data_5387 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5387 _Entry.Title ; Complete 1H, 13C, and 15N chemical shifts for human recombinant ubiquitin in reverse micelles ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-06-04 _Entry.Accession_date 2002-06-06 _Entry.Last_release_date . _Entry.Original_release_date . _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 ; This is the first protein for which complete resonance assignment is available in reverse micelles. ; _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 Charles Babu . R. . 5387 2 Peter Flynn . F. . 5387 3 'A. Joshua' Wand . . . 5387 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5387 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 576 5387 '13C chemical shifts' 340 5387 '15N chemical shifts' 82 5387 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 3 . . 2009-10-12 2002-06-04 update author 'update entry citation' 5387 2 . . 2006-05-15 2002-06-04 update author 'added the related entry 7111' 5387 1 . . 2003-06-12 2002-06-04 original author 'original release' 5387 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4245 'Relaxation data of ubiquitin' 5387 BMRB 7111 'Solid-state NMR data' 5387 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5387 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11456950 _Citation.Full_citation . _Citation.Title 'Validation of protein structure from preparations of encapsulated proteins dissolved in low viscosity fluids' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Am. Chem. Soc.' _Citation.Journal_name_full . _Citation.Journal_volume 123 _Citation.Journal_issue 11 _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 2691 _Citation.Page_last 2692 _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 Charles Babu . R. . 5387 1 2 Peter Flynn . F. . 5387 1 3 A. Wand . Joshua . 5387 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID ubiquitin 5387 1 'reverse micelle' 5387 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_ubq _Assembly.Sf_category assembly _Assembly.Sf_framecode system_ubq _Assembly.Entry_ID 5387 _Assembly.ID 1 _Assembly.Name ubiquitin _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 monomer 5387 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 ubiquitin 1 $ubq . . . native . . . . . 5387 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1G6J . . . . . none 5387 1 yes PDB 1UBQ . . . . . none 5387 1 yes PDB 1D3Z . . . . . none 5387 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID ubiquitin system 5387 1 ubq abbreviation 5387 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_ubq _Entity.Sf_category entity _Entity.Sf_framecode ubq _Entity.Entry_ID 5387 _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 ; MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG ; _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 76 _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 8565 _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 . . . . . 100.00 76 98.68 98.68 2.41e-45 . . . . 5387 1 2 no BMRB 11547 . ubiquitin . . . . . 100.00 76 98.68 98.68 2.41e-45 . . . . 5387 1 3 no BMRB 15047 . denatured_ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 4 no BMRB 15410 . Ubi . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 5 no BMRB 15689 . UBB . . . . . 98.68 103 98.67 100.00 4.23e-44 . . . . 5387 1 6 no BMRB 15866 . ubiquitin . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 5387 1 7 no BMRB 15907 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 8 no BMRB 16228 . ubiquitin . . . . . 100.00 76 97.37 98.68 1.18e-44 . . . . 5387 1 9 no BMRB 16582 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 10 no BMRB 16626 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 11 no BMRB 16763 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 12 no BMRB 16880 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 13 no BMRB 16885 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 14 no BMRB 16895 . UBB+1 . . . . . 98.68 103 98.67 100.00 4.23e-44 . . . . 5387 1 15 no BMRB 17059 . ubiquitin . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 5387 1 16 no BMRB 17181 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 17 no BMRB 17239 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 18 no BMRB 17333 . UB . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 19 no BMRB 17439 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 20 no BMRB 17769 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 21 no BMRB 17919 . entity . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 22 no BMRB 18582 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 23 no BMRB 18583 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 24 no BMRB 18584 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 25 no BMRB 18610 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 26 no BMRB 18611 . Ubiquitin_A_state . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 27 no BMRB 18737 . UBIQUITIN . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 28 no BMRB 19394 . ubiquitin . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 5387 1 29 no BMRB 19399 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 30 no BMRB 19406 . entity . . . . . 100.00 152 100.00 100.00 4.37e-45 . . . . 5387 1 31 no BMRB 19412 . entity . . . . . 100.00 152 100.00 100.00 4.37e-45 . . . . 5387 1 32 no BMRB 19447 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 33 no BMRB 25070 . Ubiquitin . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 5387 1 34 no BMRB 25230 . Ubiquitin . . . . . 100.00 78 100.00 100.00 3.66e-46 . . . . 5387 1 35 no BMRB 4245 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 36 no BMRB 4375 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 37 no BMRB 4983 . Ubiquitin . . . . . 98.68 76 97.33 100.00 3.66e-44 . . . . 5387 1 38 no BMRB 5101 . uq1_51 . . . . . 67.11 53 100.00 100.00 2.13e-26 . . . . 5387 1 39 no BMRB 6457 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 40 no BMRB 6466 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 41 no BMRB 6470 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 42 no BMRB 6488 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 43 no BMRB 68 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 44 no BMRB 7111 . human_ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 45 no PDB 1AAR . "Structure Of A Diubiquitin Conjugate And A Model For Interaction With Ubiquitin Conjugating Enzyme (E2)" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 46 no PDB 1CMX . "Structural Basis For The Specificity Of Ubiquitin C- Terminal Hydrolases" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 5387 1 47 no PDB 1D3Z . "Ubiquitin Nmr Structure" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 48 no PDB 1F9J . "Structure Of A New Crystal Form Of Tetraubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 49 no PDB 1FXT . "Structure Of A Conjugating Enzyme-Ubiquitin Thiolester Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 50 no PDB 1G6J . "Structure Of Recombinant Human Ubiquitin In Aot Reverse Micelles" . . . . . 98.68 76 100.00 100.00 5.16e-45 . . . . 5387 1 51 no PDB 1GJZ . "Solution Structure Of A Dimeric N-Terminal Fragment Of Human Ubiquitin" . . . . . 67.11 53 100.00 100.00 2.13e-26 . . . . 5387 1 52 no PDB 1NBF . "Crystal Structure Of A Ubp-Family Deubiquitinating Enzyme In Isolation And In Complex With Ubiquitin Aldehyde" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 5387 1 53 no PDB 1OGW . "Synthetic Ubiquitin With Fluoro-Leu At 50 And 67" . . . . . 100.00 76 97.37 97.37 1.80e-44 . . . . 5387 1 54 no PDB 1P3Q . "Mechanism Of Ubiquitin Recognition By The Cue Domain Of Vps9" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 55 no PDB 1Q5W . "Ubiquitin Recognition By Npl4 Zinc-Fingers" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 56 no PDB 1S1Q . "Tsg101(Uev) Domain In Complex With Ubiquitin" . . . . . 98.68 76 100.00 100.00 5.16e-45 . . . . 