data_5101 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5101 _Entry.Title ; Structure and Properties of a Dimeric N-terminal Fragment of Human Ubiquitin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-08-06 _Entry.Accession_date 2001-08-06 _Entry.Last_release_date 2002-01-25 _Entry.Original_release_date 2002-01-25 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 David Bolton . . . 5101 2 Philip Evans . A. . 5101 3 Katherine Stott . . . 5101 4 Richard Broadhurst . W. . 5101 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5101 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 390 5101 '13C chemical shifts' 174 5101 '15N chemical shifts' 49 5101 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2002-01-25 2001-08-06 original author . 5101 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5101 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21592562 _Citation.DOI . _Citation.PubMed_ID 117733996 _Citation.Full_citation . _Citation.Title 'Structure and Properties of a Dimeric N-terminal Fragment of Human Ubiquitin' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 314 _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 773 _Citation.Page_last 787 _Citation.Year 2001 _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 David Bolton . . . 5101 1 2 Philip Evans . A. . 5101 1 3 Katherine Stott . . . 5101 1 4 Richard Broadhurst . W. . 5101 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID ubiquitin 5101 1 dimer 5101 1 'protein dissection' 5101 1 'structural specificity' 5101 1 'NMR spectroscopy' 5101 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_UQ(1-51) _Assembly.Sf_category assembly _Assembly.Sf_framecode system_UQ(1-51) _Assembly.Entry_ID 5101 _Assembly.ID 1 _Assembly.Name 'ubiquitin fragment' _Assembly.BMRB_code . _Assembly.Number_of_components . _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 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID dimer 5101 1 stop_ 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 'uq1_51 subunit A' 1 $uq1_51 . . . native . . 1 . . 5101 1 2 'uq1_51 subunit B' 1 $uq1_51 . . . native . . 1 . . 5101 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'ubiquitin fragment' system 5101 1 UQ(1-51) abbreviation 5101 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_uq1_51 _Entity.Sf_category entity _Entity.Sf_framecode uq1_51 _Entity.Entry_ID 5101 _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 ; GSMQIFVKTLTGKTITLEVE PSDTIENVKAKIQDKEGIPP DQQRLIFAGKQLE ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 53 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _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 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 11505 . entity . . . . . 96.23 76 98.04 98.04 6.84e-26 . . . . 5101 1 2 no BMRB 11547 . ubiquitin . . . . . 96.23 76 98.04 98.04 6.84e-26 . . . . 5101 1 3 no BMRB 15047 . denatured_ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 4 no BMRB 15410 . Ubi . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 5 no BMRB 15689 . UBB . . . . . 100.00 103 100.00 100.00 7.26e-28 . . . . 5101 1 6 no BMRB 15866 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1 7 no BMRB 15907 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 8 no BMRB 16228 . ubiquitin . . . . . 96.23 76 98.04 98.04 1.31e-25 . . . . 5101 1 9 no BMRB 16582 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 10 no BMRB 16626 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 11 no BMRB 16763 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 12 no BMRB 16880 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 13 no BMRB 16885 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 14 no BMRB 16895 . UBB+1 . . . . . 100.00 103 100.00 100.00 7.26e-28 . . . . 5101 1 15 no BMRB 17059 . ubiquitin . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1 16 no BMRB 17181 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 17 no BMRB 17239 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 18 no BMRB 17333 . UB . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 19 no BMRB 17439 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 20 no BMRB 17769 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 21 no BMRB 17919 . entity . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 22 no BMRB 18582 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 23 no BMRB 18583 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 24 no BMRB 18584 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 25 no BMRB 18610 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 26 no BMRB 18611 . Ubiquitin_A_state . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 27 no BMRB 18737 . UBIQUITIN . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 28 no BMRB 19394 . ubiquitin . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1 29 no BMRB 19399 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 30 no BMRB 19406 . entity . . . . . 96.23 152 100.00 100.00 1.06e-25 . . . . 5101 1 31 no BMRB 19412 . entity . . . . . 96.23 152 100.00 100.00 1.06e-25 . . . . 5101 1 32 no BMRB 19447 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 33 no BMRB 25070 . Ubiquitin . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1 34 no BMRB 25230 . Ubiquitin . . . . . 98.11 78 98.08 98.08 1.13e-26 . . . . 5101 1 35 no BMRB 4245 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 36 no BMRB 4375 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 37 no BMRB 5387 . ubq . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 38 no BMRB 6457 . Ub . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 39 no BMRB 6466 . Ub . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 40 no BMRB 6470 . Ub . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 41 no BMRB 6488 . Ub . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 42 no BMRB 68 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 43 no BMRB 7111 . human_ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 44 no PDB 1AAR . "Structure Of A Diubiquitin Conjugate And A Model For Interaction With Ubiquitin Conjugating Enzyme (E2)" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 45 no PDB 1CMX . "Structural Basis For The Specificity Of Ubiquitin C- Terminal Hydrolases" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1 46 no PDB 1D3Z . "Ubiquitin Nmr Structure" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 47 no PDB 1F9J . "Structure Of A New Crystal Form Of Tetraubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 48 no PDB 1FXT . "Structure Of A Conjugating Enzyme-Ubiquitin Thiolester Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 49 no PDB 1G6J . "Structure Of Recombinant Human Ubiquitin In Aot Reverse Micelles" . . . . . 94.34 76 100.00 100.00 1.52e-25 . . . . 5101 1 50 no PDB 1GJZ . "Solution Structure Of A Dimeric N-Terminal Fragment Of Human Ubiquitin" . . . . . 100.00 53 100.00 100.00 4.76e-28 . . . . 5101 1 51 no PDB 1NBF . "Crystal Structure Of A Ubp-Family Deubiquitinating Enzyme In Isolation And In Complex With Ubiquitin Aldehyde" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1 52 no PDB 1OGW . "Synthetic Ubiquitin With Fluoro-Leu At 50 And 67" . . . . . 96.23 76 98.04 98.04 1.01e-25 . . . . 5101 1 53 no PDB 1P3Q . "Mechanism Of Ubiquitin Recognition By The Cue Domain Of Vps9" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 54 no PDB 1Q5W . "Ubiquitin Recognition By Npl4 Zinc-Fingers" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 55 no PDB 1S1Q . "Tsg101(Uev) Domain In Complex With Ubiquitin" . . . . . 94.34 76 100.00 100.00 1.52e-25 . . . . 5101 1 56 no PDB 1TBE . "Structure Of Tetraubiquitin Shows How Multiubiquitin Chains Can Be Formed" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 57 no PDB 1UBI . "Synthetic Structural And Biological Studies Of The Ubiquitin System. Part 1" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 58 no PDB 1UBQ . "Structure Of Ubiquitin Refined At 1.8 Angstroms Resolution" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 59 no PDB 1UZX . "A Complex Of The Vps23 Uev With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 60 no PDB 1V80 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 61 no PDB 1V81 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 62 no PDB 1VX7 . "Cryo-em Structure Of The Plasmodium Falciparum 80s Ribosome Bound To The Anti-protozoan Drug Emetine, Large Subunit (protein On" . . . . . 96.23 128 98.04 100.00 5.03e-26 . . . . 5101 1 63 no PDB 1WR6 . "Crystal Structure Of Gga3 Gat Domain In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 64 no PDB 1WRD . "Crystal Structure Of Tom1 Gat Domain In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 65 no PDB 1XD3 . "Crystal Structure Of Uchl3-Ubvme Complex" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 66 no PDB 1XQQ . "Simultaneous Determination Of Protein Structure And Dynamics" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 67 no PDB 1YD8 . "Complex Of Human Gga3 Gat Domain And Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 68 no PDB 1YIW . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin" . . . . . 96.23 76 98.04 100.00 5.57e-26 . . . . 5101 1 69 no PDB 1YX5 . "Solution Structure Of S5a Uim-1UBIQUITIN COMPLEX" . . . . . 96.23 98 100.00 100.00 4.75e-27 . . . . 5101 1 70 no PDB 1YX6 . "Solution Structure Of S5a Uim-2UBIQUITIN COMPLEX" . . . . . 96.23 98 100.00 100.00 4.75e-27 . . . . 5101 1 71 no PDB 1ZGU . "Solution Structure Of The Human Mms2-Ubiquitin Complex" . . . . . 96.23 76 98.04 100.00 2.70e-26 . . . . 5101 1 72 no PDB 2AYO . "Structure Of Usp14 Bound To Ubquitin Aldehyde" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1 73 no PDB 2BGF . "Nmr Structure Of Lys48-Linked Di-Ubiquitin Using Chemical Shift Perturbation Data Together With Rdcs And 15n- Relaxation Data" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 74 no PDB 2C7M . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 75 no PDB 2C7N . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 76 no PDB 2D3G . "Double Sided Ubiquitin Binding Of Hrs-Uim" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 77 no PDB 2DEN . "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 78 no PDB 2DX5 . "The Complex Structure Between The Mouse Eap45-Glue Domain And Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 79 no PDB 2FCQ . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin With A Cubic Space Group" . . . . . 96.23 76 98.04 100.00 5.57e-26 . . . . 5101 1 80 no PDB 2FID . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 81 no PDB 2FIF . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 82 no PDB 2FUH . "Solution Structure Of The Ubch5cUB NON-Covalent Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 83 no PDB 2G45 . "Co-Crystal Structure Of Znf Ubp Domain From The Deubiquitinating Enzyme Isopeptidase T (Isot) In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 84 no PDB 2GMI . Mms2UBC13~UBIQUITIN . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 85 no PDB 2HD5 . "Usp2 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 86 no PDB 2HTH . "Structural Basis For Ubiquitin Recognition By The Human Eap45ESCRT-Ii Glue Domain" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 87 no PDB 2IBI . "Covalent Ubiquitin-Usp2 Complex" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 88 no PDB 2J7Q . "Crystal Structure Of The Ubiquitin-Specific Protease Encoded By Murine Cytomegalovirus Tegument Protein M48 In Complex With A U" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 89 no PDB 2JF5 . "Crystal Structure Of Lys63-Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 90 no PDB 2JRI . "Solution Structure Of The Josephin Domain Of Ataxin-3 In Complex With Ubiquitin Molecule." . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 91 no PDB 2JY6 . "Solution Structure Of The Complex Of Ubiquitin And Ubiquilin 1 Uba Domain" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 92 no PDB 2JZZ . "Solid-State Nmr Structure Of Microcrystalline Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 93 no PDB 2K25 . "Automated Nmr Structure Of The Ubb By Fapsy" . . . . . 100.00 103 100.00 100.00 7.26e-28 . . . . 5101 1 94 no PDB 2K39 . "Recognition Dynamics Up To Microseconds Revealed From Rdc Derived Ubiquitin Ensemble In Solution" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 95 no PDB 2K6D . "Cin85 Sh3-C Domain In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1 96 no PDB 2K8B . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Cis Isomer In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 97 no PDB 2K8C . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Trans Isomer In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 98 no PDB 2KDE . "Nmr Structure Of Major S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 99 no PDB 2KDF . "Nmr Structure Of Minor S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 100 no PDB 2KHW . "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1 101 no PDB 2KJH . "Nmr Based Structural Model Of The Ubch8-Ubiquitin Complex" . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1 102 no PDB 2KLG . "Pere Nmr Structure Of Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 103 no PDB 2KN5 . "A Correspondence Between Solution-State Dynamics Of An Individual Protein And The Sequence And Conformational Diversity Of Its " . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 104 no PDB 2KOX . "Nmr Residual Dipolar Couplings Identify Long Range Correlated Motions In The Backbone Of The Protein Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 105 no PDB 2KTF . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 106 no PDB 2KWU . "Solution Structure Of Ubm2 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 107 no PDB 2KWV . "Solution Structure Of Ubm1 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 108 no PDB 2KX0 . "The Solution Structure Of Ubb+1, Frameshift Mutant Of Ubiquitin B" . . . . . 100.00 103 100.00 100.00 7.26e-28 . . . . 5101 1 109 no PDB 2L0F . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 (P692a Mutant) In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 110 no PDB 2L0T . "Solution Structure Of The Complex Of Ubiquitin And The Vhs Domain Of Stam2" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 111 no PDB 2L3Z . "Proton-Detected 4d Dream Solid-State Nmr Structure Of Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 112 no PDB 2LD9 . "Backbone Structure Of Ubiquitin Determined Using Backbone Amide Noes And Backbone N-H And N-C Rdcs" . . . . . 96.23 77 100.00 100.00 1.56e-26 . . . . 5101 1 113 no PDB 2LJ5 . "Description Of The Structural Fluctuations Of Proteins From Structure- Based Calculations Of Residual Dipolar Couplings" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 114 no PDB 2LVO . "Structure Of The Gp78cue Domain Bound To Monubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 115 no PDB 2LVP . "Gp78cue Domain Bound To The Distal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 116 no PDB 2LVQ . "Gp78cue Domain Bound To The Proximal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 117 no PDB 2LZ6 . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 118 no PDB 2MBB . "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" . . . . . 98.11 78 98.08 98.08 1.13e-26 . . . . 5101 1 119 no PDB 2MBH . "Nmr Structure Of Eklf(22-40)/ubiquitin Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 120 no PDB 2MBO . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 0 Mm Nacl" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 121 no PDB 2MBQ . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 150 Mm Nacl" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 122 no PDB 2MCN . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 123 no PDB 2MJ5 . "Structure Of The Uba Domain Of Human Nbr1 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 124 no PDB 2MJB . "Solution Nmr Structure Of Ubiquitin Refined Against Dipolar Couplings In 4 Media" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 125 no PDB 2MOR . "A Tensor-free Method For The Structural And Dynamical Refinement Of Proteins Using Residual Dipolar Couplings" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 126 no PDB 2MRE . "Nmr Structure Of The Rad18-ubz/ubiquitin Complex" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1 127 no PDB 2MUR . "Solution Structure Of The Human Faap20 Ubz-ubiquitin Complex" . . . . . 98.11 78 98.08 98.08 1.13e-26 . . . . 5101 1 128 no PDB 2NR2 . "The Mumo (Minimal Under-Restraining Minimal Over- Restraining) Method For The Determination Of Native States Ensembles Of Prote" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 129 no PDB 2O6V . "Crystal Structure And Solution Nmr Studies Of Lys48-Linked Tetraubiquitin At Neutral Ph" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 130 no PDB 2OJR . "Structure Of Ubiquitin Solved By Sad Using The Lanthanide- Binding Tag" . . . . . 98.11 111 98.08 100.00 2.03e-26 . . . . 5101 1 131 no PDB 2OOB . "Crystal Structure Of The Uba Domain From Cbl-B Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 132 no PDB 2PE9 . "Nmr Based Structure Of The Open Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Tenso" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 133 no PDB 2PEA . "Nmr Based Structure Of The Closed Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Ten" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 134 no PDB 2QHO . "Crystal Structure Of The Uba Domain From Edd Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 135 no PDB 2RR9 . "The Solution Structure Of The K63-Ub2:tuims Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 136 no PDB 2RSU . "Alternative Structure Of Ubiquitin" . . . . . 96.23 76 98.04 98.04 6.84e-26 . . . . 5101 1 137 no PDB 2RU6 . "The Pure Alternative State Of Ubiquitin" . . . . . 96.23 76 98.04 98.04 6.84e-26 . . . . 5101 1 138 no PDB 2W9N . "Crystal Structure Of Linear Di-Ubiquitin" . . . . . 94.34 152 100.00 100.00 9.10e-25 . . . . 5101 1 139 no PDB 2WDT . "Crystal Structure Of Plasmodium Falciparum Uchl3 In Complex With The Suicide Inhibitor Ubvme" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1 140 no PDB 2WWZ . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P212121" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 141 no PDB 2WX0 . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P21" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 142 no PDB 2WX1 . "Tab2 Nzf Domain In Complex With Lys63-Linked Tri-Ubiquitin, P212121" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 143 no PDB 2XBB . "Nedd4 Hect:ub Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 144 no PDB 2XEW . "Crystal Structure Of K11-Linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 145 no PDB 2XK5 . "Crystal Structure Of K6-Linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 146 no PDB 2Y5B . "Structure Of Usp21 In Complex With Linear Diubiquitin-Aldehyde" . . . . . 96.23 152 100.00 100.00 8.44e-26 . . . . 5101 1 147 no PDB 2Z59 . "Complex Structures Of Mouse Rpn13 (22-130aa) And Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 148 no PDB 2ZCC . "Ubiquitin Crystallized Under High Pressure" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 149 no PDB 2ZNV . "Crystal Structure Of Human Amsh-Lp Dub Domain In Complex With Lys63-Linked Ubiquitin Dimer" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1 150 no PDB 2ZVN . "Nemo Cozi Domain Incomplex With Diubiquitin In P212121 Space Group" . . . . . 100.00 154 98.11 98.11 1.39e-26 . . . . 5101 1 151 no PDB 2ZVO . "Nemo Cozi Domain In Complex With Diubiquitin In C2 Space Group" . . . . . 100.00 154 98.11 98.11 1.39e-26 . . . . 5101 1 152 no PDB 3A1Q . "Crystal Structure Of The Mouse Rap80 Uims In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1 153 no PDB 3A33 . "Ubch5b~ubiquitin Conjugate" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 154 no PDB 3A9J . "Crystal Structure Of The Mouse Tab2-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1 155 no PDB 3A9K . "Crystal Structure Of The Mouse Tab3-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1 156 no PDB 3AI5 . "Crystal Structure Of Yeast Enhanced Green Fluorescent Protein- Ubiquitin Fusion Protein" . . . . . 100.00 307 100.00 100.00 3.41e-26 . . . . 5101 1 157 no PDB 3ALB . "Cyclic Lys48-Linked Tetraubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 158 no PDB 3AUL . "Crystal Structure Of Wild-Type Lys48-Linked Diubiquitin In An Open Conformation" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 159 no PDB 3AXC . "Crystal Structure Of Linear Diubiquitin" . . . . . 100.00 154 98.11 98.11 1.39e-26 . . . . 5101 1 160 no PDB 3B08 . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 96.23 152 100.00 100.00 1.06e-25 . . . . 5101 1 161 no PDB 3B0A . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 96.23 152 100.00 100.00 1.06e-25 . . . . 5101 1 162 no PDB 3BY4 . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 163 no PDB 3C0R . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 164 no PDB 3DVG . "Crystal Structure Of K63-Specific Fab Apu.3a8 Bound To K63-Linked Di- Ubiquitin" . . . . . 98.11 79 98.08 98.08 1.10e-26 . . . . 5101 1 165 no PDB 3DVN . "Crystal Structure Of K63-specific Fab Apu2.16 Bound To K63-linked Di- Ubiquitin" . . . . . 98.11 79 98.08 98.08 1.10e-26 . . . . 5101 1 166 no PDB 3EEC . "X-Ray Structure Of Human Ubiquitin Cd(Ii) Adduct" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 167 no PDB 3EFU . "X-Ray Structure Of Human Ubiquitin-Hg(Ii) Adduct" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 168 no PDB 3EHV . "X-Ray Structure Of Human Ubiquitin Zn(Ii) Adduct" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 169 no PDB 3H1U . "Structure Of Ubiquitin In Complex With Cd Ions" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 170 no PDB 3H7P . "Crystal Structure Of K63-Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1 171 no PDB 3H7S . "Crystal Structures Of K63-Linked Di- And Tri-Ubiquitin Reveal A Highly Extended Chain Architecture" . . . . . 