16228 1 377 . 1 1 34 34 GLU N N 15 114.419 0.400 . 1 . . . . 34 GLU N . 16228 1 378 . 1 1 35 35 GLY H H 1 8.431 0.020 . 1 . . . . 35 GLY H . 16228 1 379 . 1 1 35 35 GLY HA2 H 1 3.832 0.020 . 1 . . . . 35 GLY HA2 . 16228 1 380 . 1 1 35 35 GLY C C 13 173.823 0.400 . 1 . . . . 35 GLY C . 16228 1 381 . 1 1 35 35 GLY CA C 13 45.745 0.400 . 1 . . . . 35 GLY CA . 16228 1 382 . 1 1 35 35 GLY N N 15 108.772 0.400 . 1 . . . . 35 GLY N . 16228 1 383 . 1 1 36 36 ILE H H 1 6.102 0.020 . 1 . . . . 36 ILE H . 16228 1 384 . 1 1 36 36 ILE HA H 1 4.344 0.020 . 1 . . . . 36 ILE HA . 16228 1 385 . 1 1 36 36 ILE HB H 1 1.329 0.020 . 1 . . . . 36 ILE HB . 16228 1 386 . 1 1 36 36 ILE HD11 H 1 0.642 0.020 . 1 . . . . 36 ILE HD11 . 16228 1 387 . 1 1 36 36 ILE HD12 H 1 0.642 0.020 . 1 . . . . 36 ILE HD12 . 16228 1 388 . 1 1 36 36 ILE HD13 H 1 0.642 0.020 . 1 . . . . 36 ILE HD13 . 16228 1 389 . 1 1 36 36 ILE HG12 H 1 0.984 0.020 . 1 . . . . 36 ILE HG12 . 16228 1 390 . 1 1 36 36 ILE HG21 H 1 0.819 0.020 . 1 . . . . 36 ILE HG21 . 16228 1 391 . 1 1 36 36 ILE HG22 H 1 0.819 0.020 . 1 . . . . 36 ILE HG22 . 16228 1 392 . 1 1 36 36 ILE HG23 H 1 0.819 0.020 . 1 . . . . 36 ILE HG23 . 16228 1 393 . 1 1 36 36 ILE CA C 13 57.687 0.400 . 1 . . . . 36 ILE CA . 16228 1 394 . 1 1 36 36 ILE CB C 13 40.158 0.400 . 1 . . . . 36 ILE CB . 16228 1 395 . 1 1 36 36 ILE CD1 C 13 13.240 0.400 . 1 . . . . 36 ILE CD1 . 16228 1 396 . 1 1 36 36 ILE CG1 C 13 26.395 0.400 . 1 . . . . 36 ILE CG1 . 16228 1 397 . 1 1 36 36 ILE CG2 C 13 17.051 0.400 . 1 . . . . 36 ILE CG2 . 16228 1 398 . 1 1 36 36 ILE N N 15 120.295 0.400 . 1 . . . . 36 ILE N . 16228 1 399 . 1 1 37 37 PRO HA H 1 4.550 0.020 . 1 . . . . 37 PRO HA . 16228 1 400 . 1 1 37 37 PRO HB2 H 1 1.872 0.020 . 1 . . . . 37 PRO HB2 . 16228 1 401 . 1 1 37 37 PRO HD2 H 1 4.092 0.020 . 1 . . . . 37 PRO HD2 . 16228 1 402 . 1 1 37 37 PRO HG2 H 1 1.994 0.020 . 1 . . . . 37 PRO HG2 . 16228 1 403 . 1 1 37 37 PRO CA C 13 61.397 0.400 . 1 . . . . 37 PRO CA . 16228 1 404 . 1 1 37 37 PRO CB C 13 31.379 0.400 . 1 . . . . 37 PRO CB . 16228 1 405 . 1 1 37 37 PRO CD C 13 50.639 0.400 . 1 . . . . 37 PRO CD . 16228 1 406 . 1 1 37 37 PRO CG C 13 27.646 0.400 . 1 . . . . 37 PRO CG . 16228 1 407 . 1 1 38 38 PRO HA H 1 4.030 0.020 . 1 . . . . 38 PRO HA . 16228 1 408 . 1 1 38 38 PRO HB2 H 1 1.940 0.020 . 1 . . . . 38 PRO HB2 . 16228 1 409 . 1 1 38 38 PRO HD2 H 1 3.644 0.020 . 1 . . . . 38 PRO HD2 . 16228 1 410 . 1 1 38 38 PRO HG2 H 1 2.085 0.020 . 1 . . . . 38 PRO HG2 . 16228 1 411 . 1 1 38 38 PRO C C 13 178.171 0.400 . 1 . . . . 38 PRO C . 16228 1 412 . 1 1 38 38 PRO CA C 13 66.016 0.400 . 1 . . . . 38 PRO CA . 16228 1 413 . 1 1 38 38 PRO CB C 13 32.333 0.400 . 1 . . . . 38 PRO CB . 16228 1 414 . 1 1 38 38 PRO CD C 13 50.687 0.400 . 1 . . . . 38 PRO CD . 16228 1 415 . 1 1 38 38 PRO CG C 13 27.102 0.400 . 1 . . . . 38 PRO CG . 16228 1 416 . 1 1 39 39 ASP H H 1 8.456 0.020 . 1 . . . . 39 ASP H . 16228 1 417 . 1 1 39 39 ASP HA H 1 4.334 0.020 . 1 . . . . 39 ASP HA . 16228 1 418 . 1 1 39 39 ASP HB2 H 1 2.684 0.020 . 1 . . . . 39 ASP HB2 . 16228 1 419 . 1 1 39 39 ASP C C 13 176.946 0.400 . 1 . . . . 39 ASP C . 16228 1 420 . 1 1 39 39 ASP CA C 13 55.724 0.400 . 1 . . . . 39 ASP CA . 16228 1 421 . 1 1 39 39 ASP CB C 13 39.651 0.400 . 1 . . . . 39 ASP CB . 16228 1 422 . 1 1 39 39 ASP N N 15 113.557 0.400 . 1 . . . . 39 ASP N . 16228 1 423 . 1 1 40 40 GLN H H 1 7.755 0.020 . 1 . . . . 40 GLN H . 16228 1 424 . 1 1 40 40 GLN HA H 1 4.380 0.020 . 1 . . . . 40 GLN HA . 16228 1 425 . 1 1 40 40 GLN HB2 H 1 1.733 0.020 . 1 . . . . 40 GLN HB2 . 16228 1 426 . 1 1 40 40 GLN HE21 H 1 7.619 0.020 . 2 . . . . 40 GLN HE21 . 16228 1 427 . 1 1 40 40 GLN HE22 H 1 6.680 0.020 . 2 . . . . 40 GLN HE22 . 16228 1 428 . 1 1 40 40 GLN HG2 H 1 2.300 0.020 . 1 . . . . 40 GLN HG2 . 16228 1 429 . 1 1 40 40 GLN C C 13 175.297 0.400 . 1 . . . . 40 GLN C . 16228 1 430 . 1 1 40 40 GLN CA C 13 55.404 0.400 . 1 . . . . 40 GLN CA . 16228 1 431 . 1 1 40 40 GLN CB C 13 29.677 0.400 . 1 . . . . 