5387 1 57 no PDB 1TBE . "Structure Of Tetraubiquitin Shows How Multiubiquitin Chains Can Be Formed" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 58 no PDB 1UBI . "Synthetic Structural And Biological Studies Of The Ubiquitin System. Part 1" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 59 no PDB 1UBQ . "Structure Of Ubiquitin Refined At 1.8 Angstroms Resolution" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 60 no PDB 1UZX . "A Complex Of The Vps23 Uev With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 61 no PDB 1V80 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 62 no PDB 1V81 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 63 no PDB 1VX7 . "Cryo-em Structure Of The Plasmodium Falciparum 80s Ribosome Bound To The Anti-protozoan Drug Emetine, Large Subunit (protein On" . . . . . 100.00 128 98.68 100.00 9.37e-46 . . . . 5387 1 64 no PDB 1WR6 . "Crystal Structure Of Gga3 Gat Domain In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 65 no PDB 1WRD . "Crystal Structure Of Tom1 Gat Domain In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 66 no PDB 1XD3 . "Crystal Structure Of Uchl3-Ubvme Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 67 no PDB 1XQQ . "Simultaneous Determination Of Protein Structure And Dynamics" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 68 no PDB 1YD8 . "Complex Of Human Gga3 Gat Domain And Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 69 no PDB 1YIW . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin" . . . . . 100.00 76 98.68 100.00 1.94e-45 . . . . 5387 1 70 no PDB 1YJ1 . "X-Ray Crystal Structure Of A Chemically Synthesized [d-Gln35]ubiquitin" . . . . . 100.00 76 97.37 98.68 2.29e-44 . . . . 5387 1 71 no PDB 1YX5 . "Solution Structure Of S5a Uim-1UBIQUITIN COMPLEX" . . . . . 100.00 98 100.00 100.00 1.57e-46 . . . . 5387 1 72 no PDB 1YX6 . "Solution Structure Of S5a Uim-2UBIQUITIN COMPLEX" . . . . . 100.00 98 100.00 100.00 1.57e-46 . . . . 5387 1 73 no PDB 1ZGU . "Solution Structure Of The Human Mms2-Ubiquitin Complex" . . . . . 100.00 76 98.68 100.00 1.06e-45 . . . . 5387 1 74 no PDB 2AYO . "Structure Of Usp14 Bound To Ubquitin Aldehyde" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 5387 1 75 no PDB 2BGF . "Nmr Structure Of Lys48-Linked Di-Ubiquitin Using Chemical Shift Perturbation Data Together With Rdcs And 15n- Relaxation Data" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 76 no PDB 2C7M . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 77 no PDB 2C7N . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 78 no PDB 2D3G . "Double Sided Ubiquitin Binding Of Hrs-Uim" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 79 no PDB 2DEN . "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 80 no PDB 2DX5 . "The Complex Structure Between The Mouse Eap45-Glue Domain And Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 81 no PDB 2FCM . "X-Ray Crystal Structure Of A Chemically Synthesized [d-Gln35]ubiquitin With A Cubic Space Group" . . . . . 100.00 76 97.37 98.68 2.29e-44 . . . . 5387 1 82 no PDB 2FCN . "X-Ray Crystal Structure Of A Chemically Synthesized [d-Val35]ubiquitin With A Cubic Space Group" . . . . . 100.00 76 97.37 98.68 2.29e-44 . . . . 5387 1 83 no PDB 2FCQ . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin With A Cubic Space Group" . . . . . 100.00 76 98.68 100.00 1.94e-45 . . . . 5387 1 84 no PDB 2FCS . "X-Ray Crystal Structure Of A Chemically Synthesized [l-Gln35]ubiquitin With A Cubic Space Group" . . . . . 100.00 76 97.37 98.68 2.61e-44 . . . . 5387 1 85 no PDB 2FID . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 86 no PDB 2FIF . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 87 no PDB 2FUH . "Solution Structure Of The Ubch5cUB NON-Covalent Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 88 no PDB 2G45 . "Co-Crystal Structure Of Znf Ubp Domain From The Deubiquitinating Enzyme Isopeptidase T (Isot) In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 89 no PDB 2GMI . Mms2UBC13~UBIQUITIN . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 90 no PDB 2HD5 . "Usp2 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 91 no PDB 2HTH . "Structural Basis For Ubiquitin Recognition By The Human Eap45ESCRT-Ii Glue Domain" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 92 no PDB 2IBI . "Covalent Ubiquitin-Usp2 Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 93 no PDB 2J7Q . "Crystal Structure Of The Ubiquitin-Specific Protease Encoded By Murine Cytomegalovirus Tegument Protein M48 In Complex With A U" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 94 no PDB 2JF5 . "Crystal Structure Of Lys63-Linked Di-Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 95 no PDB 2JRI . "Solution Structure Of The Josephin Domain Of Ataxin-3 In Complex With Ubiquitin Molecule." . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 96 no PDB 2JY6 . "Solution Structure Of The Complex Of Ubiquitin And Ubiquilin 1 Uba Domain" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 97 no PDB 2JZZ . "Solid-State Nmr Structure Of Microcrystalline Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 98 no PDB 2K25 . "Automated Nmr Structure Of The Ubb By Fapsy" . . . . . 98.68 103 98.67 100.00 4.23e-44 . . . . 5387 1 99 no PDB 2K39 . "Recognition Dynamics Up To Microseconds Revealed From Rdc Derived Ubiquitin Ensemble In Solution" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 100 no PDB 2K6D . "Cin85 Sh3-C Domain In Complex With Ubiquitin" . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 5387 1 101 no PDB 2K8B . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Cis Isomer In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 102 no PDB 2K8C . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Trans Isomer In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 103 no PDB 2KDE . "Nmr Structure Of Major S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 104 no PDB 2KDF . "Nmr Structure Of Minor S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 105 no PDB 2KHW . "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 5387 1 106 no PDB 2KJH . "Nmr Based Structural Model Of The Ubch8-Ubiquitin Complex" . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 5387 1 107 no PDB 2KLG . "Pere Nmr Structure Of Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 108 no PDB 2KN5 . "A Correspondence Between Solution-State Dynamics Of An Individual Protein And The Sequence And Conformational Diversity Of Its " . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 109 no PDB 2KOX . "Nmr Residual Dipolar Couplings Identify Long Range Correlated Motions In The Backbone Of The Protein Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 110 no PDB 2KTF . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 111 no PDB 2KWU . "Solution Structure Of Ubm2 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 112 no PDB 2KWV . "Solution Structure Of Ubm1 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 113 no PDB 2KX0 . "The Solution Structure Of Ubb+1, Frameshift Mutant Of Ubiquitin B" . . . . . 98.68 103 98.67 100.00 4.23e-44 . . . . 5387 1 114 no PDB 2L0F . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 (P692a Mutant) In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 115 no PDB 2L0T . "Solution Structure Of The Complex Of Ubiquitin And The Vhs Domain Of Stam2" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 116 no PDB 2L3Z . "Proton-Detected 4d Dream Solid-State Nmr Structure Of Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 117 no PDB 2LD9 . "Backbone Structure Of Ubiquitin Determined Using Backbone Amide Noes And Backbone N-H And N-C Rdcs" . . . . . 100.00 77 100.00 100.00 5.39e-46 . . . . 5387 1 118 no PDB 2LJ5 . "Description Of The Structural Fluctuations Of Proteins From Structure- Based Calculations Of Residual Dipolar Couplings" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 119 no PDB 2LVO . "Structure Of The Gp78cue Domain Bound To Monubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 120 no PDB 2LVP . "Gp78cue Domain Bound To The Distal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 121 no PDB 2LVQ . "Gp78cue Domain Bound To The Proximal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 122 no PDB 2LZ6 . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 123 no PDB 2MBB . "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" . . . . . 100.00 78 100.00 100.00 3.66e-46 . . . . 5387 1 124 no PDB 2MBH . "Nmr Structure Of Eklf(22-40)/ubiquitin Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 125 no PDB 2MBO . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 0 Mm Nacl" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 126 no PDB 2MBQ . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 150 Mm Nacl" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 127 no PDB 2MCN . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 128 no PDB 2MJ5 . "Structure Of The Uba Domain Of Human Nbr1 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 129 no PDB 2MJB . "Solution Nmr Structure Of Ubiquitin Refined Against Dipolar Couplings In 4 Media" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 130 no PDB 2MOR . "A Tensor-free Method For The Structural And Dynamical Refinement Of Proteins Using Residual Dipolar Couplings" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 131 no PDB 2MRE . "Nmr Structure Of The Rad18-ubz/ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 5387 1 132 no PDB 2MUR . "Solution Structure Of The Human Faap20 Ubz-ubiquitin Complex" . . . . . 100.00 78 100.00 100.00 3.66e-46 . . . . 5387 1 133 no PDB 2NR2 . "The Mumo (Minimal Under-Restraining Minimal Over- Restraining) Method For The Determination Of Native States Ensembles Of Prote" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 134 no PDB 2O6V . "Crystal Structure And Solution Nmr Studies Of Lys48-Linked Tetraubiquitin At Neutral Ph" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 135 no PDB 2OJR . "Structure Of Ubiquitin Solved By Sad Using The Lanthanide- Binding Tag" . . . . . 100.00 111 100.00 100.00 1.56e-45 . . . . 5387 1 136 no PDB 2OOB . "Crystal Structure Of The Uba Domain From Cbl-B Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 137 no PDB 2PE9 . "Nmr Based Structure Of The Open Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Tenso" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 138 no PDB 2PEA . "Nmr Based Structure Of The Closed Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Ten" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 139 no PDB 2QHO . "Crystal Structure Of The Uba Domain From Edd Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 140 no PDB 2RR9 . "The Solution Structure Of The K63-Ub2:tuims Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 141 no PDB 2RSU . "Alternative Structure Of Ubiquitin" . . . . . 100.00 76 98.68 98.68 2.41e-45 . . . . 5387 1 142 no PDB 2RU6 . "The Pure Alternative State Of Ubiquitin" . . . . . 100.00 76 98.68 98.68 2.41e-45 . . . . 5387 1 143 no PDB 2W9N . "Crystal Structure Of Linear Di-Ubiquitin" . . . . . 98.68 152 100.00 100.00 3.82e-44 . . . . 5387 1 144 no PDB 2WDT . "Crystal Structure Of Plasmodium Falciparum Uchl3 In Complex With The Suicide Inhibitor Ubvme" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 5387 1 145 no PDB 2WWZ . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P212121" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 146 no PDB 2WX0 . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P21" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 147 no PDB 2WX1 . "Tab2 Nzf Domain In Complex With Lys63-Linked Tri-Ubiquitin, P212121" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 148 no PDB 2XBB . "Nedd4 Hect:ub Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 149 no PDB 2XEW . "Crystal Structure Of K11-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 150 no PDB 2XK5 . "Crystal Structure Of K6-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 151 no PDB 2Y5B . "Structure Of Usp21 In Complex With Linear Diubiquitin-Aldehyde" . . . . . 98.68 152 100.00 100.00 2.82e-44 . . . . 5387 1 152 no PDB 2Z59 . "Complex Structures Of Mouse Rpn13 (22-130aa) And Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 153 no PDB 2ZCB . "Crystal Structure Of Ubiquitin P37aP38A" . . . . . 100.00 76 97.37 97.37 2.34e-44 . . . . 5387 1 154 no PDB 2ZCC . "Ubiquitin Crystallized Under High Pressure" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 155 no PDB 2ZNV . "Crystal Structure Of Human Amsh-Lp Dub Domain In Complex With Lys63-Linked Ubiquitin Dimer" . . . . . 100.00 77 100.00 100.00 5.05e-46 . . . . 5387 1 156 no PDB 2ZVN . "Nemo Cozi Domain Incomplex With Diubiquitin In P212121 Space Group" . . . . . 100.00 154 100.00 100.00 4.07e-45 . . . . 5387 1 157 no PDB 2ZVO . "Nemo Cozi Domain In Complex With Diubiquitin In C2 Space Group" . . . . . 100.00 154 100.00 100.00 4.07e-45 . . . . 5387 1 158 no PDB 3A1Q . "Crystal Structure Of The Mouse Rap80 Uims In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 100.00 77 100.00 100.00 5.05e-46 . . . . 5387 1 159 no PDB 3A33 . "Ubch5b~ubiquitin Conjugate" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 160 no PDB 3A9J . "Crystal Structure Of The Mouse Tab2-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 100.00 77 100.00 100.00 5.05e-46 . . . . 5387 1 161 no PDB 3A9K . "Crystal Structure Of The Mouse Tab3-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 100.00 77 100.00 100.00 5.05e-46 . . . . 5387 1 162 no PDB 3AI5 . "Crystal Structure Of Yeast Enhanced Green Fluorescent Protein- Ubiquitin Fusion Protein" . . . . . 97.37 307 100.00 100.00 1.12e-41 . . . . 5387 1 163 no PDB 3ALB . "Cyclic Lys48-Linked Tetraubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 164 no PDB 3AUL . "Crystal Structure Of Wild-Type Lys48-Linked Diubiquitin In An Open Conformation" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 165 no PDB 3AXC . "Crystal Structure Of Linear Diubiquitin" . . . . . 100.00 154 100.00 100.00 4.07e-45 . . . . 5387 1 166 no PDB 3B08 . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 100.00 152 100.00 100.00 4.37e-45 . . . . 5387 1 167 no PDB 3B0A . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 100.00 152 100.00 100.00 4.37e-45 . . . . 5387 1 168 no PDB 3BY4 . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 169 no PDB 3C0R . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 170 no PDB 3DVG . "Crystal Structure Of K63-Specific Fab Apu.3a8 Bound To K63-Linked Di- Ubiquitin" . . . . . 100.00 80 100.00 100.00 5.61e-46 . . . . 5387 1 171 no PDB 3DVN . "Crystal Structure Of K63-specific Fab Apu2.16 Bound To K63-linked Di- Ubiquitin" . . . . . 100.00 80 100.00 100.00 5.61e-46 . . . . 5387 1 172 no PDB 3EEC . "X-Ray Structure Of Human Ubiquitin Cd(Ii) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 173 no PDB 3EFU . "X-Ray Structure Of Human Ubiquitin-Hg(Ii) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 174 no PDB 3EHV . "X-Ray Structure Of Human Ubiquitin Zn(Ii) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 175 no PDB 3H1U . "Structure Of Ubiquitin In Complex With Cd Ions" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 176 no PDB 3H7P . "Crystal Structure Of K63-Linked Di-Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 177 no PDB 3H7S . "Crystal Structures Of K63-Linked Di- And Tri-Ubiquitin Reveal A Highly Extended Chain Architecture" . . . . . 100.00 76 98.68 98.68 1.91e-43 . . . . 5387 1 178 no PDB 3HM3 . "The Structure And Conformation Of Lys-63 Linked Tetra-Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 179 no PDB 3I3T . "Crystal Structure Of Covalent Ubiquitin-usp21 Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 180 no PDB 3IFW . "Crystal Structure Of The S18y Variant Of Ubiquitin Carboxy T Hydrolase L1 Bound To Ubiquitin Vinylmethylester." . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 181 no PDB 3IHP . "Covalent Ubiquitin-Usp5 Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 182 no PDB 3JSV . "Crystal Structure Of Mouse Nemo Cozi In Complex With Lys63- Linked Di-Ubiquitin" . . . . . 100.00 77 100.00 100.00 5.05e-46 . . . . 5387 1 183 no PDB 3JVZ . E2~ubiquitin-Hect . . . . . 100.00 81 100.00 100.00 5.23e-46 . . . . 5387 1 184 no PDB 3JW0 . E2~ubiquitin-Hect . . . . . 100.00 81 100.00 100.00 5.23e-46 . . . . 5387 1 185 no PDB 3K9O . "The Crystal Structure Of E2-25k And Ubb+1 Complex" . . . . . 98.68 96 100.00 100.00 8.68e-45 . . . . 5387 1 186 no PDB 3K9P . "The Crystal Structure Of E2-25k And Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 5387 1 187 no PDB 3KVF . "Crystal Structure Of The I93m Mutant Of Ubiquitin Carboxy Te Hydrolase L1 Bound To Ubiquitin Vinylmethylester" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 188 no PDB 3KW5 . "Crystal Structure Of Ubiquitin Carboxy Terminal Hydrolase L1 Ubiquitin Vinylmethylester" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 189 no PDB 3LDZ . "Crystal Structure Of Human Stam1 Vhs Domain In Complex With Ubiquitin" . . . . . 96.05 73 100.00 100.00 1.22e-43 . . . . 5387 1 190 no PDB 3M3J . "A New Crystal Form Of Lys48-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 191 no PDB 3MHS . "Structure Of The Saga Ubp8SGF11SUS1SGF73 DUB MODULE BOUND Ubiquitin Aldehyde" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 5387 1 192 no PDB 3MTN . "Usp21 In Complex With A Ubiquitin-based, Usp21-specific Inhibitor" . . . . . 88.16 85 98.51 98.51 1.00e-37 . . . . 5387 1 193 no PDB 3N30 . "Crystal Structure Of Cubic Zn3-Hub (Human Ubiquitin) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 194 no PDB 3N32 . "The Crystal Structure Of Human Ubiquitin Adduct With Zeise's Salt" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 195 no PDB 3NHE . "High Resolution Structure (1.26a) Of Usp2a In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 196 no PDB 3NOB . "Structure Of K11-linked Di-ubiquitin" . . . . . 100.00 78 100.00 100.00 3.66e-46 . . . . 5387 1 197 no PDB 3NS8 . "Crystal Structure Of An Open Conformation Of Lys48-Linked Diubiquitin At Ph 7.5" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 198 no PDB 3O65 . "Crystal Structure Of A Josephin-Ubiquitin Complex: Evolutionary Restraints On Ataxin-3 Deubiquitinating Activity" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 5387 1 199 no PDB 3OFI . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 200 no PDB 3OJ3 . "Crystal Structure Of The A20 Znf4 And Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 5387 1 201 no PDB 3OJ4 . "Crystal Structure Of The A20 Znf4, Ubiquitin And Ubch5a Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 5387 1 202 no PDB 3ONS . "Crystal Structure Of Human Ubiquitin In A New Crystal Form" . . . . . 94.74 72 100.00 100.00 5.80e-43 . . . . 5387 1 203 no PDB 3PHD . "Crystal Structure Of Human Hdac6 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 204 no PDB 3PHW . "Otu Domain Of Crimean Congo Hemorrhagic Fever Virus In Complex With Ubiquitin" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 205 no PDB 3PRM . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 206 no PDB 3PRP . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 207 no PDB 3PT2 . "Structure Of A Viral Otu Domain Protease Bound To Ubiquitin" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 208 no PDB 3PTF . "X-Ray Structure Of The Non-Covalent Complex Between Ubch5a And Ubiquitin" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 5387 1 209 no PDB 3Q3F . "Engineering Domain-Swapped Binding Interfaces By Mutually Exclusive Folding: Insertion Of Ubiquitin Into Position 103 Of Barnas" . . . . . 98.68 189 100.00 100.00 3.64e-44 . . . . 5387 1 210 no PDB 3RUL . "New Strategy To Analyze Structures Of Glycopeptide-Target Complexes" . . . . . 98.68 79 100.00 100.00 2.70e-45 . . . . 5387 1 211 no PDB 3TBL . "Structure Of Mono-ubiquitinated Pcna: Implications For Dna Polymerase Switching And Okazaki Fragment Maturation" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 212 no PDB 3TMP . "The Catalytic Domain Of Human Deubiquitinase Duba In Complex With Ubiquitin Aldehyde" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 5387 1 213 no PDB 3U30 . "Crystal Structure Of A Linear-Specific Ubiquitin Fab Bound To Linear Ubiquitin" . . . . . 100.00 172 100.00 100.00 4.69e-45 . . . . 5387 1 214 no PDB 3UGB . "Ubch5c~ubiquitin Conjugate" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 215 no PDB 3VDZ . "Tailoring Encodable Lanthanide-Binding Tags As Mri Contrast Agents: Xq-Dse3-Ubiquitin At 2.4 Angstroms" . . . . . 100.00 111 100.00 100.00 9.99e-46 . . . . 5387 1 216 no PDB 3VFK . "The Structure Of Monodechloro-teicoplanin In Complex With Its Ligand, Using Ubiquitin As A Ligand Carrier" . . . . . 98.68 79 100.00 100.00 2.70e-45 . . . . 5387 1 217 no PDB 3VHT . "Crystal Structure Of Gfp-Wrnip1 Ubz Domain Fusion Protein In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 218 no PDB 3VUW . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form I" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 219 no PDB 3VUX . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form Ii" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 220 no PDB 3VUY . "Crystal Structure Of A20 Zf7 In Complex With Linear Tetraubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 221 no PDB 3ZLZ . "Lys6-linked Tri-ubiquitin" . . . . . 100.00 76 98.68 100.00 1.06e-45 . . . . 5387 1 222 no PDB 3ZNH . "Crimean Congo Hemorrhagic Fever Virus Otu Domain In Complex With Ubiquitin-propargyl." . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 5387 1 223 no PDB 3ZNI . "Structure Of Phosphotyr363-cbl-b - Ubch5b-ub - Zap-70 Peptide Complex" . . . . . 100.00 81 100.00 100.00 5.23e-46 . . . . 5387 1 224 no PDB 3ZNZ . "Crystal Structure Of Otulin Otu Domain (c129a) In Complex With Met1-di Ubiquitin" . . . . . 100.00 152 100.00 100.00 4.37e-45 . . . . 5387 1 225 no PDB 4A18 . "T.Thermophila 60s Ribosomal Subunit In Complex With Initiation Factor 6. This File Contains 26s Rrna And Proteins Of Molecule 1" . . . . . 100.00 129 97.37 98.68 1.83e-44 . . . . 5387 1 226 no PDB 4A19 . "T.Thermophila 60s Ribosomal Subunit In Complex With Initiation Factor 6. This File Contains 26s Rrna And Proteins Of Molecule 2" . . . . . 100.00 129 97.37 98.68 1.83e-44 . . . . 5387 1 227 no PDB 4A1B . "T.Thermophila 60s Ribosomal Subunit In Complex With Initiation Factor 6. This File Contains 26s Rrna And Proteins Of Molecule 3" . . . . . 100.00 129 97.37 98.68 1.83e-44 . . . . 5387 1 228 no PDB 4A1D . "T.Thermophila 60s Ribosomal Subunit In Complex With Initiation Factor 6. This File Contains 26s Rrna And Proteins Of Molecule 4" . . . . . 100.00 129 97.37 98.68 1.83e-44 . . . . 5387 1 229 no PDB 4ADX . "The Cryo-em Structure Of The Archaeal 50s Ribosomal Subunit In Complex With Initiation Factor 6" . . . . . 100.00 129 97.37 98.68 1.83e-44 . . . . 5387 1 230 no PDB 4AP4 . "Rnf4 - Ubch5a - Ubiquitin Heterotrimeric Complex" . . . . . 100.00 80 100.00 100.00 4.66e-46 . . . . 5387 1 231 no PDB 4AUQ . "Structure Of Birc7-Ubch5b-Ub Complex." . . . . . 100.00 81 100.00 100.00 5.23e-46 . . . . 5387 1 232 no PDB 4BBN . "Nedd4 Hect-ub:ub Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 233 no PDB 4BOS . "Structure Of Otud2 Otu Domain In Complex With Ubiquitin K11- Linked Peptide" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 234 no PDB 4BOZ . "Structure Of Otud2 Otu Domain In Complex With K11-linked Di Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 235 no PDB 4BVU . "Structure Of Shigella Effector Ospg In Complex With Host Ubch5c-ubiquitin Conjugate" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 236 no PDB 4CXC . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 5387 1 237 no PDB 4CXD . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 238 no PDB 4DDG . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 239 no PDB 4DDI . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 240 no PDB 4DHJ . "The Structure Of A Ceotub1 Ubiquitin Aldehyde Ubc13~ub Complex" . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 5387 1 241 no PDB 4DHZ . "The Structure Of HCEOTUB1-Ubiquitin Aldehyde-Ubc13~ub" . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 5387 1 242 no PDB 4FJV . "Crystal Structure Of Human Otubain2 And Ubiquitin Complex" . . . . . 100.00 86 100.00 100.00 6.71e-46 . . . . 5387 1 243 no PDB 4HXD . "Diversity Of Ubiquitin And Isg15 Specificity Amongst Nairoviruses Viral Ovarian Tumor Domain Proteases" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 244 no PDB 4I6N . "Crystal Structure Of Trichinella Spiralis Uch37 Catalytic Domain Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 97.37 75 100.00 100.00 3.09e-44 . . . . 5387 1 245 no PDB 4IG7 . "Crystal Structure Of Trichinella Spiralis Uch37 Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 246 no PDB 4IUM . "Equine Arteritis Virus Papain-like Protease 2 (plp2) Covalently Bound To Ubiquitin" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 5387 1 247 no PDB 4JIO . "Bro1 V Domain And Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.30e-45 . . . . 5387 1 248 no PDB 4JQW . "Crystal Structure Of A Complex Of Nod1 Card And Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 249 no PDB 4K1R . "Crystal Structure Of Schizosaccharomyces Pombe Sst2 Catalytic Domain And Ubiquitin" . . . . . 100.00 81 100.00 100.00 7.82e-46 . . . . 5387 1 250 no PDB 4K7S . "Crystal Structure Of Zn2-hub (human Ubiquitin) Adduct From A Solution 35 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 251 no PDB 4K7U . "Crystal Structure Of Zn2.3-hub (human Ubiquitin) Adduct From A Solution 70 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 252 no PDB 4K7W . "Crystal Structure Of Zn3-hub(human Ubiquitin) Adduct From A Solution 100 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 253 no PDB 4KSK . "Gumby/fam105b In Complex With Ubiquitin" . . . . . 100.00 80 100.00 100.00 4.66e-46 . . . . 5387 1 254 no PDB 4KSL . "Gumby/fam105b In Complex With Linear Di-ubiquitin" . . . . . 100.00 156 100.00 100.00 4.31e-45 . . . . 5387 1 255 no PDB 4KZX . "Rabbit 40s Ribosomal Subunit In Complex With Eif1." . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 5387 1 256 no PDB 4KZY . "Rabbit 40s Ribosomal Subunit In Complex With Eif1 And Eif1a." . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 5387 1 257 no PDB 4KZZ . "Rabbit 40s Ribosomal Subunit In Complex With Mrna, Initiator Trna And Eif1a" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 5387 1 258 no PDB 4LCD . "Structure Of An Rsp5xubxsna3 Complex: Mechanism Of Ubiquitin Ligation And Lysine Prioritization By A Hect E3" . . . . . 97.37 83 100.00 100.00 1.22e-44 . . . . 5387 1 259 no PDB 4LDT . "The Structure Of H/ceotub1-ubiquitin Aldehyde-ubch5b~ub" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 260 no PDB 4LJO . "Structure Of An Active Ligase (hoip)/ubiquitin Transfer Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 261 no PDB 4LJP . "Structure Of An Active Ligase (hoip-h889a)/ubiquitin Transfer Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 262 no PDB 4M0W . "Crystal Structure Of Sars-cov Papain-like Protease C112s Mutant In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 263 no PDB 4MDK . "Cdc34-ubiquitin-cc0651 Complex" . . . . . 100.00 80 100.00 100.00 4.66e-46 . . . . 5387 1 264 no PDB 4MM3 . "Crystal Structure Of Sars-cov Papain-like Protease Plpro In Complex With Ubiquitin Aldehyde" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 5387 1 265 no PDB 4MSM . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 E286a Mutant Bound To Ubiquitin" . . . . . 100.00 81 100.00 100.00 7.82e-46 . . . . 5387 1 266 no PDB 4MSQ . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 Catalytic Domain Bound To Ubiquitin" . . . . . 100.00 81 100.00 100.00 7.82e-46 . . . . 5387 1 267 no PDB 4NQK . "Structure Of An Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 8.16e-46 . . . . 5387 1 268 no PDB 4NQL . "The Crystal Structure Of The Dub Domain Of Amsh Orthologue, Sst2 From S. Pombe, In Complex With Lysine 63-linked Diubiquitin" . . . . . 100.00 77 100.00 100.00 5.05e-46 . . . . 5387 1 269 no PDB 4P4H . "Caught-in-action Signaling Complex Of Rig-i 2card Domain And Mavs Card Domain" . . . . . 100.00 79 100.00 100.00 8.16e-46 . . . . 5387 1 270 no PDB 4PIG . "Crystal Structure Of The Ubiquitin K11s Mutant" . . . . . 100.00 76 98.68 98.68 1.92e-45 . . . . 5387 1 271 no PDB 4PIH . "X-ray Crystal Structure Of The K33s Mutant Of Ubiquitin" . . . . . 100.00 76 98.68 98.68 1.92e-45 . . . . 5387 1 272 no PDB 4PIJ . "X-ray Crystal Structure Of The K11s/k63s Double Mutant Of Ubiquitin" . . . . . 98.68 75 97.33 97.33 5.38e-44 . . . . 5387 1 273 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 7.82e-46 . . . . 5387 1 274 no PDB 4RF0 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 275 no PDB 4RF1 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 5387 1 276 no PDB 4UN2 . "Crystal Structure Of The Uba Domain Of Dsk2 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 277 no PDB 4UPX . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 278 no PDB 4UQ1 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 279 no PDB 4UQ4 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 5387 1 280 no PDB 4UQ5 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 5387 1 281 no PDB 4W20 . "Structure Of The Mammalian 60s Ribosomal Subunit (this Entry Contains The Large Ribosomal Proteins)" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 282 no PDB 4W22 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 283 no PDB 4W23 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Small Ribosomal Subunit)" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 5387 1 284 no PDB 4W25 . "Structure Of The Idle Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 285 no PDB 4W27 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 286 no PDB 4W28 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Small Ribosomal Subunit)" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 5387 1 287 no PDB 4WUR . "The Crystal Structure Of The Mers-cov Papain-like Protease (c111s) With Human Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 288 no PDB 4WZP . "Ser65 Phosphorylated Ubiquitin, Major Conformation" . . . . . 100.00 76 98.68 98.68 3.16e-45 . . . . 5387 1 289 no DBJ BAA03983 . "polyubiquitin [Rattus norvegicus]" . . . . . 100.00 305 100.00 100.00 2.21e-43 . . . . 5387 1 290 no DBJ BAA09860 . "polyubiquitin [Homo sapiens]" . . . . . 100.00 611 98.68 98.68 1.04e-40 . . . . 5387 1 291 no DBJ BAA11842 . "ubiquitin [Cavia porcellus]" . . . . . 100.00 311 100.00 100.00 2.40e-43 . . . . 5387 1 292 no DBJ BAA11843 . "ubiquitin extention protein [Cavia porcellus]" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 5387 1 293 no DBJ BAA23486 . "polyubiquitin [Homo sapiens]" . . . . . 100.00 609 98.68 98.68 5.60e-41 . . . . 5387 1 294 no EMBL CAA25706 . "unnamed protein product [Saccharomyces cerevisiae]" . . . . . 50.00 191 100.00 100.00 2.98e-16 . . . . 5387 1 295 no EMBL CAA26488 . "unnamed protein product [Gallus gallus]" . . . . . 100.00 157 98.68 98.68 2.66e-44 . . . . 5387 1 296 no EMBL CAA28495 . "ubiquitin [Homo sapiens]" . . . . . 100.00 229 100.00 100.00 3.53e-44 . . . . 5387 1 297 no EMBL CAA30183 . "unnamed protein product [Dictyostelium discoideum]" . . . . . 100.00 128 97.37 97.37 5.38e-44 . . . . 5387 1 298 no EMBL CAA30815 . "unnamed protein product [Cricetulus sp.]" . . . . . 93.42 223 100.00 100.00 3.70e-40 . . . . 5387 1 299 no GB AAA02769 . "polyprotein [Bovine viral diarrhea virus 1-Osloss]" . . . . . 98.68 3975 97.33 100.00 1.83e-39 . . . . 5387 1 300 no GB AAA28154 . "polyubiquitin [Caenorhabditis elegans]" . . . . . 100.00 838 97.37 98.68 7.19e-40 . . . . 5387 1 301 no GB AAA28997 . "ubiquitin [Drosophila melanogaster]" . . . . . 100.00 231 100.00 100.00 3.30e-44 . . . . 