96.23 76 100.00 100.00 1.15e-26 . . . . 5101 1 172 no PDB 3HM3 . "The Structure And Conformation Of Lys-63 Linked Tetra-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 173 no PDB 3I3T . "Crystal Structure Of Covalent Ubiquitin-usp21 Complex" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 174 no PDB 3IFW . "Crystal Structure Of The S18y Variant Of Ubiquitin Carboxy T Hydrolase L1 Bound To Ubiquitin Vinylmethylester." . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 175 no PDB 3IHP . "Covalent Ubiquitin-Usp5 Complex" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 176 no PDB 3JSV . "Crystal Structure Of Mouse Nemo Cozi In Complex With Lys63- Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1 177 no PDB 3JVZ . E2~ubiquitin-Hect . . . . . 100.00 81 100.00 100.00 4.22e-28 . . . . 5101 1 178 no PDB 3JW0 . E2~ubiquitin-Hect . . . . . 100.00 81 100.00 100.00 4.22e-28 . . . . 5101 1 179 no PDB 3K9O . "The Crystal Structure Of E2-25k And Ubb+1 Complex" . . . . . 96.23 96 100.00 100.00 2.31e-26 . . . . 5101 1 180 no PDB 3K9P . "The Crystal Structure Of E2-25k And Ubiquitin Complex" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1 181 no PDB 3KVF . "Crystal Structure Of The I93m Mutant Of Ubiquitin Carboxy Te Hydrolase L1 Bound To Ubiquitin Vinylmethylester" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 182 no PDB 3KW5 . "Crystal Structure Of Ubiquitin Carboxy Terminal Hydrolase L1 Ubiquitin Vinylmethylester" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 183 no PDB 3LDZ . "Crystal Structure Of Human Stam1 Vhs Domain In Complex With Ubiquitin" . . . . . 96.23 73 100.00 100.00 1.19e-26 . . . . 5101 1 184 no PDB 3M3J . "A New Crystal Form Of Lys48-Linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 185 no PDB 3MHS . "Structure Of The Saga Ubp8SGF11SUS1SGF73 DUB MODULE BOUND Ubiquitin Aldehyde" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1 186 no PDB 3MTN . "Usp21 In Complex With A Ubiquitin-based, Usp21-specific Inhibitor" . . . . . 96.23 85 100.00 100.00 1.61e-26 . . . . 5101 1 187 no PDB 3N30 . "Crystal Structure Of Cubic Zn3-Hub (Human Ubiquitin) Adduct" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 188 no PDB 3N32 . "The Crystal Structure Of Human Ubiquitin Adduct With Zeise's Salt" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 189 no PDB 3NHE . "High Resolution Structure (1.26a) Of Usp2a In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 190 no PDB 3NOB . "Structure Of K11-linked Di-ubiquitin" . . . . . 98.11 78 98.08 98.08 1.13e-26 . . . . 5101 1 191 no PDB 3NS8 . "Crystal Structure Of An Open Conformation Of Lys48-Linked Diubiquitin At Ph 7.5" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 192 no PDB 3O65 . "Crystal Structure Of A Josephin-Ubiquitin Complex: Evolutionary Restraints On Ataxin-3 Deubiquitinating Activity" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1 193 no PDB 3OFI . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 194 no PDB 3OJ3 . "Crystal Structure Of The A20 Znf4 And Ubiquitin Complex" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1 195 no PDB 3OJ4 . "Crystal Structure Of The A20 Znf4, Ubiquitin And Ubch5a Complex" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1 196 no PDB 3ONS . "Crystal Structure Of Human Ubiquitin In A New Crystal Form" . . . . . 96.23 72 100.00 100.00 1.10e-26 . . . . 5101 1 197 no PDB 3PHD . "Crystal Structure Of Human Hdac6 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 198 no PDB 3PHW . "Otu Domain Of Crimean Congo Hemorrhagic Fever Virus In Complex With Ubiquitin" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 199 no PDB 3PRM . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 200 no PDB 3PRP . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 201 no PDB 3PT2 . "Structure Of A Viral Otu Domain Protease Bound To Ubiquitin" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 202 no PDB 3PTF . "X-Ray Structure Of The Non-Covalent Complex Between Ubch5a And Ubiquitin" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1 203 no PDB 3Q3F . "Engineering Domain-Swapped Binding Interfaces By Mutually Exclusive Folding: Insertion Of Ubiquitin Into Position 103 Of Barnas" . . . . . 94.34 189 100.00 100.00 5.85e-25 . . . . 5101 1 204 no PDB 3RUL . "New Strategy To Analyze Structures Of Glycopeptide-Target Complexes" . . . . . 96.23 79 100.00 100.00 1.41e-26 . . . . 5101 1 205 no PDB 3TBL . "Structure Of Mono-ubiquitinated Pcna: Implications For Dna Polymerase Switching And Okazaki Fragment Maturation" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 206 no PDB 3TMP . "The Catalytic Domain Of Human Deubiquitinase Duba In Complex With Ubiquitin Aldehyde" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1 207 no PDB 3U30 . "Crystal Structure Of A Linear-Specific Ubiquitin Fab Bound To Linear Ubiquitin" . . . . . 98.11 172 98.08 98.08 6.45e-26 . . . . 5101 1 208 no PDB 3UGB . "Ubch5c~ubiquitin Conjugate" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 209 no PDB 3VDZ . "Tailoring Encodable Lanthanide-Binding Tags As Mri Contrast Agents: Xq-Dse3-Ubiquitin At 2.4 Angstroms" . . . . . 98.11 111 98.08 100.00 1.11e-26 . . . . 5101 1 210 no PDB 3VFK . "The Structure Of Monodechloro-teicoplanin In Complex With Its Ligand, Using Ubiquitin As A Ligand Carrier" . . . . . 96.23 79 100.00 100.00 1.41e-26 . . . . 5101 1 211 no PDB 3VHT . "Crystal Structure Of Gfp-Wrnip1 Ubz Domain Fusion Protein In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 212 no PDB 3VUW . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form I" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 213 no PDB 3VUX . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form Ii" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 214 no PDB 3VUY . "Crystal Structure Of A20 Zf7 In Complex With Linear Tetraubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 215 no PDB 3ZLZ . "Lys6-linked Tri-ubiquitin" . . . . . 96.23 76 98.04 100.00 2.70e-26 . . . . 5101 1 216 no PDB 3ZNH . "Crimean Congo Hemorrhagic Fever Virus Otu Domain In Complex With Ubiquitin-propargyl." . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1 217 no PDB 3ZNI . "Structure Of Phosphotyr363-cbl-b - Ubch5b-ub - Zap-70 Peptide Complex" . . . . . 100.00 81 100.00 100.00 4.22e-28 . . . . 5101 1 218 no PDB 3ZNZ . "Crystal Structure Of Otulin Otu Domain (c129a) In Complex With Met1-di Ubiquitin" . . . . . 96.23 152 100.00 100.00 1.06e-25 . . . . 5101 1 219 no PDB 4AP4 . "Rnf4 - Ubch5a - Ubiquitin Heterotrimeric Complex" . . . . . 98.11 80 98.08 98.08 1.42e-26 . . . . 5101 1 220 no PDB 4AUQ . "Structure Of Birc7-Ubch5b-Ub Complex." . . . . . 100.00 81 100.00 100.00 4.22e-28 . . . . 5101 1 221 no PDB 4BBN . "Nedd4 Hect-ub:ub Complex" . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1 222 no PDB 4BOS . "Structure Of Otud2 Otu Domain In Complex With Ubiquitin K11- Linked Peptide" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 223 no PDB 4BOZ . "Structure Of Otud2 Otu Domain In Complex With K11-linked Di Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 224 no PDB 4BVU . "Structure Of Shigella Effector Ospg In Complex With Host Ubch5c-ubiquitin Conjugate" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 225 no PDB 4CXC . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1 226 no PDB 4CXD . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 227 no PDB 4DDG . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 228 no PDB 4DDI . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 229 no PDB 4DHJ . "The Structure Of A Ceotub1 Ubiquitin Aldehyde Ubc13~ub Complex" . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1 230 no PDB 4DHZ . "The Structure Of HCEOTUB1-Ubiquitin Aldehyde-Ubc13~ub" . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1 231 no PDB 4HXD . "Diversity Of Ubiquitin And Isg15 Specificity Amongst Nairoviruses Viral Ovarian Tumor Domain Proteases" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 232 no PDB 4I6N . "Crystal Structure Of Trichinella Spiralis Uch37 Catalytic Domain Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 94.34 75 100.00 100.00 1.28e-25 . . . . 5101 1 233 no PDB 4IG7 . "Crystal Structure Of Trichinella Spiralis Uch37 Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 234 no PDB 4IUM . "Equine Arteritis Virus Papain-like Protease 2 (plp2) Covalently Bound To Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1 235 no PDB 4JIO . "Bro1 V Domain And Ubiquitin" . . . . . 96.23 76 98.04 98.04 9.07e-26 . . . . 5101 1 236 no PDB 4JQW . "Crystal Structure Of A Complex Of Nod1 Card And Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 237 no PDB 4K1R . "Crystal Structure Of Schizosaccharomyces Pombe Sst2 Catalytic Domain And Ubiquitin" . . . . . 100.00 81 100.00 100.00 6.23e-28 . . . . 5101 1 238 no PDB 4K7S . "Crystal Structure Of Zn2-hub (human Ubiquitin) Adduct From A Solution 35 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 239 no PDB 4K7U . "Crystal Structure Of Zn2.3-hub (human Ubiquitin) Adduct From A Solution 70 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 240 no PDB 4K7W . "Crystal Structure Of Zn3-hub(human Ubiquitin) Adduct From A Solution 100 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 241 no PDB 4KSK . "Gumby/fam105b In Complex With Ubiquitin" . . . . . 98.11 80 98.08 98.08 1.42e-26 . . . . 5101 1 242 no PDB 4KSL . "Gumby/fam105b In Complex With Linear Di-ubiquitin" . . . . . 96.23 156 100.00 100.00 1.14e-25 . . . . 5101 1 243 no PDB 4KZX . "Rabbit 40s Ribosomal Subunit In Complex With Eif1." . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1 244 no PDB 4KZY . "Rabbit 40s Ribosomal Subunit In Complex With Eif1 And Eif1a." . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1 245 no PDB 4KZZ . "Rabbit 40s Ribosomal Subunit In Complex With Mrna, Initiator Trna And Eif1a" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1 246 no PDB 4LCD . "Structure Of An Rsp5xubxsna3 Complex: Mechanism Of Ubiquitin Ligation And Lysine Prioritization By A Hect E3" . . . . . 98.11 83 98.08 98.08 3.66e-27 . . . . 5101 1 247 no PDB 4LDT . "The Structure Of H/ceotub1-ubiquitin Aldehyde-ubch5b~ub" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1 248 no PDB 4LJO . "Structure Of An Active Ligase (hoip)/ubiquitin Transfer Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 249 no PDB 4LJP . "Structure Of An Active Ligase (hoip-h889a)/ubiquitin Transfer Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 250 no PDB 4M0W . "Crystal Structure Of Sars-cov Papain-like Protease C112s Mutant In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 251 no PDB 4MDK . "Cdc34-ubiquitin-cc0651 Complex" . . . . . 