40 GLN CB . 16228 1 432 . 1 1 40 40 GLN CG C 13 33.971 0.400 . 1 . . . . 40 GLN CG . 16228 1 433 . 1 1 40 40 GLN N N 15 116.811 0.400 . 1 . . . . 40 GLN N . 16228 1 434 . 1 1 40 40 GLN NE2 N 15 111.154 0.400 . 1 . . . . 40 GLN NE2 . 16228 1 435 . 1 1 41 41 GLN H H 1 7.415 0.020 . 1 . . . . 41 GLN H . 16228 1 436 . 1 1 41 41 GLN HA H 1 4.141 0.020 . 1 . . . . 41 GLN HA . 16228 1 437 . 1 1 41 41 GLN HB2 H 1 1.852 0.020 . 1 . . . . 41 GLN HB2 . 16228 1 438 . 1 1 41 41 GLN HE21 H 1 6.455 0.020 . 2 . . . . 41 GLN HE21 . 16228 1 439 . 1 1 41 41 GLN HE22 H 1 6.143 0.020 . 2 . . . . 41 GLN HE22 . 16228 1 440 . 1 1 41 41 GLN HG2 H 1 1.558 0.020 . 1 . . . . 41 GLN HG2 . 16228 1 441 . 1 1 41 41 GLN C C 13 176.050 0.400 . 1 . . . . 41 GLN C . 16228 1 442 . 1 1 41 41 GLN CA C 13 56.547 0.400 . 1 . . . . 41 GLN CA . 16228 1 443 . 1 1 41 41 GLN CB C 13 31.075 0.400 . 1 . . . . 41 GLN CB . 16228 1 444 . 1 1 41 41 GLN CG C 13 33.151 0.400 . 1 . . . . 41 GLN CG . 16228 1 445 . 1 1 41 41 GLN N N 15 118.028 0.400 . 1 . . . . 41 GLN N . 16228 1 446 . 1 1 41 41 GLN NE2 N 15 104.238 0.400 . 1 . . . . 41 GLN NE2 . 16228 1 447 . 1 1 42 42 ARG H H 1 8.443 0.020 . 1 . . . . 42 ARG H . 16228 1 448 . 1 1 42 42 ARG HA H 1 4.394 0.020 . 1 . . . . 42 ARG HA . 16228 1 449 . 1 1 42 42 ARG HB3 H 1 1.528 0.020 . 1 . . . . 42 ARG HB3 . 16228 1 450 . 1 1 42 42 ARG HD2 H 1 2.955 0.020 . 1 . . . . 42 ARG HD2 . 16228 1 451 . 1 1 42 42 ARG HG3 H 1 1.383 0.020 . 1 . . . . 42 ARG HG3 . 16228 1 452 . 1 1 42 42 ARG C C 13 173.712 0.400 . 1 . . . . 42 ARG C . 16228 1 453 . 1 1 42 42 ARG CA C 13 55.031 0.400 . 1 . . . . 42 ARG CA . 16228 1 454 . 1 1 42 42 ARG CB C 13 31.200 0.400 . 1 . . . . 42 ARG CB . 16228 1 455 . 1 1 42 42 ARG CD C 13 43.172 0.400 . 1 . . . . 42 ARG CD . 16228 1 456 . 1 1 42 42 ARG CG C 13 26.443 0.400 . 1 . . . . 42 ARG CG . 16228 1 457 . 1 1 42 42 ARG N N 15 123.086 0.400 . 1 . . . . 42 ARG N . 16228 1 458 . 1 1 43 43 LEU H H 1 8.744 0.020 . 1 . . . . 43 LEU H . 16228 1 459 . 1 1 43 43 LEU HA H 1 5.287 0.020 . 1 . . . . 43 LEU HA . 16228 1 460 . 1 1 43 43 LEU HB3 H 1 1.051 0.020 . 1 . . . . 43 LEU HB3 . 16228 1 461 . 1 1 43 43 LEU HD11 H 1 0.638 0.020 . 1 . . . . 43 LEU HD11 . 16228 1 462 . 1 1 43 43 LEU HD12 H 1 0.638 0.020 . 1 . . . . 43 LEU HD12 . 16228 1 463 . 1 1 43 43 LEU HD13 H 1 0.638 0.020 . 1 . . . . 43 LEU HD13 . 16228 1 464 . 1 1 43 43 LEU HG H 1 1.352 0.020 . 1 . . . . 43 LEU HG . 16228 1 465 . 1 1 43 43 LEU C C 13 175.214 0.400 . 1 . . . . 43 LEU C . 16228 1 466 . 1 1 43 43 LEU CA C 13 52.971 0.400 . 1 . . . . 43 LEU CA . 16228 1 467 . 1 1 43 43 LEU CB C 13 45.112 0.400 . 1 . . . . 43 LEU CB . 16228 1 468 . 1 1 43 43 LEU CD1 C 13 25.580 0.400 . 1 . . . . 43 LEU CD1 . 16228 1 469 . 1 1 43 43 LEU CG C 13 26.490 0.400 . 1 . . . . 43 LEU CG . 16228 1 470 . 1 1 43 43 LEU N N 15 124.371 0.400 . 1 . . . . 43 LEU N . 16228 1 471 . 1 1 44 44 ILE H H 1 9.074 0.020 . 1 . . . . 44 ILE H . 16228 1 472 . 1 1 44 44 ILE HA H 1 4.847 0.020 . 1 . . . . 44 ILE HA . 16228 1 473 . 1 1 44 44 ILE HB H 1 1.651 0.020 . 1 . . . . 44 ILE HB . 16228 1 474 . 1 1 44 44 ILE HD11 H 1 0.551 0.020 . 1 . . . . 44 ILE HD11 . 16228 1 475 . 1 1 44 44 ILE HD12 H 1 0.551 0.020 . 1 . . . . 44 ILE HD12 . 16228 1 476 . 1 1 44 44 ILE HD13 H 1 0.551 0.020 . 1 . . . . 44 ILE HD13 . 16228 1 477 . 1 1 44 44 ILE HG12 H 1 0.947 0.020 . 1 . . . . 44 ILE HG12 . 16228 1 478 . 1 1 44 44 ILE HG21 H 1 0.565 0.020 . 1 . . . . 44 ILE HG21 . 16228 1 479 . 1 1 44 44 ILE HG22 H 1 0.565 0.020 . 1 . . . . 44 ILE HG22 . 16228 1 480 . 1 1 44 44 ILE HG23 H 1 0.565 0.020 . 1 . . . . 44 ILE HG23 . 16228 1 481 . 1 1 44 44 ILE C C 13 175.620 0.400 . 1 . . . . 44 ILE C . 16228 1 482 . 1 1 44 44 ILE CA C 13 59.001 0.400 . 1 . . . . 44 ILE CA . 16228 1 483 . 1 1 44 44 ILE CB C 13 40.778 0.400 . 1 . . . . 44 ILE CB . 16228 1 484 . 1 1 44 44 ILE CD1 C 13 11.898 0.400 . 1 . . . . 44 ILE CD1 . 16228 1 485 . 1 1 44 44 ILE CG1 C 13 27.102 0.400 . 1 . . . . 44 ILE CG1 . 16228 1 486 . 1 1 44 44 ILE CG2 C 13 16.977 0.400 . 