5387 1 302 no GB AAA28998 . "ubiquitin-hybrid protein precursor [Drosophila melanogaster]" . . . . . 100.00 156 100.00 100.00 9.66e-46 . . . . 5387 1 303 no GB AAA28999 . "ubiquitin, partial [Drosophila melanogaster]" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 304 no PIR I50437 . "polyubiquitin 4 - chicken [Gallus gallus]" . . . . . 100.00 305 100.00 100.00 2.21e-43 . . . . 5387 1 305 no PIR I51568 . "polyubiquitin - African clawed frog (fragment)" . . . . . 100.00 167 100.00 100.00 6.83e-45 . . . . 5387 1 306 no PIR I65237 . "ubiquitin / ribosomal protein L40, cytosolic [validated] - rat" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 307 no PIR JN0790 . "ubiquitin/ribosomal protein CEP52 fusion protein - Leishmania major" . . . . . 100.00 128 97.37 98.68 2.33e-45 . . . . 5387 1 308 no PIR S13928 . "ubiquitin precursor - chicken [Gallus gallus]" . . . . . 100.00 229 100.00 100.00 3.64e-44 . . . . 5387 1 309 no PRF 0412265A . ubiquitin . . . . . 98.68 75 98.67 98.67 1.22e-44 . . . . 5387 1 310 no PRF 1101405A . "ubiquitin precursor" . . . . . 50.00 191 100.00 100.00 2.95e-16 . . . . 5387 1 311 no PRF 1212243A . "ubiquitin S1" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 312 no PRF 1212243B . "ubiquitin S5" . . . . . 92.11 77 98.57 98.57 7.61e-41 . . . . 5387 1 313 no PRF 1212243C . "ubiquitin S3" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 5387 1 314 no REF NP_001005123 . "ubiquitin A-52 residue ribosomal protein fusion product 1 [Xenopus (Silurana) tropicalis]" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 315 no REF NP_001006688 . "ubiquitin C [Xenopus (Silurana) tropicalis]" . . . . . 100.00 609 100.00 100.00 9.87e-42 . . . . 5387 1 316 no REF NP_001009117 . "polyubiquitin-B [Pan troglodytes]" . . . . . 100.00 229 100.00 100.00 3.53e-44 . . . . 5387 1 317 no REF NP_001009202 . "polyubiquitin-B [Ovis aries]" . . . . . 100.00 305 98.68 100.00 3.89e-43 . . . . 5387 1 318 no REF NP_001009286 . "ubiquitin-60S ribosomal protein L40 [Ovis aries]" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 319 no SP P0C273 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 320 no SP P0C275 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 321 no SP P0C276 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 322 no SP P0CG47 . "RecName: Full=Polyubiquitin-B; Contains: RecName: Full=Ubiquitin; Flags: Precursor [Homo sapiens]" . . . . . 100.00 229 100.00 100.00 3.53e-44 . . . . 5387 1 323 no SP P0CG48 . "RecName: Full=Polyubiquitin-C; Contains: RecName: Full=Ubiquitin; Flags: Precursor [Homo sapiens]" . . . . . 100.00 685 100.00 100.00 1.45e-41 . . . . 5387 1 324 no TPD FAA00319 . "TPA: polyubiquitin [Cryptococcus neoformans var. neoformans B-3501A]" . . . . . 100.00 456 97.37 98.68 7.53e-41 . . . . 5387 1 325 no TPG DAA18802 . "TPA: polyubiquitin [Bos taurus]" . . . . . 100.00 305 100.00 100.00 2.33e-43 . . . . 5387 1 326 no TPG DAA20663 . "TPA: ubiquitin C [Bos taurus]" . . . . . 98.68 314 98.67 100.00 8.85e-42 . . . . 5387 1 327 no TPG DAA20672 . "TPA: ubiquitin B-like [Bos taurus]" . . . . . 100.00 77 98.68 98.68 3.32e-45 . . . . 5387 1 328 no TPG DAA24675 . "TPA: 40S ribosomal protein S27a [Bos taurus]" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 5387 1 329 no TPG DAA28295 . "TPA: ubiquitin and ribosomal protein L40 [Bos taurus]" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 5387 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID ubiquitin common 5387 1 ubq abbreviation 5387 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . MET . 5387 1 2 . GLN . 5387 1 3 . ILE . 5387 1 4 . PHE . 5387 1 5 . VAL . 5387 1 6 . LYS . 5387 1 7 . THR . 5387 1 8 . LEU . 5387 1 9 . THR . 5387 1 10 . GLY . 5387 1 11 . LYS . 5387 1 12 . THR . 5387 1 13 . ILE . 5387 1 14 . THR . 5387 1 15 . LEU . 5387 1 16 . GLU . 5387 1 17 . VAL . 5387 1 18 . GLU . 5387 1 19 . PRO . 5387 1 20 . SER . 5387 1 21 . ASP . 5387 1 22 . THR . 5387 1 23 . ILE . 5387 1 24 . GLU . 5387 1 25 . ASN . 5387 1 26 . VAL . 5387 1 27 . LYS . 5387 1 28 . ALA . 5387 1 29 . LYS . 5387 1 30 . ILE . 5387 1 31 . GLN . 5387 1 32 . ASP . 5387 1 33 . LYS . 5387 1 34 . GLU . 5387 1 35 . GLY . 5387 1 36 . ILE . 5387 1 37 . PRO . 5387 1 38 . PRO . 5387 1 39 . ASP . 5387 1 40 . GLN . 5387 1 41 . GLN . 5387 1 42 . ARG . 5387 1 43 . LEU . 5387 1 44 . ILE . 5387 1 45 . PHE . 5387 1 46 . ALA . 5387 1 47 . GLY . 5387 1 48 . LYS . 5387 1 49 . GLN . 5387 1 50 . LEU . 5387 1 51 . GLU . 5387 1 52 . ASP . 5387 1 53 . GLY . 5387 1 54 . ARG . 5387 1 55 . THR . 5387 1 56 . LEU . 5387 1 57 . SER . 5387 1 58 . ASP . 5387 1 59 . TYR . 5387 1 60 . ASN . 5387 1 61 . ILE . 5387 1 62 . GLN . 5387 1 63 . LYS . 5387 1 64 . GLU . 5387 1 65 . SER . 5387 1 66 . THR . 5387 1 67 . LEU . 5387 1 68 . HIS . 5387 1 69 . LEU . 5387 1 70 . VAL . 5387 1 71 . LEU . 5387 1 72 . ARG . 5387 1 73 . LEU . 5387 1 74 . ARG . 5387 1 75 . GLY . 5387 1 76 . GLY . 5387 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 5387 1 . GLN 2 2 5387 1 . ILE 3 3 5387 1 . PHE 4 4 5387 1 . VAL 5 5 5387 1 . LYS 6 6 5387 1 . THR 7 7 5387 1 . LEU 8 8 5387 1 . THR 9 9 5387 1 . GLY 10 10 5387 1 . LYS 11 11 5387 1 . THR 12 12 5387 1 . ILE 13 13 5387 1 . THR 14 14 5387 1 . LEU 15 15 5387 1 . GLU 16 16 5387 1 . VAL 17 17 5387 1 . GLU 18 18 5387 1 . PRO 19 19 5387 1 . SER 20 20 5387 1 . ASP 21 21 5387 1 . THR 22 22 5387 1 . ILE 23 23 5387 1 . GLU 24 24 5387 1 . ASN 25 25 5387 1 . VAL 26 26 5387 1 . LYS 27 27 5387 1 . ALA 28 28 5387 1 . LYS 29 29 5387 1 . ILE 30 30 5387 1 . GLN 31 31 5387 1 . ASP 32 32 5387 1 . LYS 33 33 5387 1 . GLU 34 34 5387 1 . GLY 35 35 5387 1 . ILE 36 36 5387 1 . PRO 37 37 5387 1 . PRO 38 38 5387 1 . ASP 39 39 5387 1 . GLN 40 40 5387 1 . GLN 41 41 5387 1 . ARG 42 42 5387 1 . LEU 43 43 5387 1 . ILE 44 44 5387 1 . PHE 45 45 5387 1 . ALA 46 46 5387 1 . GLY 47 47 5387 1 . LYS 48 48 5387 1 . GLN 49 49 5387 1 . LEU 50 50 5387 1 . GLU 51 51 5387 1 . ASP 52 52 5387 1 . GLY 53 53 5387 1 . ARG 54 54 5387 1 . THR 55 55 5387 1 . LEU 56 56 5387 1 . SER 57 57 5387 1 . ASP 58 58 5387 1 . TYR 59 59 5387 1 . ASN 60 60 5387 1 . ILE 61 61 5387 1 . GLN 62 62 5387 1 . LYS 63 63 5387 1 . GLU 64 64 5387 1 . SER 65 65 5387 1 . THR 66 66 5387 1 . LEU 67 67 5387 1 . HIS 68 68 5387 1 . LEU 69 69 5387 1 . VAL 70 70 5387 1 . LEU 71 71 5387 1 . ARG 72 72 5387 1 . LEU 73 73 5387 1 . ARG 74 74 5387 1 . GLY 75 75 5387 1 . GLY 76 76 5387 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 5387 _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 $ubq . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5387 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 5387 _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 $ubq . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli . . . . . . . . . . . . . . . . pET . . . . . . 5387 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5387 _Sample.ID 1 _Sample.Type 'reverse micelle' _Sample.Sub_type . _Sample.Details emulsion _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-13C; U-15N]' . . 1 $ubq . . 0.3 . . mM . . . . 5387 1 2 d-pentane . . . . . . . 98 . . % . . . . 5387 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 5387 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; Sample preparation is reported in the paper. Since the protein is in pentane, pH was not measured in a typical way. ; 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 5.0 0.2 na 5387 1 temperature 293 1 K 5387 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer1 _NMR_spectrometer.Entry_ID 5387 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer2 _NMR_spectrometer.Entry_ID 5387 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5387 _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_spectrometer1 Varian INOVA . 600 . . . 5387 1 2 NMR_spectrometer2 Varian INOVA . 750 . . . 5387 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 5387 _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 HNCO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5387 1 2 HNCACB . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5387 1 3 CBCA(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5387 1 4 CC(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5387 1 5 TOCSY-15N-HSQC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5387 1 6 HCCH-TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5387 1 7 CT-13C-HSQC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5387 1 8 15N-HSQC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5387 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 5387 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name HNCO _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 5387 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name HNCACB _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 5387 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name 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_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5387 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name CC(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_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5387 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name TOCSY-15N-HSQC _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 5387 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name 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_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 5387 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name CT-13C-HSQC _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_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 5387 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name 15N-HSQC _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 5387 _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 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5387 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5387 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 . direct 1.000000000 . . . . . . . . . 5387 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 5387 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_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 HNCO 1 $sample_1 . 5387 1 2 HNCACB 1 $sample_1 . 5387 1 3 CBCA(CO)NH 1 $sample_1 . 5387 1 4 CC(CO)NH 1 $sample_1 . 5387 1 5 TOCSY-15N-HSQC 1 $sample_1 . 5387 1 6 HCCH-TOCSY 1 $sample_1 . 5387 1 7 CT-13C-HSQC 1 $sample_1 . 5387 1 8 15N-HSQC 1 $sample_1 . 5387 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 MET CA C 13 54.5 0.05 . 1 . . . . . . . . 5387 1 2 . 1 1 1 1 MET HA H 1 4.28 0.01 . 1 . . . . . . . . 5387 1 3 . 1 1 1 1 MET CB C 13 33.3 0.05 . 1 . . . . . . . . 5387 1 4 . 1 1 1 1 MET HB2 H 1 2.15 0.01 . 2 . . . . . . . . 5387 1 5 . 1 1 1 1 MET HB3 H 1 2.06 0.01 . 2 . . . . . . . . 5387 1 6 . 1 1 1 1 MET CG C 13 30.9 0.05 . 1 . . . . . . . . 5387 1 7 . 1 1 1 1 MET HG2 H 1 2.52 0.01 . 2 . . . . . . . . 5387 1 8 . 1 1 1 1 MET HG3 H 1 1.96 0.01 . 2 . . . . . . . . 5387 1 9 . 1 1 1 1 MET HE1 H 1 1.63 0.01 . 1 . . . . . . . . 5387 1 10 . 1 1 1 1 MET HE2 H 1 1.63 0.01 . 1 . . . . . . . . 5387 1 11 . 1 1 1 1 MET HE3 H 1 1.63 0.01 . 1 . . . . . . . . 5387 1 12 . 1 1 1 1 MET CE C 13 17.9 0.05 . 1 . . . . . . . . 5387 1 13 . 1 1 1 1 MET C C 13 170.5 0.05 . 1 . . . . . . . . 5387 1 14 . 1 1 2 2 GLN N N 15 123.6 0.05 . 1 . . . . . . . . 5387 1 15 . 1 1 2 2 GLN H H 1 9.01 0.01 . 1 . . . . . . . . 5387 1 16 . 1 1 2 2 GLN CA C 13 55.0 0.05 . 1 . . . . . . . . 5387 1 17 . 1 1 2 2 GLN HA H 1 5.30 0.01 . 1 . . . . . . . . 5387 1 18 . 1 1 2 2 GLN CB C 13 30.8 0.05 . 1 . . . . . . . . 5387 1 19 . 1 1 2 2 GLN HB2 H 1 1.84 0.01 . 2 . . . . . . . . 5387 1 20 . 1 1 2 2 GLN HB3 H 1 1.63 0.01 . 2 . . . . . . . . 5387 1 21 . 1 1 2 2 GLN CG C 13 34.7 0.05 . 1 . . . . . . . . 5387 1 22 . 1 1 2 2 GLN HG2 H 1 2.21 0.01 . 2 . . . . . . . . 5387 1 23 . 1 1 2 2 GLN HG3 H 1 1.85 0.01 . 2 . . . . . . . . 5387 1 24 . 1 1 2 2 GLN NE2 N 15 112.6 0.05 . 1 . . . . . . . . 5387 1 25 . 1 1 2 2 GLN HE21 H 1 6.84 0.01 . 2 . . . . . . . . 5387 1 26 . 1 1 2 2 GLN HE22 H 1 7.63 0.01 . 2 . . . . . . . . 5387 1 27 . 1 1 2 2 GLN C C 13 175.9 0.05 . 1 . . . . . . . . 5387 1 28 . 1 1 3 3 ILE N N 15 115.0 0.05 . 1 . . . . . . . . 5387 1 29 . 1 1 3 3 ILE H H 1 8.32 0.01 . 1 . . . . . . . . 5387 1 30 . 1 1 3 3 ILE CA C 13 59.6 0.05 . 1 . . . . . . . . 5387 1 31 . 1 1 3 3 ILE HA H 1 4.17 0.01 . 1 . . . . . . . . 5387 1 32 . 1 1 3 3 ILE CB C 13 42.1 0.05 . 1 . . . . . . . . 5387 1 33 . 1 1 3 3 ILE HB H 1 1.73 0.01 . 1 . . . . . . . . 5387 1 34 . 1 1 3 3 ILE HG21 H 1 0.61 0.01 . 1 . . . . . . . . 5387 1 35 . 1 1 3 3 ILE HG22 H 1 0.61 0.01 . 1 . . . . . . . . 5387 1 36 . 1 1 3 3 ILE HG23 H 1 0.61 0.01 . 1 . . . . . . . . 5387 1 37 . 1 1 3 3 ILE CG2 C 13 17.9 0.05 . 1 . . . . . . . . 5387 1 38 . 1 1 3 3 ILE CG1 C 13 24.9 0.05 . 1 . . . . . . . . 5387 1 39 . 1 1 3 3 ILE HG12 H 1 1.03 0.01 . 2 . . . . . . . . 5387 1 40 . 1 1 3 3 ILE HG13 H 1 0.81 0.01 . 2 . . . . . . . . 5387 1 41 . 1 1 3 3 ILE HD11 H 1 0.57 0.01 . 1 . . . . . . . . 5387 1 42 . 1 1 3 3 ILE HD12 H 1 0.57 0.01 . 1 . . . . . . . . 5387 1 43 . 1 1 3 3 ILE HD13 H 1 0.57 0.01 . 1 . . . . . . . . 5387 1 44 . 1 1 3 3 ILE CD1 C 13 14.3 0.05 . 1 . . . . . . . . 5387 1 45 . 1 1 3 3 ILE C C 13 172.3 0.05 . 1 . . . . . . . . 5387 1 46 . 1 1 4 4 PHE N N 15 118.4 0.05 . 1 . . . . . . . . 5387 1 47 . 1 1 4 4 PHE H H 1 8.54 0.01 . 1 . . . . . . . . 5387 1 48 . 1 1 4 4 PHE CA C 13 55.2 0.05 . 1 . . . . . . . . 5387 1 49 . 1 1 4 4 PHE HA H 1 5.51 0.01 . 1 . . . . . . . . 5387 1 50 . 1 1 4 4 PHE CB C 13 41.4 0.05 . 1 . . . . . . . . 5387 1 51 . 1 1 4 4 PHE HB2 H 1 3.03 0.01 . 2 . . . . . . . . 5387 1 52 . 1 1 4 4 PHE HB3 H 1 2.84 0.01 . 2 . . . . . . . . 5387 1 53 . 1 1 4 4 PHE HD1 H 1 7.07 0.01 . 1 . . . . . . . . 5387 1 54 . 1 1 4 4 PHE HD2 H 1 7.07 0.01 . 1 . . . . . . . . 5387 1 55 . 1 1 4 4 PHE HE1 H 1 7.23 0.01 . 1 . . . . . . . . 5387 1 56 . 1 1 4 4 PHE HE2 H 1 7.23 0.01 . 1 . . . . . . . . 5387 1 57 . 1 1 4 4 PHE CD1 C 13 132.2 0.05 . 1 . . . . . . . . 5387 1 58 . 1 1 4 4 PHE CE1 C 13 131.1 0.05 . 1 . . . . . . . . 5387 1 59 . 1 1 4 4 PHE CZ C 13 129.6 0.05 . 1 . . . . . . . . 5387 1 60 . 1 1 4 4 PHE HZ H 1 7.24 0.01 . 1 . . . . . . . . 5387 1 61 . 1 1 4 4 PHE C C 13 174.8 0.05 . 1 . . . . . . . . 5387 1 62 . 1 1 5 5 VAL N N 15 122.1 0.05 . 1 . . . . . . . . 5387 1 63 . 1 1 5 5 VAL H H 1 9.33 0.01 . 1 . . . . . . . . 5387 1 64 . 1 1 5 5 VAL CA C 13 60.8 0.05 . 1 . . . . . . . . 5387 1 65 . 1 1 5 5 VAL HA H 1 4.67 0.01 . 1 . . . . . . . . 5387 1 66 . 1 1 5 5 VAL CB C 13 33.8 0.05 . 1 . . . . . . . . 5387 1 67 . 1 1 5 5 VAL HB H 1 1.93 0.01 . 1 . . . . . . . . 5387 1 68 . 1 1 5 5 VAL HG11 H 1 0.72 0.01 . 2 . . . . . . . . 5387 1 69 . 1 1 5 5 VAL HG12 H 1 0.72 0.01 . 2 . . . . . . . . 5387 1 70 . 1 1 5 5 VAL HG13 H 1 0.72 0.01 . 2 . . . . . . . . 5387 1 71 . 1 1 5 5 VAL HG21 H 1 0.70 0.01 . 2 . . . . . . . . 5387 1 72 . 1 1 5 5 VAL HG22 H 1 0.70 0.01 . 2 . . . . . . . . 5387 1 73 . 1 1 5 5 VAL HG23 H 1 0.70 0.01 . 2 . . . . . . . . 5387 1 74 . 1 1 5 5 VAL CG1 C 13 20.8 0.05 . 1 . . . . . . . . 5387 1 75 . 1 1 5 5 VAL CG2 C 13 23.2 0.05 . 1 . . . . . . . . 5387 1 76 . 1 1 5 5 VAL C C 13 174.5 0.05 . 1 . . . . . . . . 5387 1 77 . 1 1 6 6 LYS N N 15 127.4 0.05 . 1 . . . . . . . . 5387 1 78 . 1 1 6 6 LYS H H 1 8.83 0.01 . 1 . . . . . . . . 5387 1 79 . 1 1 6 6 LYS CA C 13 54.5 0.05 . 1 . . . . . . . . 5387 1 80 . 1 1 6 6 LYS HA H 1 5.63 0.01 . 1 . . . . . . . . 5387 1 81 . 1 1 6 6 LYS CB C 13 36.5 0.05 . 1 . . . . . . . . 5387 1 82 . 1 1 6 6 LYS HB2 H 1 1.72 0.01 . 2 . . . . . . . . 5387 1 83 . 1 1 6 6 LYS HB3 H 1 1.30 0.01 . 2 . . . . . . . . 5387 1 84 . 1 1 6 6 LYS CG C 13 25.1 0.05 . 1 . . . . . . . . 5387 1 85 . 1 1 6 6 LYS HG2 H 1 1.60 0.01 . 2 . . . . . . . . 5387 1 86 . 1 1 6 6 LYS HG3 H 1 1.26 0.01 . 2 . . . . . . . . 5387 1 87 . 1 1 6 6 LYS CD C 13 29.8 0.05 . 1 . . . . . . . . 5387 1 88 . 1 1 6 6 LYS HD2 H 1 1.60 0.01 . 1 . . . . . . . . 5387 1 89 . 1 1 6 6 LYS HD3 H 1 1.60 0.01 . 1 . . . . . . . . 5387 1 90 . 