98.11 80 98.08 98.08 1.42e-26 . . . . 5101 1 252 no PDB 4MM3 . "Crystal Structure Of Sars-cov Papain-like Protease Plpro In Complex With Ubiquitin Aldehyde" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1 253 no PDB 4MSM . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 E286a Mutant Bound To Ubiquitin" . . . . . 100.00 81 100.00 100.00 6.23e-28 . . . . 5101 1 254 no PDB 4MSQ . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 Catalytic Domain Bound To Ubiquitin" . . . . . 100.00 81 100.00 100.00 6.23e-28 . . . . 5101 1 255 no PDB 4NQK . "Structure Of An Ubiquitin Complex" . . . . . 98.11 79 98.08 98.08 2.27e-26 . . . . 5101 1 256 no PDB 4NQL . "The Crystal Structure Of The Dub Domain Of Amsh Orthologue, Sst2 From S. Pombe, In Complex With Lysine 63-linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1 257 no PDB 4P4H . "Caught-in-action Signaling Complex Of Rig-i 2card Domain And Mavs Card Domain" . . . . . 98.11 79 98.08 98.08 2.27e-26 . . . . 5101 1 258 no PDB 4PIG . "Crystal Structure Of The Ubiquitin K11s Mutant" . . . . . 96.23 76 98.04 98.04 6.28e-26 . . . . 5101 1 259 no PDB 4PIH . "X-ray Crystal Structure Of The K33s Mutant Of Ubiquitin" . . . . . 96.23 76 98.04 98.04 6.28e-26 . . . . 5101 1 260 no PDB 4PIJ . "X-ray Crystal Structure Of The K11s/k63s Double Mutant Of Ubiquitin" . . . . . 96.23 75 98.04 98.04 4.52e-26 . . . . 5101 1 261 no PDB 4PQT . "Insights Into The Mechanism Of Deubiquitination By Jamm Deubiquitinases From Co-crystal Structures Of Enzyme With Substrate And" . . . . . 100.00 81 100.00 100.00 6.23e-28 . . . . 5101 1 262 no PDB 4RF0 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 263 no PDB 4RF1 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1 264 no PDB 4UN2 . "Crystal Structure Of The Uba Domain Of Dsk2 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 265 no PDB 4UPX . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 266 no PDB 4UQ1 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 267 no PDB 4UQ4 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1 268 no PDB 4UQ5 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1 269 no PDB 4W20 . "Structure Of The Mammalian 60s Ribosomal Subunit (this Entry Contains The Large Ribosomal Proteins)" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 270 no PDB 4W22 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 271 no PDB 4W23 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Small Ribosomal Subunit)" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1 272 no PDB 4W25 . "Structure Of The Idle Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 273 no PDB 4W27 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 274 no PDB 4W28 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Small Ribosomal Subunit)" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1 275 no PDB 4WUR . "The Crystal Structure Of The Mers-cov Papain-like Protease (c111s) With Human Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 276 no PDB 4WZP . "Ser65 Phosphorylated Ubiquitin, Major Conformation" . . . . . 96.23 76 100.00 100.00 1.93e-26 . . . . 5101 1 277 no DBJ BAA03983 . "polyubiquitin [Rattus norvegicus]" . . . . . 96.23 305 100.00 100.00 1.37e-24 . . . . 5101 1 278 no DBJ BAA11389 . "putative ubiquitin extension protein [Brassica rapa]" . . . . . 66.04 112 97.14 97.14 5.41e-14 . . . . 5101 1 279 no DBJ BAA11842 . "ubiquitin [Cavia porcellus]" . . . . . 96.23 311 100.00 100.00 1.53e-24 . . . . 5101 1 280 no DBJ BAA11843 . "ubiquitin extention protein [Cavia porcellus]" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1 281 no DBJ BAA23486 . "polyubiquitin [Homo sapiens]" . . . . . 96.23 609 100.00 100.00 1.25e-23 . . . . 5101 1 282 no EMBL CAA28495 . "ubiquitin [Homo sapiens]" . . . . . 96.23 229 100.00 100.00 6.13e-25 . . . . 5101 1 283 no EMBL CAA30815 . "unnamed protein product [Cricetulus sp.]" . . . . . 96.23 223 100.00 100.00 4.80e-25 . . . . 5101 1 284 no EMBL CAA33466 . "unnamed protein product [Chlamydomonas reinhardtii]" . . . . . 96.23 128 98.04 98.04 1.75e-25 . . . . 5101 1 285 no EMBL CAA35999 . "ubiquitin [Mus musculus]" . . . . . 96.23 305 100.00 100.00 1.37e-24 . . . . 5101 1 286 no EMBL CAA37227 . "unnamed protein product [Drosophila melanogaster]" . . . . . 96.23 128 100.00 100.00 1.52e-26 . . . . 5101 1 287 no GB AAA02769 . "polyprotein [Bovine viral diarrhea virus 1-Osloss]" . . . . . 96.23 3975 98.04 100.00 2.19e-23 . . . . 5101 1 288 no GB AAA28153 . "ubiquitin A, partial [Caenorhabditis elegans]" . . . . . 69.81 37 97.30 97.30 1.29e-14 . . . . 5101 1 289 no GB AAA28154 . "polyubiquitin [Caenorhabditis elegans]" . . . . . 96.23 838 98.04 98.04 1.14e-22 . . . . 5101 1 290 no GB AAA28997 . "ubiquitin [Drosophila melanogaster]" . . . . . 96.23 231 100.00 100.00 5.26e-25 . . . . 5101 1 291 no GB AAA28998 . "ubiquitin-hybrid protein precursor [Drosophila melanogaster]" . . . . . 96.23 156 100.00 100.00 2.71e-26 . . . . 5101 1 292 no PIR I50437 . "polyubiquitin 4 - chicken [Gallus gallus]" . . . . . 96.23 305 100.00 100.00 1.37e-24 . . . . 5101 1 293 no PIR I51568 . "polyubiquitin - African clawed frog (fragment)" . . . . . 100.00 167 98.11 98.11 1.45e-26 . . . . 5101 1 294 no PIR I65237 . "ubiquitin / ribosomal protein L40, cytosolic [validated] - rat" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 295 no PIR JN0790 . "ubiquitin/ribosomal protein CEP52 fusion protein - Leishmania major" . . . . . 96.23 128 98.04 98.04 3.27e-26 . . . . 5101 1 296 no PIR S13928 . "ubiquitin precursor - chicken [Gallus gallus]" . . . . . 96.23 229 100.00 100.00 5.18e-25 . . . . 5101 1 297 no PRF 0412265A . ubiquitin . . . . . 96.23 75 98.04 98.04 6.19e-26 . . . . 5101 1 298 no PRF 1212243A . "ubiquitin S1" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 299 no PRF 1212243B . "ubiquitin S5" . . . . . 96.23 77 98.04 98.04 6.10e-26 . . . . 5101 1 300 no PRF 1212243C . "ubiquitin S3" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1 301 no PRF 1212243D . "ubiquitin S2" . . . . . 96.23 77 98.04 98.04 7.99e-26 . . . . 5101 1 302 no REF NP_001005123 . "ubiquitin A-52 residue ribosomal protein fusion product 1 [Xenopus (Silurana) tropicalis]" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 303 no REF NP_001006688 . "ubiquitin C [Xenopus (Silurana) tropicalis]" . . . . . 96.23 609 100.00 100.00 1.25e-23 . . . . 5101 1 304 no REF NP_001009117 . "polyubiquitin-B [Pan troglodytes]" . . . . . 96.23 229 100.00 100.00 6.13e-25 . . . . 5101 1 305 no REF NP_001009202 . "polyubiquitin-B [Ovis aries]" . . . . . 96.23 305 100.00 100.00 1.66e-24 . . . . 5101 1 306 no REF NP_001009286 . "ubiquitin-60S ribosomal protein L40 [Ovis aries]" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 307 no SP P0C273 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 308 no SP P0C275 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 309 no SP P0C276 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1 310 no SP P0CG47 . "RecName: Full=Polyubiquitin-B; Contains: RecName: Full=Ubiquitin; Flags: Precursor [Homo sapiens]" . . . . . 96.23 229 100.00 100.00 6.13e-25 . . . . 5101 1 311 no SP P0CG48 . "RecName: Full=Polyubiquitin-C; Contains: RecName: Full=Ubiquitin; Flags: Precursor [Homo sapiens]" . . . . . 96.23 685 100.00 100.00 1.59e-23 . . . . 5101 1 312 no TPG DAA18802 . "TPA: polyubiquitin [Bos taurus]" . . . . . 96.23 305 100.00 100.00 1.69e-24 . . . . 5101 1 313 no TPG DAA20663 . "TPA: ubiquitin C [Bos taurus]" . . . . . 96.23 314 98.04 98.04 6.82e-24 . . . . 5101 1 314 no TPG DAA20672 . "TPA: ubiquitin B-like [Bos taurus]" . . . . . 96.23 77 98.04 98.04 1.05e-25 . . . . 5101 1 315 no TPG DAA24675 . "TPA: 40S ribosomal protein S27a [Bos taurus]" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1 316 no TPG DAA26453 . "TPA: ubiquitin and ribosomal protein S27a-like [Bos taurus]" . . . . . 96.23 156 98.04 100.00 2.80e-26 . . . . 5101 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID Ubiquitin common 5101 1 uq1_51 abbreviation 5101 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 -1 GLY . 5101 1 2 0 SER . 5101 1 3 1 MET . 5101 1 4 2 GLN . 5101 1 5 3 ILE . 5101 1 6 4 PHE . 5101 1 7 5 VAL . 5101 1 8 6 LYS . 5101 1 9 7 THR . 5101 1 10 8 LEU . 5101 1 11 9 THR . 5101 1 12 10 GLY . 5101 1 13 11 LYS . 5101 1 14 12 THR . 5101 1 15 13 ILE . 5101 1 16 14 THR . 5101 1 17 15 LEU . 5101 1 18 16 GLU . 5101 1 19 17 VAL . 5101 1 20 18 GLU . 5101 1 21 19 PRO . 5101 1 22 20 SER . 5101 1 23 21 ASP . 5101 1 24 22 THR . 5101 1 25 23 ILE . 5101 1 26 24 GLU . 5101 1 27 25 ASN . 5101 1 28 26 VAL . 5101 1 29 27 LYS . 5101 1 30 28 ALA . 5101 1 31 29 LYS . 5101 1 32 30 ILE . 5101 1 33 31 GLN . 5101 1 34 32 ASP . 5101 1 35 33 LYS . 5101 1 36 34 GLU . 5101 1 37 35 GLY . 5101 1 38 36 ILE . 5101 1 39 37 PRO . 5101 1 40 38 PRO . 5101 1 41 39 ASP . 5101 1 42 40 GLN . 5101 1 43 41 GLN . 5101 1 44 42 ARG . 5101 1 45 43 LEU . 5101 1 46 44 ILE . 5101 1 47 45 PHE . 5101 1 48 46 ALA . 5101 1 49 47 GLY . 5101 1 50 48 LYS . 5101 1 51 49 GLN . 5101 1 52 50 LEU . 5101 1 53 51 GLU . 5101 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . GLY 1 1 5101 1 . SER 2 2 5101 1 . MET 3 3 5101 1 . GLN 4 4 5101 1 . ILE 5 5 5101 1 . PHE 6 6 5101 1 . VAL 7 7 5101 1 . LYS 8 8 5101 1 . THR 9 9 5101 1 . LEU 10 10 5101 1 . THR 11 11 5101 1 . GLY 12 12 5101 1 . LYS 13 13 5101 1 . THR 14 14 5101 1 . ILE 15 15 5101 1 . THR 16 16 5101 1 . LEU 17 17 5101 1 . GLU 18 18 5101 1 . VAL 19 19 5101 1 . GLU 20 20 5101 1 . PRO 21 21 5101 1 . SER 22 22 5101 1 . ASP 23 23 5101 1 . THR 24 24 5101 1 . ILE 25 25 5101 1 . GLU 26 26 5101 1 . ASN 27 27 5101 1 . VAL 28 28 5101 1 . LYS 29 29 5101 1 . ALA 30 30 5101 1 . LYS 31 31 5101 1 . ILE 32 32 5101 1 . GLN 33 33 5101 1 . ASP 34 34 5101 1 . LYS 35 35 5101 1 . GLU 36 36 5101 1 . GLY 37 37 5101 1 . ILE 38 38 5101 1 . PRO 39 39 5101 1 . PRO 40 40 5101 1 . ASP 41 41 5101 1 . GLN 42 42 5101 1 . GLN 43 43 5101 1 . ARG 44 44 5101 1 . LEU 45 45 5101 1 . ILE 46 46 5101 1 . PHE 47 47 5101 1 . ALA 48 48 5101 1 . GLY 49 49 5101 1 . LYS 50 50 5101 1 . GLN 51 51 5101 1 . LEU 52 52 5101 1 . GLU 53 53 5101 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 5101 _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 $uq1_51 . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5101 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 5101 _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 $uq1_51 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21 . . . . . . . . . . . . plasmid . . pGEX-4T3 . . . 'Peptide was expressed as a fusion to GST and then cleaved with thrombin.' . . 5101 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5101 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Ubiquitin '[U-100% 13C; U-100% 15N]' . . 1 $uq1_51 . . 1.0 . . mM . . . . 5101 1 2 'sodium sulphate' . . . . . . . 0.8 . . M . . . . 5101 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5101 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Ubiquitin . . . 