1 . . . . 44 ILE CG2 . 16228 1 487 . 1 1 44 44 ILE N N 15 122.344 0.400 . 1 . . . . 44 ILE N . 16228 1 488 . 1 1 45 45 PHE H H 1 8.793 0.020 . 1 . . . . 45 PHE H . 16228 1 489 . 1 1 45 45 PHE HA H 1 5.101 0.020 . 1 . . . . 45 PHE HA . 16228 1 490 . 1 1 45 45 PHE HB3 H 1 2.712 0.020 . 1 . . . . 45 PHE HB3 . 16228 1 491 . 1 1 45 45 PHE HE1 H 1 7.457 0.020 . 1 . . . . 45 PHE HE1 . 16228 1 492 . 1 1 45 45 PHE HE2 H 1 7.457 0.020 . 1 . . . . 45 PHE HE2 . 16228 1 493 . 1 1 45 45 PHE C C 13 174.536 0.400 . 1 . . . . 45 PHE C . 16228 1 494 . 1 1 45 45 PHE CA C 13 56.358 0.400 . 1 . . . . 45 PHE CA . 16228 1 495 . 1 1 45 45 PHE CB C 13 43.047 0.400 . 1 . . . . 45 PHE CB . 16228 1 496 . 1 1 45 45 PHE CE1 C 13 131.916 0.400 . 1 . . . . 45 PHE CE1 . 16228 1 497 . 1 1 45 45 PHE CE2 C 13 131.916 0.400 . 1 . . . . 45 PHE CE2 . 16228 1 498 . 1 1 45 45 PHE N N 15 124.928 0.400 . 1 . . . . 45 PHE N . 16228 1 499 . 1 1 46 46 ALA H H 1 8.923 0.020 . 1 . . . . 46 ALA H . 16228 1 500 . 1 1 46 46 ALA HA H 1 3.610 0.020 . 1 . . . . 46 ALA HA . 16228 1 501 . 1 1 46 46 ALA HB1 H 1 0.757 0.020 . 1 . . . . 46 ALA HB1 . 16228 1 502 . 1 1 46 46 ALA HB2 H 1 0.757 0.020 . 1 . . . . 46 ALA HB2 . 16228 1 503 . 1 1 46 46 ALA HB3 H 1 0.757 0.020 . 1 . . . . 46 ALA HB3 . 16228 1 504 . 1 1 46 46 ALA C C 13 177.218 0.400 . 1 . . . . 46 ALA C . 16228 1 505 . 1 1 46 46 ALA CA C 13 52.373 0.400 . 1 . . . . 46 ALA CA . 16228 1 506 . 1 1 46 46 ALA CB C 13 15.938 0.400 . 1 . . . . 46 ALA CB . 16228 1 507 . 1 1 46 46 ALA N N 15 132.790 0.400 . 1 . . . . 46 ALA N . 16228 1 508 . 1 1 47 47 GLY H H 1 8.007 0.020 . 1 . . . . 47 GLY H . 16228 1 509 . 1 1 47 47 GLY HA2 H 1 3.344 0.020 . 1 . . . . 47 GLY HA2 . 16228 1 510 . 1 1 47 47 GLY C C 13 173.603 0.400 . 1 . . . . 47 GLY C . 16228 1 511 . 1 1 47 47 GLY CA C 13 45.081 0.400 . 1 . . . . 47 GLY CA . 16228 1 512 . 1 1 47 47 GLY N N 15 102.267 0.400 . 1 . . . . 47 GLY N . 16228 1 513 . 1 1 48 48 LYS H H 1 7.921 0.020 . 1 . . . . 48 LYS H . 16228 1 514 . 1 1 48 48 LYS HA H 1 4.517 0.020 . 1 . . . . 48 LYS HA . 16228 1 515 . 1 1 48 48 LYS HB3 H 1 1.801 0.020 . 1 . . . . 48 LYS HB3 . 16228 1 516 . 1 1 48 48 LYS HD3 H 1 1.775 0.020 . 1 . . . . 48 LYS HD3 . 16228 1 517 . 1 1 48 48 LYS HE2 H 1 3.063 0.020 . 1 . . . . 48 LYS HE2 . 16228 1 518 . 1 1 48 48 LYS HG3 H 1 1.410 0.020 . 1 . . . . 48 LYS HG3 . 16228 1 519 . 1 1 48 48 LYS C C 13 174.526 0.400 . 1 . . . . 48 LYS C . 16228 1 520 . 1 1 48 48 LYS CA C 13 54.492 0.400 . 1 . . . . 48 LYS CA . 16228 1 521 . 1 1 48 48 LYS CB C 13 33.927 0.400 . 1 . . . . 48 LYS CB . 16228 1 522 . 1 1 48 48 LYS CD C 13 28.547 0.400 . 1 . . . . 48 LYS CD . 16228 1 523 . 1 1 48 48 LYS CE C 13 41.873 0.400 . 1 . . . . 48 LYS CE . 16228 1 524 . 1 1 48 48 LYS CG C 13 23.783 0.400 . 1 . . . . 48 LYS CG . 16228 1 525 . 1 1 48 48 LYS N N 15 122.029 0.400 . 1 . . . . 48 LYS N . 16228 1 526 . 1 1 49 49 GLN H H 1 8.570 0.020 . 1 . . . . 49 GLN H . 16228 1 527 . 1 1 49 49 GLN HA H 1 4.439 0.020 . 1 . . . . 49 GLN HA . 16228 1 528 . 1 1 49 49 GLN HB2 H 1 1.878 0.020 . 1 . . . . 49 GLN HB2 . 16228 1 529 . 1 1 49 49 GLN HE21 H 1 7.597 0.020 . 2 . . . . 49 GLN HE21 . 16228 1 530 . 1 1 49 49 GLN HE22 H 1 6.753 0.020 . 2 . . . . 49 GLN HE22 . 16228 1 531 . 1 1 49 49 GLN HG2 H 1 2.146 0.020 . 1 . . . . 49 GLN HG2 . 16228 1 532 . 1 1 49 49 GLN C C 13 175.438 0.400 . 1 . . . . 49 GLN C . 16228 1 533 . 1 1 49 49 GLN CA C 13 55.829 0.400 . 1 . . . . 49 GLN CA . 16228 1 534 . 1 1 49 49 GLN CB C 13 28.658 0.400 . 1 . . . . 49 GLN CB . 16228 1 535 . 1 1 49 49 GLN CG C 13 34.133 0.400 . 1 . . . . 49 GLN CG . 16228 1 536 . 1 1 49 49 GLN N N 15 123.088 0.400 . 1 . . . . 49 GLN N . 16228 1 537 . 1 1 49 49 GLN NE2 N 15 112.253 0.400 . 1 . . . . 49 GLN NE2 . 16228 1 538 . 1 1 50 50 LEU H H 1 8.498 0.020 . 1 . . . . 50 LEU H . 16228 1 539 . 1 1 50 50 LEU HA H 1 3.995 0.020 . 1 . . . . 50 LEU HA . 16228 1 540 . 1 1 50 50 LEU HB3 H 1 0.899 0.020 . 1 . . . . 50 LEU HB3 . 16228 1 541 . 1 1 50 50 LEU HD11 H 1 0.392 0.020 . 1 . . . . 50 LEU HD11 . 16228 1 542 . 1 1 50 50 LEU HD12 H 1 0.392 0.020 . 1 . . . . 50 LEU HD12 . 16228 1 543 . 1 1 50 50 LEU HD13 H 1 0.392 0.020 . 1 . . . . 50 LEU HD13 . 16228 1 544 . 1 1 50 50 LEU HG H 1 1.340 0.020 . 1 . . . . 50 LEU HG . 16228 1 545 . 1 1 50 50 LEU C C 13 176.529 0.400 . 1 . . . . 50 LEU C . 16228 1 546 . 1 1 50 50 LEU CA C 13 54.144 0.400 . 1 . . . . 50 LEU CA . 16228 1 547 . 1 1 50 50 LEU CB C 13 40.776 0.400 . 1 . . . . 50 LEU CB . 16228 1 548 . 1 1 50 50 LEU CD1 C 13 25.169 0.400 . 1 . . . . 50 LEU CD1 . 16228 1 549 . 1 1 50 50 LEU CG C 13 25.259 0.400 . 1 . . . . 50 LEU CG . 16228 1 550 . 1 1 50 50 LEU N N 15 125.663 0.400 . 1 . . . . 50 LEU N . 16228 1 551 . 1 1 51 51 GLU H H 1 8.313 0.020 . 1 . . . . 51 GLU H . 16228 1 552 . 1 1 51 51 GLU HA H 1 4.414 0.020 . 1 . . . . 51 GLU HA . 16228 1 553 . 1 1 51 51 GLU HB2 H 1 1.855 0.020 . 1 . . . . 51 GLU HB2 . 16228 1 554 . 1 1 51 51 GLU HG2 H 1 2.228 0.020 . 1 . . . . 51 GLU HG2 . 16228 1 555 . 1 1 51 51 GLU C C 13 175.302 0.400 . 1 . . . . 51 GLU C . 16228 1 556 . 1 1 51 51 GLU CA C 13 55.821 0.400 . 1 . . . . 51 GLU CA . 16228 1 557 . 1 1 51 51 GLU CB C 13 31.467 0.400 . 1 . . . . 51 GLU CB . 16228 1 558 . 1 1 51 51 GLU CG C 13 36.066 0.400 . 1 . . . . 51 GLU CG . 16228 1 559 . 1 1 51 51 GLU N N 15 123.119 0.400 . 1 . . . . 51 GLU N . 16228 1 560 . 1 1 52 52 ASP H H 1 8.088 0.020 . 1 . . . . 52 ASP H . 16228 1 561 . 1 1 52 52 ASP HA H 1 4.303 0.020 . 1 . . . . 52 ASP HA . 16228 1 562 . 1 1 52 52 ASP HB2 H 1 2.542 0.020 . 1 . . . . 52 ASP HB2 . 16228 1 563 . 1 1 52 52 ASP C C 13 177.302 0.400 . 1 . . . . 52 ASP C . 16228 1 564 . 1 1 52 52 ASP CA C 13 56.506 0.400 . 1 . . . . 52 ASP CA . 16228 1 565 . 1 1 52 52 ASP CB C 13 40.562 0.400 . 1 . . . . 52 ASP CB . 16228 1 566 . 1 1 52 52 ASP N N 15 120.358 0.400 . 1 . . . . 52 ASP N . 16228 1 567 . 1 1 53 53 GLY HA2 H 1 3.974 0.020 . 1 . . . . 53 GLY HA2 . 16228 1 568 . 1 1 53 53 GLY C C 13 174.654 0.400 . 1 . . . . 53 GLY C . 16228 1 569 . 1 1 53 53 GLY CA C 13 44.871 0.400 . 1 . . . . 53 GLY CA . 16228 1 570 . 1 1 54 54 ARG H H 1 7.411 0.020 . 1 . . . . 54 ARG H . 16228 1 571 . 1 1 54 54 ARG HA H 1 4.643 0.020 . 1 . . . . 54 ARG HA . 16228 1 572 . 1 1 54 54 ARG HB3 H 1 1.975 0.020 . 1 . . . . 54 ARG HB3 . 16228 1 573 . 1 1 54 54 ARG HD2 H 1 3.043 0.020 . 1 . . . . 54 ARG HD2 . 16228 1 574 . 1 1 54 54 ARG HG3 H 1 1.721 0.020 . 1 . . . . 54 ARG HG3 . 16228 1 575 . 1 1 54 54 ARG C C 13 175.154 0.400 . 1 . . . . 54 ARG C . 16228 1 576 . 1 1 54 54 ARG CA C 13 54.142 0.400 . 1 . . . . 54 ARG CA . 16228 1 577 . 1 1 54 54 ARG CB C 13 32.280 0.400 . 1 . . . . 54 ARG CB . 16228 1 578 . 1 1 54 54 ARG CD C 13 42.709 0.400 . 1 . . . . 54 ARG CD . 16228 1 579 . 1 1 54 54 ARG CG C 13 26.785 0.400 . 1 . . . . 54 ARG CG . 16228 1 580 . 1 1 54 54 ARG N N 15 119.297 0.400 . 1 . . . . 54 ARG N . 16228 1 581 . 1 1 55 55 THR H H 1 8.871 0.020 . 1 . . . . 55 THR H . 16228 1 582 . 1 1 55 55 THR HA H 1 5.189 0.020 . 1 . . . . 55 THR HA . 16228 1 583 . 1 1 55 55 THR HB H 1 4.435 0.020 . 1 . . . . 55 THR HB . 16228 1 584 . 1 1 55 55 THR HG21 H 1 1.030 0.020 . 1 . . . . 55 THR HG21 . 16228 1 585 . 1 1 55 55 THR HG22 H 1 1.030 0.020 . 1 . . . . 55 THR HG22 . 16228 1 586 . 1 1 55 55 THR HG23 H 1 1.030 0.020 . 1 . . . . 55 THR HG23 . 16228 1 587 . 1 1 55 55 THR C C 13 176.307 0.400 . 1 . . . . 55 THR C . 16228 1 588 . 1 1 55 55 THR CA C 13 59.645 0.400 . 1 . . . . 55 THR CA . 16228 1 589 . 1 1 55 55 THR CB C 13 72.570 0.400 . 1 . . . . 55 THR CB . 16228 1 590 . 1 1 55 55 THR CG2 C 13 21.603 0.400 . 1 . . . . 55 THR CG2 . 16228 1 591 . 1 1 55 55 THR N N 15 109.023 0.400 . 1 . . . . 55 THR N . 16228 1 592 . 1 1 56 56 LEU H H 1 8.024 0.020 . 1 . . . . 56 LEU H . 16228 1 593 . 1 1 56 56 LEU HA H 1 3.948 0.020 . 1 . . . . 56 LEU HA . 16228 1 594 . 1 1 56 56 LEU HB3 H 1 1.138 0.020 . 1 . . . . 56 LEU HB3 . 16228 1 595 . 1 1 56 56 LEU HD11 H 1 0.632 0.020 . 1 . . . . 56 LEU HD11 . 16228 1 596 . 1 1 56 56 LEU HD12 H 1 0.632 0.020 . 