1 $uq1_51 . . 1.0 . . mM . . . . 5101 2 2 'sodium sulphate' . . . . . . . 0.8 . . M . . . . 5101 2 stop_ save_ ####################### # Sample conditions # ####################### save_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode conditions_1 _Sample_condition_list.Entry_ID 5101 _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 pH 7.0 0.2 na 5101 1 temperature 298 1 K 5101 1 'ionic strength' 0.8 0.1 M 5101 1 pressure 1 0.1 atm 5101 1 stop_ save_ ############################ # Computer software used # ############################ save_AZARA _Software.Sf_category software _Software.Sf_framecode AZARA _Software.Entry_ID 5101 _Software.ID 1 _Software.Name AZARA _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 5101 1 stop_ save_ save_ANSIG _Software.Sf_category software _Software.Sf_framecode ANSIG _Software.Entry_ID 5101 _Software.ID 2 _Software.Name ANSIG _Software.Version 3.3 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID assignment 5101 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5101 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5101 _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 NMR_spectrometer Bruker DRX . 500 . . . 5101 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 5101 _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 '3D 1H-1H-15N NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1 2 '3D 1H-1H-15N TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1 3 '3D 13C-1H-1H NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1 4 '3D 1H-13C-1H HCCH-TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1 5 '3D CBCA(CO)NH' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1 6 '3D HNCA' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1 7 '3D HN(CO)CA' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5101 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '3D 1H-1H-15N NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5101 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '3D 1H-1H-15N TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5101 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '3D 13C-1H-1H NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5101 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '3D 1H-13C-1H HCCH-TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5101 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '3D CBCA(CO)NH' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5101 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name '3D HNCA' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 5101 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name '3D HN(CO)CA' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5101 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 5101 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5101 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5101 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5101 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _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 '3D 1H-1H-15N NOESY' . . . 5101 1 2 '3D 1H-1H-15N TOCSY' . . . 5101 1 3 '3D 13C-1H-1H NOESY' . . . 5101 1 4 '3D 1H-13C-1H HCCH-TOCSY' . . . 5101 1 5 '3D CBCA(CO)NH' . . . 5101 1 6 '3D HNCA' . . . 5101 1 7 '3D HN(CO)CA' . . . 5101 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 GLY CA C 13 43.61 0.05 . 1 . . . . -1 . . . 5101 1 2 . 1 1 1 1 GLY HA2 H 1 3.89 0.01 . 2 . . . . -1 . . . 5101 1 3 . 1 1 1 1 GLY HA3 H 1 3.76 0.01 . 2 . . . . -1 . . . 5101 1 4 . 1 1 2 2 SER CA C 13 58.41 0.05 . 1 . . . . 0 . . . 5101 1 5 . 1 1 2 2 SER CB C 13 64.28 0.05 . 1 . . . . 0 . . . 5101 1 6 . 1 1 2 2 SER HA H 1 4.58 0.01 . 1 . . . . 0 . . . 5101 1 7 . 1 1 2 2 SER HB2 H 1 3.82 0.01 . 1 . . . . 0 . . . 5101 1 8 . 1 1 2 2 SER HB3 H 1 3.82 0.01 . 1 . . . . 0 . . . 5101 1 9 . 1 1 2 2 SER N N 15 115.16 0.05 . 1 . . . . 0 . . . 5101 1 10 . 1 1 3 3 MET CB C 13 35.66 0.05 . 1 . . . . 1 . . . 5101 1 11 . 1 1 3 3 MET CE C 13 17.70 0.05 . 1 . . . . 1 . . . 5101 1 12 . 1 1 3 3 MET CG C 13 31.17 0.05 . 1 . . . . 1 . . . 5101 1 13 . 1 1 3 3 MET HA H 1 4.72 0.01 . 1 . . . . 1 . . . 5101 1 14 . 1 1 3 3 MET HB2 H 1 1.93 0.01 . 1 . . . . 1 . . . 5101 1 15 . 1 1 3 3 MET HB3 H 1 1.93 0.01 . 1 . . . . 1 . . . 5101 1 16 . 1 1 3 3 MET HE1 H 1 1.97 0.01 . 1 . . . . 1 . . . 5101 1 17 . 1 1 3 3 MET HE2 H 1 1.97 0.01 . 1 . . . . 1 . . . 5101 1 18 . 1 1 3 3 MET HE3 H 1 1.97 0.01 . 1 . . . . 1 . . . 5101 1 19 . 1 1 3 3 MET HG2 H 1 2.31 0.01 . 1 . . . . 1 . . . 5101 1 20 . 1 1 3 3 MET HG3 H 1 2.31 0.01 . 1 . . . . 1 . . . 5101 1 21 . 1 1 3 3 MET H H 1 8.94 0.01 . 1 . . . . 1 . . . 5101 1 22 . 1 1 3 3 MET N N 15 121.26 0.05 . 1 . . . . 1 . . . 5101 1 23 . 1 1 4 4 GLN CA C 13 55.30 0.05 . 1 . . . . 2 . . . 5101 1 24 . 1 1 4 4 GLN CB C 13 30.59 0.05 . 1 . . . . 2 . . . 5101 1 25 . 1 1 4 4 GLN CG C 13 34.45 0.05 . 1 . . . . 2 . . . 5101 1 26 . 1 1 4 4 GLN HA H 1 4.88 0.01 . 1 . . . . 2 . . . 5101 1 27 . 1 1 4 4 GLN HB2 H 1 1.83 0.01 . 2 . . . . 2 . . . 5101 1 28 . 1 1 4 4 GLN HB3 H 1 1.60 0.01 . 2 . . . . 2 . . . 5101 1 29 . 1 1 4 4 GLN HE21 H 1 6.78 0.01 . 2 . . . . 2 . . . 5101 1 30 . 1 1 4 4 GLN HE22 H 1 7.46 0.01 . 2 . . . . 2 . . . 5101 1 31 . 1 1 4 4 GLN HG2 H 1 2.17 0.01 . 2 . . . . 2 . . . 5101 1 32 . 1 1 4 4 GLN HG3 H 1 1.90 0.01 . 2 . . . . 2 . . . 5101 1 33 . 1 1 4 4 GLN H H 1 8.42 0.01 . 1 . . . . 2 . . . 5101 1 34 . 1 1 4 4 GLN N N 15 121.47 0.05 . 1 . . . . 2 . . . 5101 1 35 . 1 1 5 5 ILE CA C 13 58.80 0.05 . 1 . . . . 3 . . . 5101 1 36 . 1 1 5 5 ILE CB C 13 40.81 0.05 . 1 . . . . 3 . . . 5101 1 37 . 1 1 5 5 ILE CD1 C 13 15.37 0.05 . 2 . . . . 3 . . . 5101 1 38 . 1 1 5 5 ILE CG1 C 13 20.70 0.05 . 2 . . . . 3 . . . 5101 1 39 . 1 1 5 5 ILE CG2 C 13 20.10 0.05 . 1 . . . . 3 . . . 5101 1 40 . 1 1 5 5 ILE HA H 1 4.58 0.01 . 1 . . . . 3 . . . 5101 1 41 . 1 1 5 5 ILE HB H 1 1.88 0.01 . 1 . . . . 3 . . . 5101 1 42 . 1 1 5 5 ILE HD11 H 1 0.44 0.01 . 1 . . . . 3 . . . 5101 1 43 . 1 1 5 5 ILE HD12 H 1 0.44 0.01 . 1 . . . . 3 . . . 5101 1 44 . 1 1 5 5 ILE HD13 H 1 0.44 0.01 . 1 . . . . 3 . . . 5101 1 45 . 1 1 5 5 ILE HG12 H 1 1.19 0.01 . 2 . . . . 3 . . . 5101 1 46 . 1 1 5 5 ILE HG13 H 1 0.87 0.01 . 2 . . . . 3 . . . 5101 1 47 . 1 1 5 5 ILE HG21 H 1 0.84 0.01 . 1 . . . . 3 . . . 5101 1 48 . 1 1 5 5 ILE HG22 H 1 0.84 0.01 . 1 . . . . 3 . . . 5101 1 49 . 1 1 5 5 ILE HG23 H 1 0.84 0.01 . 1 . . . . 3 . . . 5101 1 50 . 1 1 5 5 ILE H H 1 8.67 0.01 . 1 . . . . 3 . . . 5101 1 51 . 1 1 5 5 ILE N N 15 117.51 0.05 . 1 . . . . 3 . . . 5101 1 52 . 1 1 6 6 PHE CA C 13 56.40 0.05 . 1 . . . . 4 . . . 5101 1 53 . 1 1 6 6 PHE CB C 13 41.38 0.05 . 1 . . . . 4 . . . 5101 1 54 . 1 1 6 6 PHE CD1 C 13 130.70 0.05 . 1 . . . . 4 . . . 5101 1 55 . 1 1 6 6 PHE CD2 C 13 130.70 0.05 . 1 . . . . 4 . . . 5101 1 56 . 1 1 6 6 PHE CE1 C 13 130.79 0.05 . 1 . . . . 4 . . . 5101 1 57 . 1 1 6 6 PHE CE2 C 13 130.79 0.05 . 1 . . . . 4 . . . 5101 1 58 . 1 1 6 6 PHE HA H 1 5.26 0.01 . 1 . . . . 4 . . . 5101 1 59 . 1 1 6 6 PHE HB2 H 1 2.78 0.01 . 2 . . . . 4 . . . 5101 1 60 . 1 1 6 6 PHE HB3 H 1 3.01 0.01 . 2 . . . . 4 . . . 5101 1 61 . 1 1 6 6 PHE HD1 H 1 7.12 0.01 . 1 . . . . 4 . . . 5101 1 62 . 1 1 6 6 PHE HD2 H 1 7.12 0.01 . 1 . . . . 4 . . . 5101 1 63 . 1 1 6 6 PHE HE1 H 1 7.24 0.01 . 1 . . . . 4 . . . 5101 1 64 . 1 1 6 6 PHE HE2 H 1 7.24 0.01 . 1 . . . . 4 . . . 5101 1 65 . 1 1 6 6 PHE H H 1 8.51 0.01 . 1 . . . . 4 . . . 5101 1 66 . 1 1 6 6 PHE N N 15 119.86 0.05 . 1 . . . . 4 . . . 5101 1 67 . 1 1 7 7 VAL CA C 13 60.28 0.05 . 1 . . . . 5 . . . 5101 1 68 . 1 1 7 7 VAL CB C 13 34.16 0.05 . 1 . . . . 5 . . . 5101 1 69 . 1 1 7 7 VAL CG1 C 13 21.13 0.05 . 1 . . . . 5 . . . 5101 1 70 . 1 1 7 7 VAL CG2 C 13 21.13 0.05 . 1 . . . . 5 . . . 5101 1 71 . 1 1 7 7 VAL HA H 1 5.00 0.01 . 1 . . . . 5 . . . 5101 1 72 . 1 1 7 7 VAL HB H 1 1.90 0.01 . 1 . . . . 5 . . . 5101 1 73 . 1 1 7 7 VAL HG11 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1 74 . 1 1 7 7 VAL HG12 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1 75 . 1 1 7 7 VAL HG13 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1 76 . 1 1 7 7 VAL HG21 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1 77 . 1 1 7 7 VAL HG22 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1 78 . 1 1 7 7 VAL HG23 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1 79 . 1 1 7 7 VAL H H 1 9.26 0.01 . 1 . . . . 5 . . . 5101 1 80 . 1 1 7 7 VAL N N 15 122.14 0.05 . 1 . . . . 5 . . . 5101 1 81 . 1 1 8 8 LYS CA C 13 54.65 0.05 . 1 . . . . 6 . . . 5101 1 82 . 1 1 8 8 LYS CB C 13 32.84 0.05 . 1 . . . . 6 . . . 5101 1 83 . 1 1 8 8 LYS CD C 13 28.98 0.05 . 1 . . . . 6 . . . 5101 1 84 . 1 1 8 8 LYS CG C 13 24.98 0.05 . 1 . . . . 6 . . . 5101 1 85 . 1 1 8 8 LYS HA H 1 5.09 0.01 . 1 . . . . 6 . . . 5101 1 86 . 1 1 8 8 LYS HB2 H 1 1.85 0.01 . 2 . . . . 6 . . . 5101 1 87 . 1 1 8 8 LYS HB3 H 1 1.65 0.01 . 2 . . . . 6 . . . 5101 1 88 . 1 1 8 8 LYS HD2 H 1 1.59 0.01 . 1 . . . . 6 . . . 5101 1 89 . 1 1 8 8 LYS HD3 H 1 1.59 0.01 . 1 . . . . 6 . . . 5101 1 90 . 1 1 8 8 LYS HE2 H 1 2.83 0.01 . 1 . . . . 6 . . . 5101 1 91 . 1 1 8 8 LYS HE3 H 1 2.83 0.01 . 1 . . . . 6 . . . 5101 1 92 . 1 1 8 8 LYS HG2 H 1 1.39 0.01 . 1 . . . . 6 . . . 5101 1 93 . 1 1 8 8 LYS HG3 H 1 1.39 0.01 . 1 . . . . 6 . . . 5101 1 94 . 1 1 8 8 LYS H H 1 8.71 0.01 . 1 . . . . 6 . . . 5101 1 95 . 1 1 8 8 LYS N N 15 127.14 0.05 . 1 . . . . 6 . . . 5101 1 96 . 1 1 9 9 THR CA C 13 61.12 0.05 . 1 . . . . 7 . . . 5101 1 97 . 1 1 9 9 THR CG2 C 13 22.88 0.05 . 1 . . . . 7 . . . 5101 1 98 . 1 1 9 9 THR HA H 1 4.33 0.01 . 1 . . . . 7 . . . 5101 1 99 . 1 1 9 9 THR HB H 1 4.70 0.01 . 1 . . . . 7 . . . 5101 1 100 . 1 1 9 9 THR HG21 H 1 1.15 0.01 . 1 . . . . 7 . . . 5101 1 101 . 1 1 9 9 THR HG22 H 1 1.15 0.01 . 1 . . . . 7 . . . 5101 1 102 . 1 1 9 9 THR HG23 H 1 1.15 0.01 . 1 . . . . 7 . . . 5101 1 103 . 1 1 9 9 THR H H 1 8.75 0.01 . 1 . . . . 7 . . . 5101 1 104 . 1 1 9 9 THR N N 15 114.88 0.05 . 1 . . . . 7 . . . 5101 1 105 . 1 1 10 10 LEU CA C 13 57.45 0.05 . 1 . . . . 8 . . . 5101 1 106 . 1 1 10 10 LEU CB C 13 41.10 0.05 . 1 . . . . 8 . . . 5101 1 107 . 1 1 10 10 LEU CD1 C 13 25.15 0.05 . 2 . . . . 8 . . . 5101 1 108 . 1 1 10 10 LEU CD2 C 13 23.03 0.05 . 2 . . . . 8 . . . 5101 1 109 . 1 1 10 10 LEU CG C 13 27.53 0.05 . 1 . . . . 8 . . . 5101 1 110 . 1 1 10 10 LEU HA H 1 4.17 0.01 . 1 . . . . 8 . . . 5101 1 111 . 1 1 10 10 LEU HB2 H 1 1.82 0.01 . 2 . . . . 8 . . . 5101 1 112 . 1 1 10 10 LEU HB3 H 1 1.65 0.01 . 2 . . . . 8 . . . 5101 1 113 . 1 1 10 10 LEU HD11 H 1 0.93 0.01 . 2 . . . . 8 . . . 5101 1 114 . 1 1 10 10 LEU HD12 H 1 0.93 0.01 . 2 . . . . 8 . . . 5101 1 115 . 1 1 10 10 LEU HD13 H 1 0.93 0.01 . 2 . . . . 8 . . . 5101 1 116 . 1 1 10 10 LEU HD21 H 1 0.84 0.01 . 2 . . . . 8 . . . 5101 1 117 . 1 1 10 10 LEU HD22 H 1 0.84 0.01 . 2 . . . . 8 . . . 5101 1 118 . 1 1 10 10 LEU HD23 H 1 0.84 0.01 . 2 . . . . 8 . . . 5101 1 119 . 1 1 10 10 LEU HG H 1 1.67 0.01 . 1 . . . . 8 . . . 5101 1 120 . 