1 . . . . 56 LEU HD12 . 16228 1 597 . 1 1 56 56 LEU HD13 H 1 0.632 0.020 . 1 . . . . 56 LEU HD13 . 16228 1 598 . 1 1 56 56 LEU HG H 1 1.611 0.020 . 1 . . . . 56 LEU HG . 16228 1 599 . 1 1 56 56 LEU C C 13 180.232 0.400 . 1 . . . . 56 LEU C . 16228 1 600 . 1 1 56 56 LEU CA C 13 58.590 0.400 . 1 . . . . 56 LEU CA . 16228 1 601 . 1 1 56 56 LEU CB C 13 39.698 0.400 . 1 . . . . 56 LEU CB . 16228 1 602 . 1 1 56 56 LEU CD1 C 13 25.803 0.400 . 1 . . . . 56 LEU CD1 . 16228 1 603 . 1 1 56 56 LEU CG C 13 26.330 0.400 . 1 . . . . 56 LEU CG . 16228 1 604 . 1 1 56 56 LEU N N 15 117.893 0.400 . 1 . . . . 56 LEU N . 16228 1 605 . 1 1 57 57 ALA H H 1 8.214 0.020 . 1 . . . . 57 ALA H . 16228 1 606 . 1 1 57 57 ALA HA H 1 4.089 0.020 . 1 . . . . 57 ALA HA . 16228 1 607 . 1 1 57 57 ALA HB1 H 1 1.206 0.020 . 1 . . . . 57 ALA HB1 . 16228 1 608 . 1 1 57 57 ALA HB2 H 1 1.206 0.020 . 1 . . . . 57 ALA HB2 . 16228 1 609 . 1 1 57 57 ALA HB3 H 1 1.206 0.020 . 1 . . . . 57 ALA HB3 . 16228 1 610 . 1 1 57 57 ALA C C 13 181.418 0.400 . 1 . . . . 57 ALA C . 16228 1 611 . 1 1 57 57 ALA CA C 13 54.678 0.400 . 1 . . . . 57 ALA CA . 16228 1 612 . 1 1 57 57 ALA CB C 13 17.613 0.400 . 1 . . . . 57 ALA CB . 16228 1 613 . 1 1 57 57 ALA N N 15 121.097 0.400 . 1 . . . . 57 ALA N . 16228 1 614 . 1 1 58 58 ASP H H 1 7.825 0.020 . 1 . . . . 58 ASP H . 16228 1 615 . 1 1 58 58 ASP HA H 1 4.164 0.020 . 1 . . . . 58 ASP HA . 16228 1 616 . 1 1 58 58 ASP HB2 H 1 2.878 0.020 . 1 . . . . 58 ASP HB2 . 16228 1 617 . 1 1 58 58 ASP C C 13 177.296 0.400 . 1 . . . . 58 ASP C . 16228 1 618 . 1 1 58 58 ASP CA C 13 57.300 0.400 . 1 . . . . 58 ASP CA . 16228 1 619 . 1 1 58 58 ASP CB C 13 40.314 0.400 . 1 . . . . 58 ASP CB . 16228 1 620 . 1 1 58 58 ASP N N 15 120.269 0.400 . 1 . . . . 58 ASP N . 16228 1 621 . 1 1 59 59 TYR H H 1 7.218 0.020 . 1 . . . . 59 TYR H . 16228 1 622 . 1 1 59 59 TYR HA H 1 4.557 0.020 . 1 . . . . 59 TYR HA . 16228 1 623 . 1 1 59 59 TYR HB3 H 1 3.350 0.020 . 1 . . . . 59 TYR HB3 . 16228 1 624 . 1 1 59 59 TYR HE1 H 1 6.806 0.020 . 1 . . . . 59 TYR HE1 . 16228 1 625 . 1 1 59 59 TYR HE2 H 1 6.806 0.020 . 1 . . . . 59 TYR HE2 . 16228 1 626 . 1 1 59 59 TYR C C 13 174.528 0.400 . 1 . . . . 59 TYR C . 16228 1 627 . 1 1 59 59 TYR CA C 13 58.030 0.400 . 1 . . . . 59 TYR CA . 16228 1 628 . 1 1 59 59 TYR CB C 13 39.541 0.400 . 1 . . . . 59 TYR CB . 16228 1 629 . 1 1 59 59 TYR CE1 C 13 118.438 0.400 . 1 . . . . 59 TYR CE1 . 16228 1 630 . 1 1 59 59 TYR CE2 C 13 118.438 0.400 . 1 . . . . 59 TYR CE2 . 16228 1 631 . 1 1 59 59 TYR N N 15 115.769 0.400 . 1 . . . . 59 TYR N . 16228 1 632 . 1 1 60 60 ASN H H 1 8.102 0.020 . 1 . . . . 60 ASN H . 16228 1 633 . 1 1 60 60 ASN HA H 1 4.236 0.020 . 1 . . . . 60 ASN HA . 16228 1 634 . 1 1 60 60 ASN HB2 H 1 2.684 0.020 . 1 . . . . 60 ASN HB2 . 16228 1 635 . 1 1 60 60 ASN HD21 H 1 7.458 0.020 . 2 . . . . 60 ASN HD21 . 16228 1 636 . 1 1 60 60 ASN HD22 H 1 6.737 0.020 . 2 . . . . 60 ASN HD22 . 16228 1 637 . 1 1 60 60 ASN C C 13 174.155 0.400 . 1 . . . . 60 ASN C . 16228 1 638 . 1 1 60 60 ASN CA C 13 54.003 0.400 . 1 . . . . 60 ASN CA . 16228 1 639 . 1 1 60 60 ASN CB C 13 37.286 0.400 . 1 . . . . 60 ASN CB . 16228 1 640 . 1 1 60 60 ASN N N 15 116.276 0.400 . 1 . . . . 60 ASN N . 16228 1 641 . 1 1 60 60 ASN ND2 N 15 111.245 0.400 . 1 . . . . 60 ASN ND2 . 16228 1 642 . 1 1 61 61 ILE H H 1 7.215 0.020 . 1 . . . . 61 ILE H . 16228 1 643 . 1 1 61 61 ILE HA H 1 3.302 0.020 . 1 . . . . 61 ILE HA . 16228 1 644 . 1 1 61 61 ILE HB H 1 1.303 0.020 . 1 . . . . 61 ILE HB . 16228 1 645 . 1 1 61 61 ILE HD11 H 1 0.275 0.020 . 1 . . . . 61 ILE HD11 . 16228 1 646 . 1 1 61 61 ILE HD12 H 1 0.275 0.020 . 1 . . . . 61 ILE HD12 . 16228 1 647 . 1 1 61 61 ILE HD13 H 1 0.275 0.020 . 1 . . . . 61 ILE HD13 . 16228 1 648 . 1 1 61 61 ILE HG12 H 1 -0.417 0.020 . 1 . . . . 61 ILE HG12 . 16228 1 649 . 1 1 61 61 ILE HG21 H 1 0.361 0.020 . 1 . . . . 61 ILE HG21 . 16228 1 650 . 1 1 61 61 ILE HG22 H 1 0.361 0.020 . 1 . . . . 61 ILE HG22 . 16228 1 651 . 1 1 61 61 ILE HG23 H 1 0.361 0.020 . 1 . . . . 61 ILE HG23 . 16228 1 652 . 1 1 61 61 ILE C C 13 174.509 0.400 . 1 . . . . 61 ILE C . 16228 1 653 . 1 1 61 61 ILE CA C 13 62.339 0.400 . 1 . . . . 61 ILE CA . 16228 1 654 . 1 1 61 61 ILE CB C 13 36.373 0.400 . 1 . . . . 61 ILE CB . 16228 1 655 . 1 1 61 61 ILE CD1 C 13 13.476 0.400 . 1 . . . . 61 ILE CD1 . 16228 1 656 . 1 1 61 61 ILE CG1 C 13 27.589 0.400 . 1 . . . . 61 ILE CG1 . 16228 1 657 . 1 1 61 61 ILE CG2 C 13 16.572 0.400 . 1 . . . . 61 ILE CG2 . 16228 1 658 . 1 1 61 61 ILE N N 15 118.921 0.400 . 1 . . . . 61 ILE N . 16228 1 659 . 1 1 62 62 GLN H H 1 7.543 0.020 . 1 . . . . 62 GLN H . 16228 1 660 . 1 1 62 62 GLN HA H 1 4.392 0.020 . 1 . . . . 62 GLN HA . 16228 1 661 . 1 1 62 62 GLN HB2 H 1 1.788 0.020 . 1 . . . . 62 GLN HB2 . 16228 1 662 . 1 1 62 62 GLN HE21 H 1 7.222 0.020 . 2 . . . . 62 GLN HE21 . 16228 1 663 . 1 1 62 62 GLN HE22 H 1 6.753 0.020 . 2 . . . . 62 GLN HE22 . 16228 1 664 . 1 1 62 62 GLN HG2 H 1 2.194 0.020 . 1 . . . . 62 GLN HG2 . 16228 1 665 . 1 1 62 62 GLN C C 13 175.623 0.400 . 1 . . . . 62 GLN C . 16228 1 666 . 1 1 62 62 GLN CA C 13 53.548 0.400 . 1 . . . . 62 GLN CA . 16228 1 667 . 1 1 62 62 GLN CB C 13 31.174 0.400 . 1 . . . . 62 GLN CB . 16228 1 668 . 1 1 62 62 GLN CG C 13 33.023 0.400 . 1 . . . . 62 GLN CG . 16228 1 669 . 1 1 62 62 GLN N N 15 124.970 0.400 . 1 . . . . 62 GLN N . 16228 1 670 . 1 1 62 62 GLN NE2 N 15 112.329 0.400 . 1 . . . . 62 GLN NE2 . 16228 1 671 . 1 1 63 63 LYS H H 1 8.392 0.020 . 1 . . . . 63 LYS H . 16228 1 672 . 1 1 63 63 LYS HA H 1 3.898 0.020 . 1 . . . . 63 LYS HA . 16228 1 673 . 1 1 63 63 LYS HB3 H 1 1.780 0.020 . 1 . . . . 63 LYS HB3 . 16228 1 674 . 1 1 63 63 LYS HD3 H 1 1.614 0.020 . 1 . . . . 63 LYS HD3 . 16228 1 675 . 1 1 63 63 LYS HE2 H 1 2.938 0.020 . 1 . . . . 63 LYS HE2 . 16228 1 676 . 1 1 63 63 LYS HG3 H 1 1.380 0.020 . 1 . . . . 63 LYS HG3 . 16228 1 677 . 1 1 63 63 LYS C C 13 175.601 0.400 . 1 . . . . 63 LYS C . 16228 1 678 . 1 1 63 63 LYS CA C 13 57.752 0.400 . 1 . . . . 63 LYS CA . 16228 1 679 . 1 1 63 63 LYS CB C 13 32.034 0.400 . 1 . . . . 63 LYS CB . 16228 1 680 . 1 1 63 63 LYS CD C 13 29.180 0.400 . 1 . . . . 63 LYS CD . 16228 1 681 . 1 1 63 63 LYS CE C 13 41.655 0.400 . 1 . . . . 63 LYS CE . 16228 1 682 . 1 1 63 63 LYS CG C 13 23.556 0.400 . 1 . . . . 63 LYS CG . 16228 1 683 . 1 1 63 63 LYS N N 15 120.463 0.400 . 1 . . . . 63 LYS N . 16228 1 684 . 1 1 64 64 GLU H H 1 9.246 0.020 . 1 . . . . 64 GLU H . 16228 1 685 . 1 1 64 64 GLU HA H 1 3.241 0.020 . 1 . . . . 64 GLU HA . 16228 1 686 . 1 1 64 64 GLU HB2 H 1 2.309 0.020 . 1 . . . . 64 GLU HB2 . 16228 1 687 . 1 1 64 64 GLU HG2 H 1 2.141 0.020 . 1 . . . . 64 GLU HG2 . 16228 1 688 . 1 1 64 64 GLU C C 13 175.116 0.400 . 1 . . . . 64 GLU C . 16228 1 689 . 1 1 64 64 GLU CA C 13 58.297 0.400 . 1 . . . . 64 GLU CA . 16228 1 690 . 1 1 64 64 GLU CB C 13 25.604 0.400 . 1 . . . . 64 GLU CB . 16228 1 691 . 1 1 64 64 GLU CG C 13 36.965 0.400 . 1 . . . . 64 GLU CG . 16228 1 692 . 1 1 64 64 GLU N N 15 114.613 0.400 . 1 . . . . 64 GLU N . 16228 1 693 . 1 1 65 65 SER H H 1 7.606 0.020 . 1 . . . . 65 SER H . 16228 1 694 . 1 1 65 65 SER HA H 1 4.550 0.020 . 1 . . . . 65 SER HA . 16228 1 695 . 1 1 65 65 SER HB3 H 1 3.803 0.020 . 1 . . . . 65 SER HB3 . 16228 1 696 . 1 1 65 65 SER C C 13 171.898 0.400 . 1 . . . . 65 SER C . 16228 1 697 . 1 1 65 65 SER CA C 13 60.794 0.400 . 1 . . . . 65 SER CA . 16228 1 698 . 1 1 65 65 SER CB C 13 64.572 0.400 . 1 . . . . 65 SER CB . 16228 1 699 . 1 1 65 65 SER N N 15 114.875 0.400 . 1 . . . . 65 SER N . 16228 1 700 . 1 1 66 66 THR H H 1 8.626 0.020 . 1 . . . . 66 THR H . 16228 1 701 . 1 1 66 66 THR HA H 1 5.200 0.020 . 1 . . . . 66 THR HA . 16228 1 702 . 1 1 66 66 THR HB H 1 3.979 0.020 . 1 . . . . 66 THR HB . 16228 1 703 . 1 1 66 66 THR HG21 H 1 0.831 0.020 . 1 . . . . 66 THR HG21 . 16228 1 704 . 1 1 66 66 THR HG22 H 1 0.831 0.020 . 1 . . . . 66 THR HG22 . 16228 1 705 . 1 1 66 66 THR HG23 H 1 0.831 0.020 . 1 . . . . 66 THR HG23 . 16228 1 706 . 