1 1 10 10 LEU H H 1 9.03 0.01 . 1 . . . . 8 . . . 5101 1 121 . 1 1 10 10 LEU N N 15 119.50 0.05 . 1 . . . . 8 . . . 5101 1 122 . 1 1 11 11 THR CA C 13 61.41 0.05 . 1 . . . . 9 . . . 5101 1 123 . 1 1 11 11 THR CB C 13 69.21 0.05 . 1 . . . . 9 . . . 5101 1 124 . 1 1 11 11 THR CG2 C 13 22.08 0.05 . 1 . . . . 9 . . . 5101 1 125 . 1 1 11 11 THR HA H 1 4.39 0.01 . 1 . . . . 9 . . . 5101 1 126 . 1 1 11 11 THR HB H 1 4.52 0.01 . 1 . . . . 9 . . . 5101 1 127 . 1 1 11 11 THR HG21 H 1 1.21 0.01 . 1 . . . . 9 . . . 5101 1 128 . 1 1 11 11 THR HG22 H 1 1.21 0.01 . 1 . . . . 9 . . . 5101 1 129 . 1 1 11 11 THR HG23 H 1 1.21 0.01 . 1 . . . . 9 . . . 5101 1 130 . 1 1 11 11 THR H H 1 7.57 0.01 . 1 . . . . 9 . . . 5101 1 131 . 1 1 11 11 THR N N 15 105.51 0.05 . 1 . . . . 9 . . . 5101 1 132 . 1 1 12 12 GLY CA C 13 45.90 0.05 . 1 . . . . 10 . . . 5101 1 133 . 1 1 12 12 GLY HA2 H 1 4.27 0.01 . 2 . . . . 10 . . . 5101 1 134 . 1 1 12 12 GLY HA3 H 1 3.60 0.01 . 2 . . . . 10 . . . 5101 1 135 . 1 1 12 12 GLY H H 1 7.78 0.01 . 1 . . . . 10 . . . 5101 1 136 . 1 1 12 12 GLY N N 15 109.47 0.05 . 1 . . . . 10 . . . 5101 1 137 . 1 1 13 13 LYS CA C 13 55.58 0.05 . 1 . . . . 11 . . . 5101 1 138 . 1 1 13 13 LYS CB C 13 33.79 0.05 . 1 . . . . 11 . . . 5101 1 139 . 1 1 13 13 LYS CD C 13 29.12 0.05 . 1 . . . . 11 . . . 5101 1 140 . 1 1 13 13 LYS CG C 13 24.95 0.05 . 1 . . . . 11 . . . 5101 1 141 . 1 1 13 13 LYS HA H 1 4.44 0.01 . 1 . . . . 11 . . . 5101 1 142 . 1 1 13 13 LYS HB2 H 1 1.66 0.01 . 1 . . . . 11 . . . 5101 1 143 . 1 1 13 13 LYS HB3 H 1 1.66 0.01 . 1 . . . . 11 . . . 5101 1 144 . 1 1 13 13 LYS HD2 H 1 1.60 0.01 . 1 . . . . 11 . . . 5101 1 145 . 1 1 13 13 LYS HD3 H 1 1.60 0.01 . 1 . . . . 11 . . . 5101 1 146 . 1 1 13 13 LYS HE2 H 1 2.92 0.01 . 1 . . . . 11 . . . 5101 1 147 . 1 1 13 13 LYS HE3 H 1 2.92 0.01 . 1 . . . . 11 . . . 5101 1 148 . 1 1 13 13 LYS HG2 H 1 1.27 0.01 . 1 . . . . 11 . . . 5101 1 149 . 1 1 13 13 LYS HG3 H 1 1.27 0.01 . 1 . . . . 11 . . . 5101 1 150 . 1 1 13 13 LYS H H 1 7.31 0.01 . 1 . . . . 11 . . . 5101 1 151 . 1 1 13 13 LYS N N 15 120.59 0.05 . 1 . . . . 11 . . . 5101 1 152 . 1 1 14 14 THR CA C 13 62.33 0.05 . 1 . . . . 12 . . . 5101 1 153 . 1 1 14 14 THR CB C 13 69.60 0.05 . 1 . . . . 12 . . . 5101 1 154 . 1 1 14 14 THR CG2 C 13 21.98 0.05 . 1 . . . . 12 . . . 5101 1 155 . 1 1 14 14 THR HA H 1 5.33 0.01 . 1 . . . . 12 . . . 5101 1 156 . 1 1 14 14 THR HB H 1 3.97 0.01 . 1 . . . . 12 . . . 5101 1 157 . 1 1 14 14 THR HG21 H 1 1.14 0.01 . 1 . . . . 12 . . . 5101 1 158 . 1 1 14 14 THR HG22 H 1 1.14 0.01 . 1 . . . . 12 . . . 5101 1 159 . 1 1 14 14 THR HG23 H 1 1.14 0.01 . 1 . . . . 12 . . . 5101 1 160 . 1 1 14 14 THR H H 1 8.65 0.01 . 1 . . . . 12 . . . 5101 1 161 . 1 1 14 14 THR N N 15 119.66 0.05 . 1 . . . . 12 . . . 5101 1 162 . 1 1 15 15 ILE CB C 13 41.78 0.05 . 1 . . . . 13 . . . 5101 1 163 . 1 1 15 15 ILE CD1 C 13 14.37 0.05 . 1 . . . . 13 . . . 5101 1 164 . 1 1 15 15 ILE CG1 C 13 26.93 0.05 . 1 . . . . 13 . . . 5101 1 165 . 1 1 15 15 ILE CG2 C 13 18.82 0.05 . 1 . . . . 13 . . . 5101 1 166 . 1 1 15 15 ILE HA H 1 4.72 0.01 . 1 . . . . 13 . . . 5101 1 167 . 1 1 15 15 ILE HB H 1 1.93 0.01 . 1 . . . . 13 . . . 5101 1 168 . 1 1 15 15 ILE HD11 H 1 0.68 0.01 . 1 . . . . 13 . . . 5101 1 169 . 1 1 15 15 ILE HD12 H 1 0.68 0.01 . 1 . . . . 13 . . . 5101 1 170 . 1 1 15 15 ILE HD13 H 1 0.68 0.01 . 1 . . . . 13 . . . 5101 1 171 . 1 1 15 15 ILE HG12 H 1 1.23 0.01 . 2 . . . . 13 . . . 5101 1 172 . 1 1 15 15 ILE HG13 H 1 1.07 0.01 . 2 . . . . 13 . . . 5101 1 173 . 1 1 15 15 ILE HG21 H 1 0.83 0.01 . 1 . . . . 13 . . . 5101 1 174 . 1 1 15 15 ILE HG22 H 1 0.83 0.01 . 1 . . . . 13 . . . 5101 1 175 . 1 1 15 15 ILE HG23 H 1 0.83 0.01 . 1 . . . . 13 . . . 5101 1 176 . 1 1 15 15 ILE H H 1 9.24 0.01 . 1 . . . . 13 . . . 5101 1 177 . 1 1 15 15 ILE N N 15 124.29 0.05 . 1 . . . . 13 . . . 5101 1 178 . 1 1 16 16 THR CA C 13 60.19 0.05 . 1 . . . . 14 . . . 5101 1 179 . 1 1 16 16 THR CB C 13 70.87 0.05 . 1 . . . . 14 . . . 5101 1 180 . 1 1 16 16 THR CG2 C 13 22.97 0.05 . 1 . . . . 14 . . . 5101 1 181 . 1 1 16 16 THR HA H 1 5.15 0.01 . 1 . . . . 14 . . . 5101 1 182 . 1 1 16 16 THR HB H 1 3.83 0.01 . 1 . . . . 14 . . . 5101 1 183 . 1 1 16 16 THR HG21 H 1 0.79 0.01 . 1 . . . . 14 . . . 5101 1 184 . 1 1 16 16 THR HG22 H 1 0.79 0.01 . 1 . . . . 14 . . . 5101 1 185 . 1 1 16 16 THR HG23 H 1 0.79 0.01 . 1 . . . . 14 . . . 5101 1 186 . 1 1 16 16 THR H H 1 8.26 0.01 . 1 . . . . 14 . . . 5101 1 187 . 1 1 16 16 THR N N 15 113.92 0.05 . 1 . . . . 14 . . . 5101 1 188 . 1 1 17 17 LEU CA C 13 53.68 0.05 . 1 . . . . 15 . . . 5101 1 189 . 1 1 17 17 LEU CB C 13 46.03 0.05 . 1 . . . . 15 . . . 5101 1 190 . 1 1 17 17 LEU CD1 C 13 24.82 0.05 . 2 . . . . 15 . . . 5101 1 191 . 1 1 17 17 LEU CD2 C 13 25.62 0.05 . 2 . . . . 15 . . . 5101 1 192 . 1 1 17 17 LEU CG C 13 27.30 0.05 . 1 . . . . 15 . . . 5101 1 193 . 1 1 17 17 LEU HA H 1 4.58 0.01 . 1 . . . . 15 . . . 5101 1 194 . 1 1 17 17 LEU HB2 H 1 1.35 0.01 . 2 . . . . 15 . . . 5101 1 195 . 1 1 17 17 LEU HB3 H 1 1.14 0.01 . 2 . . . . 15 . . . 5101 1 196 . 1 1 17 17 LEU HD11 H 1 0.66 0.01 . 2 . . . . 15 . . . 5101 1 197 . 1 1 17 17 LEU HD12 H 1 0.66 0.01 . 2 . . . . 15 . . . 5101 1 198 . 1 1 17 17 LEU HD13 H 1 0.66 0.01 . 2 . . . . 15 . . . 5101 1 199 . 1 1 17 17 LEU HD21 H 1 0.62 0.01 . 2 . . . . 15 . . . 5101 1 200 . 1 1 17 17 LEU HD22 H 1 0.62 0.01 . 2 . . . . 15 . . . 5101 1 201 . 1 1 17 17 LEU HD23 H 1 0.62 0.01 . 2 . . . . 15 . . . 5101 1 202 . 1 1 17 17 LEU HG H 1 1.38 0.01 . 1 . . . . 15 . . . 5101 1 203 . 1 1 17 17 LEU H H 1 8.30 0.01 . 1 . . . . 15 . . . 5101 1 204 . 1 1 17 17 LEU N N 15 123.19 0.05 . 1 . . . . 15 . . . 5101 1 205 . 1 1 18 18 GLU CA C 13 55.48 0.05 . 1 . . . . 16 . . . 5101 1 206 . 1 1 18 18 GLU CB C 13 30.83 0.05 . 1 . . . . 16 . . . 5101 1 207 . 1 1 18 18 GLU CG C 13 36.62 0.05 . 1 . . . . 16 . . . 5101 1 208 . 1 1 18 18 GLU HA H 1 5.03 0.01 . 1 . . . . 16 . . . 5101 1 209 . 1 1 18 18 GLU HB2 H 1 1.83 0.01 . 1 . . . . 16 . . . 5101 1 210 . 1 1 18 18 GLU HB3 H 1 1.83 0.01 . 1 . . . . 16 . . . 5101 1 211 . 1 1 18 18 GLU HG2 H 1 2.17 0.01 . 2 . . . . 16 . . . 5101 1 212 . 1 1 18 18 GLU HG3 H 1 2.04 0.01 . 2 . . . . 16 . . . 5101 1 213 . 1 1 18 18 GLU H H 1 8.30 0.01 . 1 . . . . 16 . . . 5101 1 214 . 1 1 18 18 GLU N N 15 121.07 0.05 . 1 . . . . 16 . . . 5101 1 215 . 1 1 19 19 VAL CB C 13 34.62 0.05 . 1 . . . . 17 . . . 5101 1 216 . 1 1 19 19 VAL CG1 C 13 32.27 0.05 . 2 . . . . 17 . . . 5101 1 217 . 1 1 19 19 VAL CG2 C 13 19.29 0.05 . 2 . . . . 17 . . . 5101 1 218 . 1 1 19 19 VAL HA H 1 4.69 0.01 . 1 . . . . 17 . . . 5101 1 219 . 1 1 19 19 VAL HB H 1 2.53 0.01 . 1 . . . . 17 . . . 5101 1 220 . 1 1 19 19 VAL HG11 H 1 0.72 0.01 . 2 . . . . 17 . . . 5101 1 221 . 1 1 19 19 VAL HG12 H 1 0.72 0.01 . 2 . . . . 17 . . . 5101 1 222 . 1 1 19 19 VAL HG13 H 1 0.72 0.01 . 2 . . . . 17 . . . 5101 1 223 . 1 1 19 19 VAL HG21 H 1 0.58 0.01 . 2 . . . . 17 . . . 5101 1 224 . 1 1 19 19 VAL HG22 H 1 0.58 0.01 . 2 . . . . 17 . . . 5101 1 225 . 1 1 19 19 VAL HG23 H 1 0.58 0.01 . 2 . . . . 17 . . . 5101 1 226 . 1 1 19 19 VAL H H 1 8.65 0.01 . 1 . . . . 17 . . . 5101 1 227 . 1 1 19 19 VAL N N 15 116.00 0.05 . 1 . . . . 17 . . . 5101 1 228 . 1 1 20 20 GLU CA C 13 53.03 0.05 . 1 . . . . 18 . . . 5101 1 229 . 1 1 20 20 GLU CB C 13 30.68 0.05 . 1 . . . . 18 . . . 5101 1 230 . 1 1 20 20 GLU CG C 13 35.63 0.05 . 1 . . . . 18 . . . 5101 1 231 . 1 1 20 20 GLU HA H 1 4.91 0.01 . 1 . . . . 18 . . . 5101 1 232 . 1 1 20 20 GLU HB2 H 1 2.04 0.01 . 2 . . . . 18 . . . 5101 1 233 . 1 1 20 20 GLU HB3 H 1 1.74 0.01 . 2 . . . . 18 . . . 5101 1 234 . 1 1 20 20 GLU HG2 H 1 2.31 0.01 . 1 . . . . 18 . . . 5101 1 235 . 1 1 20 20 GLU HG3 H 1 2.31 0.01 . 1 . . . . 18 . . . 5101 1 236 . 1 1 20 20 GLU H H 1 8.55 0.01 . 2 . . . . 18 . . . 5101 1 237 . 1 1 20 20 GLU N N 15 120.16 0.05 . 1 . . . . 18 . . . 5101 1 238 . 1 1 21 21 PRO CA C 13 64.73 0.05 . 1 . . . . 19 . . . 5101 1 239 . 1 1 21 21 PRO CB C 13 32.06 0.05 . 1 . . . . 19 . . . 5101 1 240 . 1 1 21 21 PRO CD C 13 50.73 0.05 . 1 . . . . 19 . . . 5101 1 241 . 1 1 21 21 PRO CG C 13 27.79 0.05 . 1 . . . . 19 . . . 5101 1 242 . 1 1 21 21 PRO HA H 1 4.18 0.01 . 1 . . . . 19 . . . 5101 1 243 . 1 1 21 21 PRO HB2 H 1 2.05 0.01 . 2 . . . . 19 . . . 5101 1 244 . 1 1 21 21 PRO HB3 H 1 2.32 0.01 . 2 . . . . 19 . . . 5101 1 245 . 1 1 21 21 PRO HD2 H 1 3.74 0.01 . 2 . . . . 19 . . . 5101 1 246 . 1 1 21 21 PRO HD3 H 1 3.73 0.01 . 2 . . . . 19 . . . 5101 1 247 . 1 1 21 21 PRO HG2 H 1 2.18 0.01 . 2 . . . . 19 . . . 5101 1 248 . 1 1 21 21 PRO HG3 H 1 1.97 0.01 . 2 . . . . 19 . . . 5101 1 249 . 1 1 22 22 SER CA C 13 57.48 0.05 . 1 . . . . 20 . . . 5101 1 250 . 1 1 22 22 SER CB C 13 63.29 0.05 . 1 . . . . 20 . . . 5101 1 251 . 1 1 22 22 SER HA H 1 4.35 0.01 . 1 . . . . 20 . . . 5101 1 252 . 1 1 22 22 SER HB2 H 1 4.16 0.01 . 2 . . . . 20 . . . 5101 1 253 . 1 1 22 22 SER HB3 H 1 3.78 0.01 . 2 . . . . 20 . . . 5101 1 254 . 1 1 22 22 SER H H 1 7.12 0.01 . 1 . . . . 20 . . . 5101 1 255 . 1 1 22 22 SER N N 15 104.57 0.05 . 1 . . . . 20 . . . 5101 1 256 . 1 1 23 23 ASP CB C 13 41.12 0.05 . 1 . . . . 21 . . . 5101 1 257 . 1 1 23 23 ASP HA H 1 4.74 0.01 . 1 . . . . 21 . . . 5101 1 258 . 1 1 23 23 ASP HB2 H 1 2.88 0.01 . 2 . . . . 21 . . . 5101 1 259 . 1 1 23 23 ASP HB3 H 1 2.50 0.01 . 2 . . . . 21 . . . 5101 1 260 . 1 1 23 23 ASP H H 1 7.89 0.01 . 1 . . . . 21 . . . 5101 1 261 . 1 1 23 23 ASP N N 15 123.85 0.05 . 1 . . . . 21 . . . 5101 1 262 . 1 1 24 24 THR CA C 13 59.61 0.05 . 1 . . . . 22 . . . 5101 1 263 . 1 1 24 24 THR CB C 13 71.08 0.05 . 1 . . . . 22 . . . 5101 1 264 . 1 1 24 24 THR CG2 C 13 22.47 0.05 . 1 . . . . 22 . . . 5101 1 265 . 1 1 24 24 THR HA H 1 4.84 0.01 . 1 . . . . 22 . . . 5101 1 266 . 1 1 24 24 THR HB H 1 4.60 0.01 . 1 . . . . 22 . . . 5101 1 267 . 1 1 24 24 THR HG21 H 1 1.23 0.01 . 1 . . . . 22 . . . 5101 1 268 . 1 1 24 24 THR HG22 H 1 1.23 0.01 . 1 . . . . 22 . . . 5101 1 269 . 1 1 24 24 THR HG23 H 1 1.23 0.01 . 1 . . . . 22 . . . 5101 1 270 . 1 1 24 24 THR H H 1 8.17 0.01 . 1 . . . . 22 . . . 5101 1 271 . 1 1 24 24 THR N N 15 109.09 0.05 . 1 . . . . 22 . . . 5101 1 272 . 1 1 25 25 ILE CA C 13 65.13 0.05 . 1 . . . . 23 . . . 5101 1 273 . 1 1 25 25 ILE CB C 13 36.70 0.05 . 1 . . . . 23 . . . 5101 1 274 . 1 1 25 25 ILE CD1 C 13 11.93 0.05 . 1 . . . . 23 . . . 5101 1 275 . 1 1 25 25 ILE CG1 C 13 28.50 0.05 . 1 . . . . 23 . . . 5101 1 276 . 1 1 25 25 ILE CG2 C 13 18.23 0.05 . 1 . . . . 23 . . . 5101 1 277 . 1 1 25 25 ILE HA H 1 3.62 0.01 . 1 . . . . 23 . . . 5101 1 278 . 1 1 25 25 ILE HB H 1 2.21 0.01 . 1 . . . . 23 . . . 5101 1 279 . 1 1 25 25 ILE HD11 H 1 0.83 0.01 . 1 . . . . 23 . . . 5101 1 280 . 1 1 25 25 ILE HD12 H 1 0.83 0.01 . 1 . . . . 23 . . . 5101 1 281 . 1 1 25 25 ILE HD13 H 1 0.83 0.01 . 1 . . . . 23 . . . 5101 1 282 . 1 1 25 25 ILE HG12 H 1 1.27 0.01 . 2 . . . . 23 . . . 5101 1 283 . 1 1 25 25 ILE HG13 H 1 1.60 0.01 . 2 . . . . 23 . . . 5101 1 284 . 1 1 25 25 ILE HG21 H 1 0.91 0.01 . 1 . . . . 23 . . . 