1 1 66 66 THR C C 13 173.563 0.400 . 1 . . . . 66 THR C . 16228 1 707 . 1 1 66 66 THR CA C 13 62.373 0.400 . 1 . . . . 66 THR CA . 16228 1 708 . 1 1 66 66 THR CB C 13 70.157 0.400 . 1 . . . . 66 THR CB . 16228 1 709 . 1 1 66 66 THR CG2 C 13 20.902 0.400 . 1 . . . . 66 THR CG2 . 16228 1 710 . 1 1 66 66 THR N N 15 117.388 0.400 . 1 . . . . 66 THR N . 16228 1 711 . 1 1 67 67 LEU H H 1 9.341 0.020 . 1 . . . . 67 LEU H . 16228 1 712 . 1 1 67 67 LEU HA H 1 4.998 0.020 . 1 . . . . 67 LEU HA . 16228 1 713 . 1 1 67 67 LEU HB3 H 1 1.506 0.020 . 1 . . . . 67 LEU HB3 . 16228 1 714 . 1 1 67 67 LEU HD11 H 1 0.571 0.020 . 1 . . . . 67 LEU HD11 . 16228 1 715 . 1 1 67 67 LEU HD12 H 1 0.571 0.020 . 1 . . . . 67 LEU HD12 . 16228 1 716 . 1 1 67 67 LEU HD13 H 1 0.571 0.020 . 1 . . . . 67 LEU HD13 . 16228 1 717 . 1 1 67 67 LEU HG H 1 1.641 0.020 . 1 . . . . 67 LEU HG . 16228 1 718 . 1 1 67 67 LEU C C 13 175.083 0.400 . 1 . . . . 67 LEU C . 16228 1 719 . 1 1 67 67 LEU CA C 13 53.642 0.400 . 1 . . . . 67 LEU CA . 16228 1 720 . 1 1 67 67 LEU CB C 13 43.854 0.400 . 1 . . . . 67 LEU CB . 16228 1 721 . 1 1 67 67 LEU CD1 C 13 24.127 0.400 . 1 . . . . 67 LEU CD1 . 16228 1 722 . 1 1 67 67 LEU CG C 13 28.674 0.400 . 1 . . . . 67 LEU CG . 16228 1 723 . 1 1 67 67 LEU N N 15 127.713 0.400 . 1 . . . . 67 LEU N . 16228 1 724 . 1 1 68 68 HIS H H 1 9.162 0.020 . 1 . . . . 68 HIS H . 16228 1 725 . 1 1 68 68 HIS HA H 1 5.036 0.020 . 1 . . . . 68 HIS HA . 16228 1 726 . 1 1 68 68 HIS HB2 H 1 2.949 0.020 . 1 . . . . 68 HIS HB2 . 16228 1 727 . 1 1 68 68 HIS HD2 H 1 6.842 0.020 . 1 . . . . 68 HIS HD2 . 16228 1 728 . 1 1 68 68 HIS HE1 H 1 7.595 0.020 . 1 . . . . 68 HIS HE1 . 16228 1 729 . 1 1 68 68 HIS C C 13 173.876 0.400 . 1 . . . . 68 HIS C . 16228 1 730 . 1 1 68 68 HIS CA C 13 56.169 0.400 . 1 . . . . 68 HIS CA . 16228 1 731 . 1 1 68 68 HIS CB C 13 32.230 0.400 . 1 . . . . 68 HIS CB . 16228 1 732 . 1 1 68 68 HIS CD2 C 13 119.263 0.400 . 1 . . . . 68 HIS CD2 . 16228 1 733 . 1 1 68 68 HIS CE1 C 13 138.265 0.400 . 1 . . . . 68 HIS CE1 . 16228 1 734 . 1 1 68 68 HIS N N 15 119.704 0.400 . 1 . . . . 68 HIS N . 16228 1 735 . 1 1 69 69 LEU H H 1 8.212 0.020 . 1 . . . . 69 LEU H . 16228 1 736 . 1 1 69 69 LEU HA H 1 5.088 0.020 . 1 . . . . 69 LEU HA . 16228 1 737 . 1 1 69 69 LEU HB3 H 1 1.522 0.020 . 1 . . . . 69 LEU HB3 . 16228 1 738 . 1 1 69 69 LEU HD11 H 1 0.740 0.020 . 1 . . . . 69 LEU HD11 . 16228 1 739 . 1 1 69 69 LEU HD12 H 1 0.740 0.020 . 1 . . . . 69 LEU HD12 . 16228 1 740 . 1 1 69 69 LEU HD13 H 1 0.740 0.020 . 1 . . . . 69 LEU HD13 . 16228 1 741 . 1 1 69 69 LEU HG H 1 1.222 0.020 . 1 . . . . 69 LEU HG . 16228 1 742 . 1 1 69 69 LEU C C 13 175.305 0.400 . 1 . . . . 69 LEU C . 16228 1 743 . 1 1 69 69 LEU CA C 13 53.672 0.400 . 1 . . . . 69 LEU CA . 16228 1 744 . 1 1 69 69 LEU CB C 13 43.678 0.400 . 1 . . . . 69 LEU CB . 16228 1 745 . 1 1 69 69 LEU CD1 C 13 23.241 0.400 . 1 . . . . 69 LEU CD1 . 16228 1 746 . 1 1 69 69 LEU CG C 13 27.046 0.400 . 1 . . . . 69 LEU CG . 16228 1 747 . 1 1 69 69 LEU N N 15 123.782 0.400 . 1 . . . . 69 LEU N . 16228 1 748 . 1 1 70 70 VAL H H 1 9.102 0.020 . 1 . . . . 70 VAL H . 16228 1 749 . 1 1 70 70 VAL HA H 1 4.304 0.020 . 1 . . . . 70 VAL HA . 16228 1 750 . 1 1 70 70 VAL HB H 1 1.934 0.020 . 1 . . . . 70 VAL HB . 16228 1 751 . 1 1 70 70 VAL HG21 H 1 0.720 0.020 . 1 . . . . 70 VAL HG21 . 16228 1 752 . 1 1 70 70 VAL HG22 H 1 0.720 0.020 . 1 . . . . 70 VAL HG22 . 16228 1 753 . 1 1 70 70 VAL HG23 H 1 0.720 0.020 . 1 . . . . 70 VAL HG23 . 16228 1 754 . 1 1 70 70 VAL C C 13 173.992 0.400 . 1 . . . . 70 VAL C . 16228 1 755 . 1 1 70 70 VAL CA C 13 60.407 0.400 . 1 . . . . 70 VAL CA . 16228 1 756 . 1 1 70 70 VAL CB C 13 34.303 0.400 . 1 . . . . 70 VAL CB . 16228 1 757 . 1 1 70 70 VAL CG2 C 13 19.894 0.400 . 1 . . . . 70 VAL CG2 . 16228 1 758 . 1 1 70 70 VAL N N 15 126.426 0.400 . 1 . . . . 70 VAL N . 16228 1 759 . 1 1 71 71 LEU H H 1 8.016 0.020 . 1 . . . . 71 LEU H . 16228 1 760 . 1 1 71 71 LEU HA H 1 4.928 0.020 . 1 . . . . 71 LEU HA . 16228 1 761 . 