5101 1 285 . 1 1 25 25 ILE HG22 H 1 0.91 0.01 . 1 . . . . 23 . . . 5101 1 286 . 1 1 25 25 ILE HG23 H 1 0.91 0.01 . 1 . . . . 23 . . . 5101 1 287 . 1 1 25 25 ILE H H 1 8.48 0.01 . 1 . . . . 23 . . . 5101 1 288 . 1 1 25 25 ILE N N 15 120.45 0.05 . 1 . . . . 23 . . . 5101 1 289 . 1 1 26 26 GLU CA C 13 59.41 0.05 . 1 . . . . 24 . . . 5101 1 290 . 1 1 26 26 GLU CB C 13 29.43 0.05 . 1 . . . . 24 . . . 5101 1 291 . 1 1 26 26 GLU CG C 13 35.16 0.05 . 1 . . . . 24 . . . 5101 1 292 . 1 1 26 26 GLU HA H 1 3.95 0.01 . 1 . . . . 24 . . . 5101 1 293 . 1 1 26 26 GLU HB2 H 1 2.01 0.01 . 2 . . . . 24 . . . 5101 1 294 . 1 1 26 26 GLU HB3 H 1 1.87 0.01 . 2 . . . . 24 . . . 5101 1 295 . 1 1 26 26 GLU HG2 H 1 2.17 0.01 . 1 . . . . 24 . . . 5101 1 296 . 1 1 26 26 GLU HG3 H 1 2.17 0.01 . 1 . . . . 24 . . . 5101 1 297 . 1 1 26 26 GLU H H 1 8.69 0.01 . 1 . . . . 24 . . . 5101 1 298 . 1 1 26 26 GLU N N 15 116.72 0.05 . 1 . . . . 24 . . . 5101 1 299 . 1 1 27 27 ASN CA C 13 55.97 0.05 . 1 . . . . 25 . . . 5101 1 300 . 1 1 27 27 ASN CB C 13 38.53 0.05 . 1 . . . . 25 . . . 5101 1 301 . 1 1 27 27 ASN HA H 1 4.51 0.01 . 1 . . . . 25 . . . 5101 1 302 . 1 1 27 27 ASN HB2 H 1 3.06 0.01 . 2 . . . . 25 . . . 5101 1 303 . 1 1 27 27 ASN HB3 H 1 2.81 0.01 . 2 . . . . 25 . . . 5101 1 304 . 1 1 27 27 ASN HD22 H 1 8.02 0.01 . 2 . . . . 25 . . . 5101 1 305 . 1 1 27 27 ASN H H 1 7.87 0.01 . 1 . . . . 25 . . . 5101 1 306 . 1 1 27 27 ASN N N 15 120.19 0.05 . 1 . . . . 25 . . . 5101 1 307 . 1 1 28 28 VAL CA C 13 67.00 0.05 . 1 . . . . 26 . . . 5101 1 308 . 1 1 28 28 VAL CB C 13 31.16 0.05 . 1 . . . . 26 . . . 5101 1 309 . 1 1 28 28 VAL CG1 C 13 23.67 0.05 . 2 . . . . 26 . . . 5101 1 310 . 1 1 28 28 VAL CG2 C 13 23.71 0.05 . 2 . . . . 26 . . . 5101 1 311 . 1 1 28 28 VAL HA H 1 3.50 0.01 . 1 . . . . 26 . . . 5101 1 312 . 1 1 28 28 VAL HB H 1 2.14 0.01 . 1 . . . . 26 . . . 5101 1 313 . 1 1 28 28 VAL HG11 H 1 1.06 0.01 . 2 . . . . 26 . . . 5101 1 314 . 1 1 28 28 VAL HG12 H 1 1.06 0.01 . 2 . . . . 26 . . . 5101 1 315 . 1 1 28 28 VAL HG13 H 1 1.06 0.01 . 2 . . . . 26 . . . 5101 1 316 . 1 1 28 28 VAL HG21 H 1 0.52 0.01 . 2 . . . . 26 . . . 5101 1 317 . 1 1 28 28 VAL HG22 H 1 0.52 0.01 . 2 . . . . 26 . . . 5101 1 318 . 1 1 28 28 VAL HG23 H 1 0.52 0.01 . 2 . . . . 26 . . . 5101 1 319 . 1 1 28 28 VAL H H 1 8.47 0.01 . 1 . . . . 26 . . . 5101 1 320 . 1 1 28 28 VAL N N 15 122.87 0.05 . 1 . . . . 26 . . . 5101 1 321 . 1 1 29 29 LYS CA C 13 59.67 0.05 . 1 . . . . 27 . . . 5101 1 322 . 1 1 29 29 LYS CB C 13 33.71 0.05 . 1 . . . . 27 . . . 5101 1 323 . 1 1 29 29 LYS CE C 13 42.72 0.05 . 1 . . . . 27 . . . 5101 1 324 . 1 1 29 29 LYS CG C 13 25.90 0.05 . 1 . . . . 27 . . . 5101 1 325 . 1 1 29 29 LYS HA H 1 4.48 0.01 . 1 . . . . 27 . . . 5101 1 326 . 1 1 29 29 LYS HB2 H 1 2.03 0.01 . 2 . . . . 27 . . . 5101 1 327 . 1 1 29 29 LYS HB3 H 1 1.46 0.01 . 2 . . . . 27 . . . 5101 1 328 . 1 1 29 29 LYS HD2 H 1 1.66 0.01 . 1 . . . . 27 . . . 5101 1 329 . 1 1 29 29 LYS HD3 H 1 1.66 0.01 . 1 . . . . 27 . . . 5101 1 330 . 1 1 29 29 LYS HE2 H 1 2.83 0.01 . 1 . . . . 27 . . . 5101 1 331 . 1 1 29 29 LYS HE3 H 1 2.83 0.01 . 1 . . . . 27 . . . 5101 1 332 . 1 1 29 29 LYS HG2 H 1 1.86 0.01 . 2 . . . . 27 . . . 5101 1 333 . 1 1 29 29 LYS HG3 H 1 1.70 0.01 . 2 . . . . 27 . . . 5101 1 334 . 1 1 29 29 LYS H H 1 8.65 0.01 . 1 . . . . 27 . . . 5101 1 335 . 1 1 29 29 LYS N N 15 117.95 0.05 . 1 . . . . 27 . . . 5101 1 336 . 1 1 30 30 ALA CA C 13 55.15 0.05 . 1 . . . . 28 . . . 5101 1 337 . 1 1 30 30 ALA CB C 13 18.13 0.05 . 1 . . . . 28 . . . 5101 1 338 . 1 1 30 30 ALA HA H 1 4.12 0.01 . 1 . . . . 28 . . . 5101 1 339 . 1 1 30 30 ALA HB1 H 1 1.53 0.01 . 1 . . . . 28 . . . 5101 1 340 . 1 1 30 30 ALA HB2 H 1 1.53 0.01 . 1 . . . . 28 . . . 5101 1 341 . 1 1 30 30 ALA HB3 H 1 1.53 0.01 . 1 . . . . 28 . . . 5101 1 342 . 1 1 30 30 ALA H H 1 7.78 0.01 . 1 . . . . 28 . . . 5101 1 343 . 1 1 30 30 ALA N N 15 121.61 0.05 . 1 . . . . 28 . . . 5101 1 344 . 1 1 31 31 LYS CA C 13 59.27 0.05 . 1 . . . . 29 . . . 5101 1 345 . 1 1 31 31 LYS CB C 13 32.20 0.05 . 1 . . . . 29 . . . 5101 1 346 . 1 1 31 31 LYS CD C 13 29.69 0.05 . 1 . . . . 29 . . . 5101 1 347 . 1 1 31 31 LYS CG C 13 25.84 0.05 . 1 . . . . 29 . . . 5101 1 348 . 1 1 31 31 LYS HA H 1 4.09 0.01 . 1 . . . . 29 . . . 5101 1 349 . 1 1 31 31 LYS HB2 H 1 1.83 0.01 . 2 . . . . 29 . . . 5101 1 350 . 1 1 31 31 LYS HB3 H 1 1.95 0.01 . 2 . . . . 29 . . . 5101 1 351 . 1 1 31 31 LYS HD2 H 1 1.54 0.01 . 1 . . . . 29 . . . 5101 1 352 . 1 1 31 31 LYS HD3 H 1 1.54 0.01 . 1 . . . . 29 . . . 5101 1 353 . 1 1 31 31 LYS HE2 H 1 2.92 0.01 . 1 . . . . 29 . . . 5101 1 354 . 1 1 31 31 LYS HE3 H 1 2.92 0.01 . 1 . . . . 29 . . . 5101 1 355 . 1 1 31 31 LYS HG2 H 1 1.60 0.01 . 2 . . . . 29 . . . 5101 1 356 . 1 1 31 31 LYS HG3 H 1 1.35 0.01 . 2 . . . . 29 . . . 5101 1 357 . 1 1 31 31 LYS H H 1 7.80 0.01 . 1 . . . . 29 . . . 5101 1 358 . 1 1 31 31 LYS N N 15 121.20 0.05 . 1 . . . . 29 . . . 5101 1 359 . 1 1 32 32 ILE CA C 13 65.69 0.05 . 1 . . . . 30 . . . 5101 1 360 . 1 1 32 32 ILE CB C 13 37.03 0.05 . 1 . . . . 30 . . . 5101 1 361 . 1 1 32 32 ILE CD1 C 13 14.39 0.05 . 1 . . . . 30 . . . 5101 1 362 . 1 1 32 32 ILE CG1 C 13 30.19 0.05 . 1 . . . . 30 . . . 5101 1 363 . 1 1 32 32 ILE CG2 C 13 17.68 0.05 . 1 . . . . 30 . . . 5101 1 364 . 1 1 32 32 ILE HA H 1 3.26 0.01 . 1 . . . . 30 . . . 5101 1 365 . 1 1 32 32 ILE HB H 1 1.81 0.01 . 1 . . . . 30 . . . 5101 1 366 . 1 1 32 32 ILE HD11 H 1 -0.03 0.01 . 1 . . . . 30 . . . 5101 1 367 . 1 1 32 32 ILE HD12 H 1 -0.03 0.01 . 1 . . . . 30 . . . 5101 1 368 . 1 1 32 32 ILE HD13 H 1 -0.03 0.01 . 1 . . . . 30 . . . 5101 1 369 . 1 1 32 32 ILE HG12 H 1 0.37 0.01 . 2 . . . . 30 . . . 5101 1 370 . 1 1 32 32 ILE HG13 H 1 1.27 0.01 . 2 . . . . 30 . . . 5101 1 371 . 1 1 32 32 ILE HG21 H 1 0.52 0.01 . 1 . . . . 30 . . . 5101 1 372 . 1 1 32 32 ILE HG22 H 1 0.52 0.01 . 1 . . . . 30 . . . 5101 1 373 . 1 1 32 32 ILE HG23 H 1 0.52 0.01 . 1 . . . . 30 . . . 5101 1 374 . 1 1 32 32 ILE H H 1 8.10 0.01 . 1 . . . . 30 . . . 5101 1 375 . 1 1 32 32 ILE N N 15 120.42 0.05 . 1 . . . . 30 . . . 5101 1 376 . 1 1 33 33 GLN CA C 13 59.79 0.05 . 1 . . . . 31 . . . 5101 1 377 . 1 1 33 33 GLN CB C 13 28.02 0.05 . 1 . . . . 31 . . . 5101 1 378 . 1 1 33 33 GLN CG C 13 33.67 0.05 . 1 . . . . 31 . . . 5101 1 379 . 1 1 33 33 GLN HA H 1 3.74 0.01 . 1 . . . . 31 . . . 5101 1 380 . 1 1 33 33 GLN HB2 H 1 2.27 0.01 . 2 . . . . 31 . . . 5101 1 381 . 1 1 33 33 GLN HB3 H 1 1.85 0.01 . 2 . . . . 31 . . . 5101 1 382 . 1 1 33 33 GLN HE21 H 1 6.84 0.01 . 2 . . . . 31 . . . 5101 1 383 . 1 1 33 33 GLN HE22 H 1 7.60 0.01 . 2 . . . . 31 . . . 5101 1 384 . 1 1 33 33 GLN HG2 H 1 1.96 0.01 . 1 . . . . 31 . . . 5101 1 385 . 1 1 33 33 GLN HG3 H 1 1.96 0.01 . 1 . . . . 31 . . . 5101 1 386 . 1 1 33 33 GLN H H 1 8.19 0.01 . 1 . . . . 31 . . . 5101 1 387 . 1 1 33 33 GLN N N 15 122.43 0.05 . 1 . . . . 31 . . . 5101 1 388 . 1 1 34 34 ASP CA C 13 57.22 0.05 . 1 . . . . 32 . . . 5101 1 389 . 1 1 34 34 ASP CB C 13 41.58 0.05 . 1 . . . . 32 . . . 5101 1 390 . 1 1 34 34 ASP HA H 1 4.25 0.01 . 1 . . . . 32 . . . 5101 1 391 . 1 1 34 34 ASP HB2 H 1 2.74 0.01 . 2 . . . . 32 . . . 5101 1 392 . 1 1 34 34 ASP HB3 H 1 2.68 0.01 . 2 . . . . 32 . . . 5101 1 393 . 1 1 34 34 ASP H H 1 8.08 0.01 . 1 . . . . 32 . . . 5101 1 394 . 1 1 34 34 ASP N N 15 119.95 0.05 . 1 . . . . 32 . . . 5101 1 395 . 1 1 35 35 LYS CA C 13 58.42 0.05 . 1 . . . . 33 . . . 5101 1 396 . 1 1 35 35 LYS CB C 13 33.74 0.05 . 1 . . . . 33 . . . 5101 1 397 . 1 1 35 35 LYS CD C 13 28.70 0.05 . 1 . . . . 33 . . . 5101 1 398 . 1 1 35 35 LYS CE C 13 42.38 0.05 . 1 . . . . 33 . . . 5101 1 399 . 1 1 35 35 LYS CG C 13 25.16 0.05 . 1 . . . . 33 . . . 5101 1 400 . 1 1 35 35 LYS HA H 1 4.19 0.01 . 1 . . . . 33 . . . 5101 1 401 . 1 1 35 35 LYS HB2 H 1 1.85 0.01 . 1 . . . . 33 . . . 5101 1 402 . 1 1 35 35 LYS HB3 H 1 1.85 0.01 . 1 . . . . 33 . . . 5101 1 403 . 1 1 35 35 LYS HD2 H 1 1.59 0.01 . 1 . . . . 33 . . . 5101 1 404 . 1 1 35 35 LYS HD3 H 1 1.59 0.01 . 1 . . . . 33 . . . 5101 1 405 . 1 1 35 35 LYS HE2 H 1 2.96 0.01 . 1 . . . . 33 . . . 5101 1 406 . 1 1 35 35 LYS HE3 H 1 2.96 0.01 . 1 . . . . 33 . . . 5101 1 407 . 1 1 35 35 LYS HG2 H 1 1.51 0.01 . 1 . . . . 33 . . . 5101 1 408 . 1 1 35 35 LYS HG3 H 1 1.51 0.01 . 1 . . . . 33 . . . 5101 1 409 . 1 1 35 35 LYS H H 1 8.05 0.01 . 1 . . . . 33 . . . 5101 1 410 . 1 1 35 35 LYS N N 15 115.80 0.05 . 1 . . . . 33 . . . 5101 1 411 . 1 1 36 36 GLU CB C 13 32.10 0.05 . 1 . . . . 34 . . . 5101 1 412 . 1 1 36 36 GLU HA H 1 4.61 0.01 . 1 . . . . 34 . . . 5101 1 413 . 1 1 36 36 GLU HB2 H 1 2.30 0.01 . 2 . . . . 34 . . . 5101 1 414 . 1 1 36 36 GLU HB3 H 1 1.58 0.01 . 2 . . . . 34 . . . 5101 1 415 . 1 1 36 36 GLU HG2 H 1 2.01 0.01 . 1 . . . . 34 . . . 5101 1 416 . 1 1 36 36 GLU HG3 H 1 2.01 0.01 . 1 . . . . 34 . . . 5101 1 417 . 1 1 36 36 GLU H H 1 8.46 0.01 . 1 . . . . 34 . . . 5101 1 418 . 1 1 36 36 GLU N N 15 113.62 0.05 . 1 . . . . 34 . . . 5101 1 419 . 1 1 37 37 GLY CA C 13 46.47 0.05 . 1 . . . . 35 . . . 5101 1 420 . 1 1 37 37 GLY HA2 H 1 4.04 0.01 . 2 . . . . 35 . . . 5101 1 421 . 1 1 37 37 GLY HA3 H 1 3.92 0.01 . 2 . . . . 35 . . . 5101 1 422 . 1 1 37 37 GLY H H 1 8.00 0.01 . 1 . . . . 35 . . . 5101 1 423 . 1 1 37 37 GLY N N 15 108.68 0.05 . 1 . . . . 35 . . . 5101 1 424 . 1 1 38 38 ILE CA C 13 58.81 0.05 . 1 . . . . 36 . . . 5101 1 425 . 1 1 38 38 ILE CB C 13 39.70 0.05 . 1 . . . . 36 . . . 5101 1 426 . 1 1 38 38 ILE CD1 C 13 13.38 0.05 . 1 . . . . 36 . . . 5101 1 427 . 1 1 38 38 ILE CG1 C 13 27.58 0.05 . 1 . . . . 36 . . . 5101 1 428 . 1 1 38 38 ILE CG2 C 13 18.60 0.05 . 1 . . . . 36 . . . 5101 1 429 . 1 1 38 38 ILE HA H 1 4.35 0.01 . 1 . . . . 36 . . . 5101 1 430 . 1 1 38 38 ILE HB H 1 1.42 0.01 . 1 . . . . 36 . . . 5101 1 431 . 1 1 38 38 ILE HD11 H 1 0.69 0.01 . 1 . . . . 36 . . . 5101 1 432 . 1 1 38 38 ILE HD12 H 1 0.69 0.01 . 1 . . . . 36 . . . 5101 1 433 . 1 1 38 38 ILE HD13 H 1 0.69 0.01 . 1 . . . . 36 . . . 5101 1 434 . 1 1 38 38 ILE HG12 H 1 1.40 0.01 . 2 . . . . 36 . . . 5101 1 435 . 1 1 38 38 ILE HG13 H 1 0.94 0.01 . 2 . . . . 36 . . . 5101 1 436 . 1 1 38 38 ILE HG21 H 1 0.89 0.01 . 1 . . . . 36 . . . 5101 1 437 . 1 1 38 38 ILE HG22 H 1 0.89 0.01 . 1 . . . . 36 . . . 5101 1 438 . 1 1 38 38 ILE HG23 H 1 0.89 0.01 . 1 . . . . 36 . . . 5101 1 439 . 1 1 38 38 ILE H H 1 6.29 0.01 . 1 . . . . 36 . . . 5101 1 440 . 1 1 38 38 ILE N N 15 119.43 0.05 . 1 . . . . 36 . . . 5101 1 441 . 1 1 39 39 PRO CA C 13 61.75 0.05 . 1 . . . . 37 . . . 5101 1 442 . 1 1 39 39 PRO CB C 13 31.75 0.05 . 1 . . . . 37 . . . 5101 1 443 . 1 1 39 39 PRO CD C 13 51.03 0.05 . 1 . . . . 37 . . . 5101 1 444 . 1 1 39 39 PRO CG C 13 28.45 0.05 . 1 . . . . 37 . . . 5101 1 445 . 1 1 39 39 PRO HA H 1 4.53 0.01 . 1 . . . . 37 . . . 5101 1 446 . 1 1 39 39 PRO HB2 H 1 2.39 0.01 . 2 . . . . 37 . . . 5101 1 447 . 1 1 39 39 PRO HB3 H 1 1.84 0.01 . 2 . . . . 37 . . . 5101 1 448 . 1 1 39 39 PRO HD2 H 1 3.48 0.01 . 2 . . . . 37 . . . 5101 1 449 . 1 1 39 39 PRO HD3 H 1 4.27 0.01 . 2 . . . . 37 . . . 5101 1 450 . 1 1 39 39 PRO HG2 H 1 2.01 0.01 . 1 . . . . 37 . . . 5101 1 451 . 1 1 39 39 PRO HG3 H 1 2.01 0.01 . 1 . . . . 37 . . . 5101 1 452 . 1 1 40 40 PRO CA C 13 66.14 0.05 . 1 . . . . 38 . . . 5101 1 453 . 1 1 40 40 PRO CB C 13 32.66 0.05 . 1 . . . . 38 . . . 5101 1 454 . 1 1 40 40 PRO CD C 13 50.86 0.05 . 1 . . . . 38 . . . 5101 1 455 . 1 1 40 40 PRO CG C 13 27.60 0.05 . 1 . . . . 38 . . . 5101 1 456 . 1 1 40 40 PRO HA H 1 4.160 0.01 . 1 . . . . 38 . . . 5101 1 457 . 1 1 40 40 PRO HB2 H 1 2.03 0.01 . 2 . . . . 38 . . . 5101 1 458 . 1 1 40 40 PRO HB3 H 1 2.21 0.01 . 2 . . . . 38 . . . 5101 1 459 . 1 1 40 40 PRO HD2 H 1 3.72 0.01 . 1 . . . . 38 . . . 5101 1 460 . 1 1 40 40 PRO HD3 H 1 3.72 0.01 . 1 . . . . 38 . . . 5101 1 461 . 1 1 40 40 PRO HG2 H 1 2.15 0.01 . 2 . . . . 38 . . . 5101 1 462 . 1 1 40 40 PRO HG3 H 1 1.71 0.01 . 2 . . . . 38 . . . 5101 1 463 . 1 1 41 41 ASP CA C 13 55.90 0.05 . 1 . . . . 39 . . . 5101 1 464 . 1 1 41 41 ASP CB C 13 39.83 0.05 . 1 . . . . 39 . . . 5101 1 465 . 1 1 41 41 ASP HA H 1 4.46 0.01 . 1 . . . . 39 . . . 5101 1 466 . 1 1 41 41 ASP HB2 H 1 2.71 0.01 . 1 . . . . 39 . . . 5101 1 467 . 1 1 41 41 ASP HB3 H 1 2.71 0.01 . 1 . . . . 39 . . . 5101 1 468 . 1 1 41 41 ASP H H 1 8.68 0.01 . 1 . . . . 39 . . . 5101 1 469 . 1 1 41 41 ASP N N 15 114.55 0.05 . 1 . . . . 39 . . . 5101 1 470 . 1 1 42 42 GLN CA C 13 54.96 0.05 . 1 . . . . 40 . . . 5101 1 471 . 1 1 42 42 GLN CB C 13 30.03 0.05 . 1 . . . . 40 . . . 5101 1 472 . 1 1 42 42 GLN CG C 13 34.47 0.05 . 1 . . . . 40 . . . 5101 1 473 . 1 1 42 42 GLN HA H 1 4.35 0.01 . 1 . . . . 40 . . . 5101 1 474 . 1 1 42 42 GLN HB2 H 1 2.57 0.01 . 2 . . . . 40 . . . 5101 1 475 . 1 1 42 42 GLN HB3 H 1 1.79 0.01 . 2 . . . . 40 . . . 5101 1 476 . 1 1 42 42 GLN HE21 H 1 7.69 0.01 . 2 . . . . 40 . . . 5101 1 477 . 1 1 42 42 GLN HE22 H 1 6.81 0.01 . 2 . . . . 40 . . . 5101 1 478 . 1 1 42 42 GLN HG2 H 1 2.32 0.01 . 1 . . . . 40 . . . 5101 1 479 . 1 1 42 42 GLN HG3 H 1 2.32 0.01 . 1 . . . . 40 . . . 5101 1 480 . 1 1 42 42 GLN H H 1 7.96 0.01 . 1 . . . . 40 . . . 5101 1 481 . 1 1 42 42 GLN N N 15 117.05 0.05 . 1 . . . . 40 . . . 5101 1 482 . 1 1 43 43 GLN CA C 13 55.62 0.05 . 1 . . . . 41 . . . 5101 1 483 . 1 1 43 43 GLN HA H 1 4.57 0.01 . 1 . . . . 41 . . . 5101 1 484 . 1 1 43 43 GLN HB2 H 1 2.00 0.01 . 1 . . . . 41 . . . 5101 1 485 . 1 1 43 43 GLN HB3 H 1 2.00 0.01 . 1 . . . . 41 . . . 5101 1 486 . 1 1 43 43 GLN HE21 H 1 6.74 0.01 . 2 . . . . 41 . . . 5101 1 487 . 1 1 43 43 GLN HE22 H 1 6.54 0.01 . 2 . . . . 41 . . . 5101 1 488 . 1 1 43 43 GLN H H 1 7.18 0.01 . 1 . . . . 41 . . . 5101 1 489 . 1 1 43 43 GLN N N 15 117.97 0.05 . 1 . . . . 41 . . . 5101 1 490 . 1 1 44 44 ARG CA C 13 54.67 0.05 . 1 . . . . 42 . . . 5101 1 491 . 1 1 44 44 ARG CB C 13 32.37 0.05 . 1 . . . . 42 . . . 5101 1 492 . 1 1 44 44 ARG CD C 13 43.27 0.05 . 1 . . . . 42 . . . 5101 1 493 . 1 1 44 44 ARG CG C 13 27.31 0.05 . 1 . . . . 42 . . . 5101 1 494 . 1 1 44 44 ARG HA H 1 4.59 0.01 . 1 . . . . 42 . . . 5101 1 495 . 1 1 44 44 ARG HB2 H 1 1.65 0.01 . 1 . . . . 42 . . . 5101 1 496 . 1 1 44 44 ARG HB3 H 1 1.65 0.01 . 1 . . . . 42 . . . 5101 1 497 . 1 1 44 44 ARG HD2 H 1 2.79 0.01 . 1 . . . . 42 . . . 5101 1 498 . 1 1 44 44 ARG HD3 H 1 2.79 0.01 . 1 . . . . 42 . . . 5101 1 499 . 1 1 44 44 ARG HG2 H 1 1.52 0.01 . 2 . . . . 42 . . . 5101 1 500 . 1 1 44 44 ARG HG3 H 1 1.42 0.01 . 2 . . . . 42 . . . 5101 1 501 . 1 1 44 44 ARG H H 1 9.14 0.01 . 1 . . . . 42 . . . 5101 1 502 . 1 1 44 44 ARG N N 15 125.09 0.05 . 1 . . . . 42 . . . 5101 1 503 . 1 1 45 45 LEU CA C 13 55.50 0.05 . 1 . . . . 43 . . . 5101 1 504 . 1 1 45 45 LEU CB C 13 42.86 0.05 . 1 . . . . 43 . . . 5101 1 505 . 1 1 45 45 LEU CD1 C 13 23.25 0.05 . 2 . . . . 43 . . . 5101 1 506 . 1 1 45 45 LEU CD2 C 13 26.70 0.05 . 2 . . . . 43 . . . 5101 1 507 . 1 1 45 45 LEU CG C 13 28.50 0.05 . 1 . . . . 43 . . . 5101 1 508 . 1 1 45 45 LEU HA H 1 4.58 0.01 . 1 . . . . 43 . . . 5101 1 509 . 1 1 45 45 LEU HB2 H 1 1.48 0.01 . 2 . . . . 43 . . . 5101 1 510 . 1 1 45 45 LEU HB3 H 1 1.23 0.01 . 2 . . . . 43 . . . 5101 1 511 . 1 1 45 45 LEU HD11 H 1 0.19 0.01 . 2 . . . . 43 . . . 5101 1 512 . 1 1 45 45 LEU HD12 H 1 0.19 0.01 . 2 . . . . 43 . . . 5101 1 513 . 1 1 45 45 LEU HD13 H 1 0.19 0.01 . 2 . . . . 43 . . . 5101 1 514 . 1 1 45 45 LEU HD21 H 1 0.67 0.01 . 2 . . . . 43 . . . 5101 1 515 . 1 1 45 45 LEU HD22 H 1 0.67 0.01 . 2 . . . . 43 . . . 5101 1 516 . 1 1 45 45 LEU HD23 H 1 0.67 0.01 . 2 . . . . 43 . . . 5101 1 517 . 1 1 45 45 LEU HG H 1 0.87 0.01 . 1 . . . . 43 . . . 5101 1 518 . 1 1 45 45 LEU H H 1 8.74 0.01 . 1 . . . . 43 . . . 5101 1 519 . 1 1 45 45 LEU N N 15 127.01 0.05 . 1 . . . . 43 . . . 5101 1 520 . 1 1 46 46 ILE CA C 13 59.79 0.05 . 1 . . . . 44 . . . 5101 1 521 . 1 1 46 46 ILE CB C 13 41.60 0.05 . 1 . . . . 44 . . . 5101 1 522 . 1 1 46 46 ILE CD1 C 13 15.24 0.05 . 1 . . . . 44 . . . 5101 1 523 . 1 1 46 46 ILE CG1 C 13 28.49 0.05 . 1 . . . . 44 . . . 5101 1 524 . 1 1 46 46 ILE CG2 C 13 18.10 0.05 . 1 . . . . 44 . . . 5101 1 525 . 1 1 46 46 ILE HA H 1 5.00 0.01 . 1 . . . . 44 . . . 5101 1 526 . 1 1 46 46 ILE HB H 1 1.70 0.01 . 1 . . . . 44 . . . 5101 1 527 . 1 1 46 46 ILE HD11 H 1 0.67 0.01 . 1 . . . . 44 . . . 5101 1 528 . 1 1 46 46 ILE HD12 H 1 0.67 0.01 . 1 . . . . 44 . . . 5101 1 529 . 1 1 46 46 ILE HD13 H 1 0.67 0.01 . 1 . . . . 44 . . . 5101 1 530 . 1 1 46 46 ILE HG12 H 1 0.86 0.01 . 2 . . . . 44 . . . 5101 1 531 . 1 1 46 46 ILE HG13 H 1 1.40 0.01 . 2 . . . . 44 . . . 5101 1 532 . 1 1 46 46 ILE HG21 H 1 0.75 0.01 . 1 . . . . 44 . . . 5101 1 533 . 1 1 46 46 ILE HG22 H 1 0.75 0.01 . 1 . . . . 44 . . . 5101 1 534 . 1 1 46 46 ILE HG23 H 1 0.75 0.01 . 1 . . . . 44 . . . 5101 1 535 . 1 1 46 46 ILE H H 1 9.13 0.01 . 1 . . . . 44 . . . 5101 1 536 . 1 1 46 46 ILE N N 15 125.22 0.05 . 1 . . . . 44 . . . 5101 1 537 . 1 1 47 47 PHE CA C 13 55.96 0.05 . 1 . . . . 45 . . . 5101 1 538 . 1 1 47 47 PHE CB C 13 41.23 0.05 . 1 . . . . 45 . . . 5101 1 539 . 1 1 47 47 PHE CD1 C 13 131.70 0.05 . 1 . . . . 45 . . . 5101 1 540 . 1 1 47 47 PHE CD2 C 13 131.70 0.05 . 1 . . . . 45 . . . 5101 1 541 . 1 1 47 47 PHE CE1 C 13 129.99 0.05 . 1 . . . . 45 . . . 5101 1 542 . 1 1 47 47 PHE CE2 C 13 129.99 0.05 . 1 . . . . 45 . . . 5101 1 543 . 1 1 47 47 PHE CZ C 13 127.33 0.05 . 1 . . . . 45 . . . 5101 1 544 . 1 1 47 47 PHE HA H 1 5.26 0.01 . 1 . . . . 45 . . . 5101 1 545 . 1 1 47 47 PHE HB2 H 1 2.53 0.01 . 2 . . . . 45 . . . 5101 1 546 . 1 1 47 47 PHE HB3 H 1 3.00 0.01 . 2 . . . . 45 . . . 5101 1 547 . 1 1 47 47 PHE HD1 H 1 7.20 0.01 . 1 . . . . 45 . . . 5101 1 548 . 1 1 47 47 PHE HD2 H 1 7.20 0.01 . 1 . . . . 45 . . . 5101 1 549 . 1 1 47 47 PHE HE1 H 1 6.92 0.01 . 1 . . . . 45 . . . 5101 1 550 . 1 1 47 47 PHE HE2 H 1 6.92 0.01 . 1 . . . . 45 . . . 5101 1 551 . 1 1 47 47 PHE H H 1 9.29 0.01 . 1 . . . . 45 . . . 5101 1 552 . 1 1 47 47 PHE HZ H 1 6.87 0.01 . 1 . . . . 45 . . . 5101 1 553 . 1 1 47 47 PHE N N 15 125.99 0.05 . 1 . . . . 45 . . . 5101 1 554 . 1 1 48 48 ALA CA C 13 50.30 0.05 . 1 . . . . 46 . . . 5101 1 555 . 1 1 48 48 ALA CB C 13 22.09 0.05 . 1 . . . . 46 . . . 5101 1 556 . 1 1 48 48 ALA HA H 1 4.87 0.01 . 1 . . . . 46 . . . 5101 1 557 . 1 1 48 48 ALA HB1 H 1 1.30 0.01 . 1 . . . . 46 . . . 5101 1 558 . 1 1 48 48 ALA HB2 H 1 1.30 0.01 . 1 . . . . 46 . . . 5101 1 559 . 1 1 48 48 ALA HB3 H 1 1.30 0.01 . 1 . . . . 46 . . . 5101 1 560 . 1 1 48 48 ALA H H 1 9.19 0.01 . 1 . . . . 46 . . . 5101 1 561 . 1 1 48 48 ALA N N 15 125.08 0.05 . 1 . . . . 46 . . . 5101 1 562 . 1 1 49 49 GLY CA C 13 45.04 0.05 . 1 . . . . 47 . . . 5101 1 563 . 1 1 49 49 GLY HA2 H 1 4.59 0.01 . 2 . . . . 47 . . . 5101 1 564 . 1 1 49 49 GLY HA3 H 1 3.45 0.01 . 2 . . . . 47 . . . 5101 1 565 . 1 1 49 49 GLY H H 1 8.69 0.01 . 1 . . . . 47 . . . 5101 1 566 . 1 1 49 49 GLY N N 15 108.53 0.05 . 1 . . . . 47 . . . 5101 1 567 . 1 1 50 50 LYS CA C 13 56.01 0.05 . 1 . . . . 48 . . . 5101 1 568 . 1 1 50 50 LYS CB C 13 33.56 0.05 . 1 . . . . 48 . . . 5101 1 569 . 1 1 50 50 LYS CD C 13 29.42 0.05 . 1 . . . . 48 . . . 5101 1 570 . 1 1 50 50 LYS CG C 13 24.73 0.05 . 1 . . . . 48 . . . 5101 1 571 . 1 1 50 50 LYS HA H 1 4.27 0.01 . 1 . . . . 48 . . . 5101 1 572 . 1 1 50 50 LYS HB2 H 1 1.60 0.01 . 2 . . . . 48 . . . 5101 1 573 . 1 1 50 50 LYS HB3 H 1 1.73 0.01 . 2 . . . . 48 . . . 5101 1 574 . 1 1 50 50 LYS HD2 H 1 1.63 0.01 . 1 . . . . 48 . . . 5101 1 575 . 1 1 50 50 LYS HD3 H 1 1.63 0.01 . 1 . . . . 48 . . . 5101 1 576 . 1 1 50 50 LYS HE2 H 1 2.92 0.01 . 1 . . . . 48 . . . 5101 1 577 . 1 1 50 50 LYS HE3 H 1 2.92 0.01 . 1 . . . . 48 . . . 5101 1 578 . 1 1 50 50 LYS HG2 H 1 1.31 0.01 . 1 . . . . 48 . . . 5101 1 579 . 1 1 50 50 LYS HG3 H 1 1.31 0.01 . 1 . . . . 48 . . . 5101 1 580 . 1 1 50 50 LYS H H 1 8.43 0.01 . 1 . . . . 48 . . . 5101 1 581 . 1 1 50 50 LYS N N 15 122.94 0.05 . 1 . . . . 48 . . . 5101 1 582 . 1 1 51 51 GLN CA C 13 55.97 0.05 . 1 . . . . 49 . . . 5101 1 583 . 1 1 51 51 GLN CB C 13 29.47 0.05 . 1 . . . . 49 . . . 5101 1 584 . 1 1 51 51 GLN CG C 13 33.81 0.05 . 1 . . . . 49 . . . 5101 1 585 . 1 1 51 51 GLN HA H 1 4.22 0.01 . 1 . . . . 49 . . . 5101 1 586 . 1 1 51 51 GLN HB2 H 1 2.04 0.01 . 2 . . . . 49 . . . 5101 1 587 . 1 1 51 51 GLN HB3 H 1 1.92 0.01 . 2 . . . . 49 . . . 5101 1 588 . 1 1 51 51 GLN HG2 H 1 2.33 0.01 . 1 . . . . 49 . . . 5101 1 589 . 1 1 51 51 GLN HG3 H 1 2.33 0.01 . 1 . . . . 49 . . . 5101 1 590 . 1 1 51 51 GLN H H 1 8.51 0.01 . 1 . . . . 49 . . . 5101 1 591 . 1 1 51 51 GLN N N 15 121.27 0.05 . 1 . . . . 49 . . . 5101 1 592 . 1 1 52 52 LEU CA C 13 55.33 0.05 . 1 . . . . 50 . . . 5101 1 593 . 1 1 52 52 LEU CB C 13 42.18 0.05 . 1 . . . . 50 . . . 5101 1 594 . 1 1 52 52 LEU CD1 C 13 24.00 0.05 . 2 . . . . 50 . . . 5101 1 595 . 1 1 52 52 LEU CD2 C 13 24.73 0.05 . 2 . . . . 50 . . . 5101 1 596 . 1 1 52 52 LEU HA H 1 4.28 0.01 . 1 . . . . 50 . . . 5101 1 597 . 1 1 52 52 LEU HB2 H 1 1.57 0.01 . 1 . . . . 50 . . . 5101 1 598 . 1 1 52 52 LEU HB3 H 1 1.57 0.01 . 1 . . . . 50 . . . 5101 1 599 . 1 1 52 52 LEU HD11 H 1 0.79 0.01 . 2 . . . . 50 . . . 5101 1 600 . 1 1 52 52 LEU HD12 H 1 0.79 0.01 . 2 . . . . 50 . . . 5101 1 601 . 1 1 52 52 LEU HD13 H 1 0.79 0.01 . 2 . . . . 50 . . . 5101 1 602 . 1 1 52 52 LEU HD21 H 1 0.81 0.01 . 2 . . . . 50 . . . 5101 1 603 . 1 1 52 52 LEU HD22 H 1 0.81 0.01 . 2 . . . . 50 . . . 5101 1 604 . 1 1 52 52 LEU HD23 H 1 0.81 0.01 . 2 . . . . 50 . . . 5101 1 605 . 1 1 52 52 LEU H H 1 8.27 0.01 . 1 . . . . 50 . . . 5101 1 606 . 1 1 52 52 LEU N N 15 124.03 0.05 . 1 . . . . 50 . . . 5101 1 607 . 1 1 53 53 GLU CA C 13 57.97 0.05 . 1 . . . . 51 . . . 5101 1 608 . 1 1 53 53 GLU CG C 13 36.99 0.05 . 1 . . . . 51 . . . 5101 1 609 . 1 1 53 53 GLU HA H 1 4.06 0.01 . 1 . . . . 51 . . . 5101 1 610 . 1 1 53 53 GLU HG2 H 1 2.14 0.01 . 1 . . . . 51 . . . 5101 1 611 . 1 1 53 53 GLU HG3 H 1 2.14 0.01 . 1 . . . . 51 . . . 5101 1 612 . 1 1 53 53 GLU H H 1 7.87 0.01 . 1 . . . . 51 . . . 5101 1 613 . 1 1 53 53 GLU N N 15 126.04 0.05 . 1 . . . . 51 . . . 5101 1 stop_ save_