1 1 71 71 LEU HB3 H 1 1.441 0.020 . 1 . . . . 71 LEU HB3 . 16228 1 762 . 1 1 71 71 LEU HD11 H 1 0.849 0.020 . 1 . . . . 71 LEU HD11 . 16228 1 763 . 1 1 71 71 LEU HD12 H 1 0.849 0.020 . 1 . . . . 71 LEU HD12 . 16228 1 764 . 1 1 71 71 LEU HD13 H 1 0.849 0.020 . 1 . . . . 71 LEU HD13 . 16228 1 765 . 1 1 71 71 LEU HG H 1 1.546 0.020 . 1 . . . . 71 LEU HG . 16228 1 766 . 1 1 71 71 LEU C C 13 177.736 0.400 . 1 . . . . 71 LEU C . 16228 1 767 . 1 1 71 71 LEU CA C 13 53.897 0.400 . 1 . . . . 71 LEU CA . 16228 1 768 . 1 1 71 71 LEU CB C 13 42.256 0.400 . 1 . . . . 71 LEU CB . 16228 1 769 . 1 1 71 71 LEU CD1 C 13 24.210 0.400 . 1 . . . . 71 LEU CD1 . 16228 1 770 . 1 1 71 71 LEU CG C 13 27.000 0.400 . 1 . . . . 71 LEU CG . 16228 1 771 . 1 1 71 71 LEU N N 15 122.932 0.400 . 1 . . . . 71 LEU N . 16228 1 772 . 1 1 72 72 ARG H H 1 8.518 0.020 . 1 . . . . 72 ARG H . 16228 1 773 . 1 1 72 72 ARG HA H 1 4.179 0.020 . 1 . . . . 72 ARG HA . 16228 1 774 . 1 1 72 72 ARG HB3 H 1 1.649 0.020 . 1 . . . . 72 ARG HB3 . 16228 1 775 . 1 1 72 72 ARG HD2 H 1 3.050 0.020 . 1 . . . . 72 ARG HD2 . 16228 1 776 . 1 1 72 72 ARG HG3 H 1 1.441 0.020 . 1 . . . . 72 ARG HG3 . 16228 1 777 . 1 1 72 72 ARG C C 13 175.206 0.400 . 1 . . . . 72 ARG C . 16228 1 778 . 1 1 72 72 ARG CA C 13 55.612 0.400 . 1 . . . . 72 ARG CA . 16228 1 779 . 1 1 72 72 ARG CB C 13 30.809 0.400 . 1 . . . . 72 ARG CB . 16228 1 780 . 1 1 72 72 ARG CD C 13 43.083 0.400 . 1 . . . . 72 ARG CD . 16228 1 781 . 1 1 72 72 ARG CG C 13 26.637 0.400 . 1 . . . . 72 ARG CG . 16228 1 782 . 1 1 72 72 ARG N N 15 123.658 0.400 . 1 . . . . 72 ARG N . 16228 1 783 . 1 1 73 73 LEU H H 1 8.265 0.020 . 1 . . . . 73 LEU H . 16228 1 784 . 1 1 73 73 LEU HA H 1 4.304 0.020 . 1 . . . . 73 LEU HA . 16228 1 785 . 1 1 73 73 LEU HB3 H 1 1.461 0.020 . 1 . . . . 73 LEU HB3 . 16228 1 786 . 1 1 73 73 LEU HD11 H 1 0.808 0.020 . 1 . . . . 73 LEU HD11 . 16228 1 787 . 1 1 73 73 LEU HD12 H 1 0.808 0.020 . 1 . . . . 73 LEU HD12 . 16228 1 788 . 1 1 73 73 LEU HD13 H 1 0.808 0.020 . 1 . . . . 73 LEU HD13 . 16228 1 789 . 1 1 73 73 LEU HG H 1 1.502 0.020 . 1 . . . . 73 LEU HG . 16228 1 790 . 1 1 73 73 LEU C C 13 177.311 0.400 . 1 . . . . 73 LEU C . 16228 1 791 . 1 1 73 73 LEU CA C 13 54.723 0.400 . 1 . . . . 73 LEU CA . 16228 1 792 . 1 1 73 73 LEU CB C 13 41.929 0.400 . 1 . . . . 73 LEU CB . 16228 1 793 . 1 1 73 73 LEU CD1 C 13 24.211 0.400 . 1 . . . . 73 LEU CD1 . 16228 1 794 . 1 1 73 73 LEU CG C 13 26.671 0.400 . 1 . . . . 73 LEU CG . 16228 1 795 . 1 1 73 73 LEU N N 15 124.455 0.400 . 1 . . . . 73 LEU N . 16228 1 796 . 1 1 74 74 ARG H H 1 8.359 0.020 . 1 . . . . 74 ARG H . 16228 1 797 . 1 1 74 74 ARG HA H 1 4.202 0.020 . 1 . . . . 74 ARG HA . 16228 1 798 . 1 1 74 74 ARG HB3 H 1 1.761 0.020 . 1 . . . . 74 ARG HB3 . 16228 1 799 . 1 1 74 74 ARG HD2 H 1 3.108 0.020 . 1 . . . . 74 ARG HD2 . 16228 1 800 . 1 1 74 74 ARG HG3 H 1 1.556 0.020 . 1 . . . . 74 ARG HG3 . 16228 1 801 . 1 1 74 74 ARG C C 13 176.781 0.400 . 1 . . . . 74 ARG C . 16228 1 802 . 1 1 74 74 ARG CA C 13 56.479 0.400 . 1 . . . . 74 ARG CA . 16228 1 803 . 1 1 74 74 ARG CB C 13 30.150 0.400 . 1 . . . . 74 ARG CB . 16228 1 804 . 1 1 74 74 ARG CD C 13 42.930 0.400 . 1 . . . . 74 ARG CD . 16228 1 805 . 1 1 74 74 ARG CG C 13 26.534 0.400 . 1 . . . . 74 ARG CG . 16228 1 806 . 1 1 74 74 ARG N N 15 121.940 0.400 . 1 . . . . 74 ARG N . 16228 1 807 . 1 1 75 75 GLY H H 1 8.394 0.020 . 1 . . . . 75 GLY H . 16228 1 808 . 1 1 75 75 GLY HA2 H 1 3.857 0.020 . 1 . . . . 75 GLY HA2 . 16228 1 809 . 1 1 75 75 GLY C C 13 173.507 0.400 . 1 . . . . 75 GLY C . 16228 1 810 . 1 1 75 75 GLY CA C 13 44.929 0.400 . 1 . . . . 75 GLY CA . 16228 1 811 . 1 1 75 75 GLY N N 15 110.942 0.400 . 1 . . . . 75 GLY N . 16228 1 812 . 1 1 76 76 GLY H H 1 7.861 0.020 . 1 . . . . 76 GLY H . 16228 1 813 . 1 1 76 76 GLY HA2 H 1 3.728 0.020 . 1 . . . . 76 GLY HA2 . 16228 1 814 . 1 1 76 76 GLY CA C 13 45.728 0.400 . 1 . . . . 76 GLY CA . 16228 1 815 . 1 1 76 76 GLY N N 15 115.052 0.400 . 1 . . . . 76 GLY N . 16228 1 stop_ save_