1 1 6 6 LYS CE C 13 42.2 0.05 . 1 . . . . . . . . 5387 1 91 . 1 1 6 6 LYS HE2 H 1 2.98 0.01 . 2 . . . . . . . . 5387 1 92 . 1 1 6 6 LYS HE3 H 1 2.91 0.01 . 2 . . . . . . . . 5387 1 93 . 1 1 7 7 THR N N 15 116.5 0.05 . 1 . . . . . . . . 5387 1 94 . 1 1 7 7 THR H H 1 8.77 0.01 . 1 . . . . . . . . 5387 1 95 . 1 1 7 7 THR CA C 13 60.4 0.05 . 1 . . . . . . . . 5387 1 96 . 1 1 7 7 THR HA H 1 5.33 0.01 . 1 . . . . . . . . 5387 1 97 . 1 1 7 7 THR CB C 13 70.7 0.05 . 1 . . . . . . . . 5387 1 98 . 1 1 7 7 THR HB H 1 4.99 0.01 . 1 . . . . . . . . 5387 1 99 . 1 1 7 7 THR HG21 H 1 1.22 0.01 . 1 . . . . . . . . 5387 1 100 . 1 1 7 7 THR HG22 H 1 1.22 0.01 . 1 . . . . . . . . 5387 1 101 . 1 1 7 7 THR HG23 H 1 1.22 0.01 . 1 . . . . . . . . 5387 1 102 . 1 1 7 7 THR CG2 C 13 21.6 0.05 . 1 . . . . . . . . 5387 1 103 . 1 1 7 7 THR C C 13 176.6 0.05 . 1 . . . . . . . . 5387 1 104 . 1 1 8 8 LEU N N 15 121.8 0.05 . 1 . . . . . . . . 5387 1 105 . 1 1 8 8 LEU H H 1 9.32 0.01 . 1 . . . . . . . . 5387 1 106 . 1 1 8 8 LEU CA C 13 57.5 0.05 . 1 . . . . . . . . 5387 1 107 . 1 1 8 8 LEU HA H 1 4.32 0.01 . 1 . . . . . . . . 5387 1 108 . 1 1 8 8 LEU CB C 13 41.8 0.05 . 1 . . . . . . . . 5387 1 109 . 1 1 8 8 LEU HB2 H 1 1.93 0.01 . 2 . . . . . . . . 5387 1 110 . 1 1 8 8 LEU HB3 H 1 1.75 0.01 . 2 . . . . . . . . 5387 1 111 . 1 1 8 8 LEU CG C 13 27.4 0.05 . 1 . . . . . . . . 5387 1 112 . 1 1 8 8 LEU HG H 1 1.96 0.01 . 1 . . . . . . . . 5387 1 113 . 1 1 8 8 LEU HD11 H 1 1.01 0.01 . 2 . . . . . . . . 5387 1 114 . 1 1 8 8 LEU HD12 H 1 1.01 0.01 . 2 . . . . . . . . 5387 1 115 . 1 1 8 8 LEU HD13 H 1 1.01 0.01 . 2 . . . . . . . . 5387 1 116 . 1 1 8 8 LEU HD21 H 1 0.92 0.01 . 2 . . . . . . . . 5387 1 117 . 1 1 8 8 LEU HD22 H 1 0.92 0.01 . 2 . . . . . . . . 5387 1 118 . 1 1 8 8 LEU HD23 H 1 0.92 0.01 . 2 . . . . . . . . 5387 1 119 . 1 1 8 8 LEU CD1 C 13 25.6 0.05 . 1 . . . . . . . . 5387 1 120 . 1 1 8 8 LEU CD2 C 13 23.9 0.05 . 1 . . . . . . . . 5387 1 121 . 1 1 8 8 LEU C C 13 176.5 0.05 . 1 . . . . . . . . 5387 1 122 . 1 1 9 9 THR N N 15 101.1 0.05 . 1 . . . . . . . . 5387 1 123 . 1 1 9 9 THR H H 1 7.42 0.01 . 1 . . . . . . . . 5387 1 124 . 1 1 9 9 THR CA C 13 61.0 0.05 . 1 . . . . . . . . 5387 1 125 . 1 1 9 9 THR HA H 1 4.29 0.01 . 1 . . . . . . . . 5387 1 126 . 1 1 9 9 THR CB C 13 69.0 0.05 . 1 . . . . . . . . 5387 1 127 . 1 1 9 9 THR HB H 1 4.62 0.01 . 1 . . . . . . . . 5387 1 128 . 1 1 9 9 THR HG21 H 1 1.23 0.01 . 1 . . . . . . . . 5387 1 129 . 1 1 9 9 THR HG22 H 1 1.23 0.01 . 1 . . . . . . . . 5387 1 130 . 1 1 9 9 THR HG23 H 1 1.23 0.01 . 1 . . . . . . . . 5387 1 131 . 1 1 9 9 THR CG2 C 13 22.2 0.05 . 1 . . . . . . . . 5387 1 132 . 1 1 9 9 THR C C 13 174.5 0.05 . 1 . . . . . . . . 5387 1 133 . 1 1 10 10 GLY N N 15 107.1 0.05 . 1 . . . . . . . . 5387 1 134 . 1 1 10 10 GLY H H 1 7.65 0.01 . 1 . . . . . . . . 5387 1 135 . 1 1 10 10 GLY CA C 13 45.6 0.05 . 1 . . . . . . . . 5387 1 136 . 1 1 10 10 GLY HA2 H 1 4.28 0.01 . 2 . . . . . . . . 5387 1 137 . 1 1 10 10 GLY HA3 H 1 3.64 0.01 . 2 . . . . . . . . 5387 1 138 . 1 1 10 10 GLY C C 13 174.6 0.05 . 1 . . . . . . . . 5387 1 139 . 1 1 11 11 LYS N N 15 122.4 0.05 . 1 . . . . . . . . 5387 1 140 . 1 1 11 11 LYS H H 1 7.47 0.01 . 1 . . . . . . . . 5387 1 141 . 1 1 11 11 LYS CA C 13 56.6 0.05 . 1 . . . . . . . . 5387 1 142 . 1 1 11 11 LYS HA H 1 4.33 0.01 . 1 . . . . . . . . 5387 1 143 . 1 1 11 11 LYS CB C 13 32.5 0.05 . 1 . . . . . . . . 5387 1 144 . 1 1 11 11 LYS HB2 H 1 1.86 0.01 . 2 . . . . . . . . 5387 1 145 . 1 1 11 11 LYS HB3 H 1 1.79 0.01 . 2 . . . . . . . . 5387 1 146 . 1 1 11 11 LYS CG C 13 24.8 0.05 . 1 . . . . . . . . 5387 1 147 . 1 1 11 11 LYS HG2 H 1 1.43 0.01 . 2 . . . . . . . . 5387 1 148 . 1 1 11 11 LYS HG3 H 1 1.26 0.01 . 2 . . . . . . . . 5387 1 149 . 1 1 11 11 LYS CD C 13 29.2 0.05 . 1 . . . . . . . . 5387 1 150 . 1 1 11 11 LYS HD2 H 1 1.64 0.01 . 1 . . . . . . . . 5387 1 151 . 1 1 11 11 LYS HD3 H 1 1.64 0.01 . 1 . . . . . . . . 5387 1 152 . 1 1 11 11 LYS CE C 13 42.1 0.05 . 1 . . . . . . . . 5387 1 153 . 1 1 11 11 LYS HE2 H 1 2.95 0.01 . 1 . . . . . . . . 5387 1 154 . 1 1 11 11 LYS HE3 H 1 2.95 0.01 . 1 . . . . . . . . 5387 1 155 . 1 1 11 11 LYS C C 13 176.4 0.05 . 1 . . . . . . . . 5387 1 156 . 1 1 12 12 THR N N 15 120.9 0.05 . 1 . . . . . . . . 5387 1 157 . 1 1 12 12 THR H H 1 8.61 0.01 . 1 . . . . . . . . 5387 1 158 . 1 1 12 12 THR CA C 13 62.6 0.05 . 1 . . . . . . . . 5387 1 159 . 1 1 12 12 THR HA H 1 4.97 0.01 . 1 . . . . . . . . 5387 1 160 . 1 1 12 12 THR CB C 13 69.9 0.05 . 1 . . . . . . . . 5387 1 161 . 1 1 12 12 THR HB H 1 3.98 0.01 . 1 . . . . . . . . 5387 1 162 . 1 1 12 12 THR HG21 H 1 1.09 0.01 . 1 . . . . . . . . 5387 1 163 . 1 1 12 12 THR HG22 H 1 1.09 0.01 . 1 . . . . . . . . 5387 1 164 . 1 1 12 12 THR HG23 H 1 1.09 0.01 . 1 . . . . . . . . 5387 1 165 . 1 1 12 12 THR CG2 C 13 21.8 0.05 . 1 . . . . . . . . 5387 1 166 . 1 1 12 12 THR C C 13 174.0 0.05 . 1 . . . . . . . . 5387 1 167 . 1 1 13 13 ILE N N 15 129.2 0.05 . 1 . . . . . . . . 5387 1 168 . 1 1 13 13 ILE H H 1 9.62 0.01 . 1 . . . . . . . . 5387 1 169 . 1 1 13 13 ILE CA C 13 60.2 0.05 . 1 . . . . . . . . 5387 1 170 . 1 1 13 13 ILE HA H 1 4.45 0.01 . 1 . . . . . . . . 5387 1 171 . 1 1 13 13 ILE CB C 13 41.1 0.05 . 1 . . . . . . . . 5387 1 172 . 1 1 13 13 ILE HB H 1 1.84 0.01 . 1 . . . . . . . . 5387 1 173 . 1 1 13 13 ILE HG21 H 1 0.87 0.01 . 1 . . . . . . . . 5387 1 174 . 1 1 13 13 ILE HG22 H 1 0.87 0.01 . 1 . . . . . . . . 5387 1 175 . 1 1 13 13 ILE HG23 H 1 0.87 0.01 . 1 . . . . . . . . 5387 1 176 . 1 1 13 13 ILE CG2 C 13 17.9 0.05 . 1 . . . . . . . . 5387 1 177 . 1 1 13 13 ILE CG1 C 13 27.2 0.05 . 1 . . . . . . . . 5387 1 178 . 1 1 13 13 ILE HG12 H 1 1.50 0.01 . 2 . . . . . . . . 5387 1 179 . 1 1 13 13 ILE HG13 H 1 1.04 0.01 . 2 . . . . . . . . 5387 1 180 . 1 1 13 13 ILE HD11 H 1 0.70 0.01 . 1 . . . . . . . . 5387 1 181 . 1 1 13 13 ILE HD12 H 1 0.70 0.01 . 1 . . . . . . . . 5387 1 182 . 1 1 13 13 ILE HD13 H 1 0.70 0.01 . 1 . . . . . . . . 5387 1 183 . 1 1 13 13 ILE CD1 C 13 14.8 0.05 . 1 . . . . . . . . 5387 1 184 . 1 1 13 13 ILE C C 13 175.1 0.05 . 1 . . . . . . . . 5387 1 185 . 1 1 14 14 THR N N 15 123.2 0.05 . 1 . . . . . . . . 5387 1 186 . 1 1 14 14 THR H H 1 8.80 0.01 . 1 . . . . . . . . 5387 1 187 . 1 1 14 14 THR CA C 13 62.2 0.05 . 1 . . . . . . . . 5387 1 188 . 1 1 14 14 THR HA H 1 4.92 0.01 . 1 . . . . . . . . 5387 1 189 . 1 1 14 14 THR CB C 13 69.5 0.05 . 1 . . . . . . . . 5387 1 190 . 1 1 14 14 THR HB H 1 4.04 0.01 . 1 . . . . . . . . 5387 1 191 . 1 1 14 14 THR HG21 H 1 1.13 0.01 . 1 . . . . . . . . 5387 1 192 . 1 1 14 14 THR HG22 H 1 1.13 0.01 . 1 . . . . . . . . 5387 1 193 . 1 1 14 14 THR HG23 H 1 1.13 0.01 . 1 . . . . . . . . 5387 1 194 . 1 1 14 14 THR CG2 C 13 21.9 0.05 . 1 . . . . . . . . 5387 1 195 . 1 1 14 14 THR C C 13 173.7 0.05 . 1 . . . . . . . . 5387 1 196 . 1 1 15 15 LEU N N 15 125.0 0.05 . 1 . . . . . . . . 5387 1 197 . 1 1 15 15 LEU H H 1 8.64 0.01 . 1 . . . . . . . . 5387 1 198 . 1 1 15 15 LEU CA C 13 52.8 0.05 . 1 . . . . . . . . 5387 1 199 . 1 1 15 15 LEU HA H 1 4.84 0.01 . 1 . . . . . . . . 5387 1 200 . 1 1 15 15 LEU CB C 13 47.2 0.05 . 1 . . . . . . . . 5387 1 201 . 1 1 15 15 LEU HB2 H 1 1.34 0.01 . 2 . . . . . . . . 5387 1 202 . 1 1 15 15 LEU HB3 H 1 1.21 0.01 . 2 . . . . . . . . 5387 1 203 . 1 1 15 15 LEU CG C 13 26.8 0.05 . 1 . . . . . . . . 5387 1 204 . 1 1 15 15 LEU HG H 1 1.41 0.01 . 1 . . . . . . . . 5387 1 205 . 1 1 15 15 LEU HD11 H 1 0.70 0.01 . 2 . . . . . . . . 5387 1 206 . 1 1 15 15 LEU HD12 H 1 0.70 0.01 . 2 . . . . . . . . 5387 1 207 . 1 1 15 15 LEU HD13 H 1 0.70 0.01 . 2 . . . . . . . . 5387 1 208 . 1 1 15 15 LEU HD21 H 1 0.76 0.01 . 2 . . . . . . . . 5387 1 209 . 1 1 15 15 LEU HD22 H 1 0.76 0.01 . 2 . . . . . . . . 5387 1 210 . 1 1 15 15 LEU HD23 H 1 0.76 0.01 . 2 . . . . . . . . 5387 1 211 . 1 1 15 15 LEU CD1 C 13 27.4 0.05 . 1 . . . . . . . . 5387 1 212 . 1 1 15 15 LEU CD2 C 13 24.3 0.05 . 1 . . . . . . . . 5387 1 213 . 1 1 15 15 LEU C C 13 174.5 0.05 . 1 . . . . . . . . 5387 1 214 . 1 1 16 16 GLU N N 15 123.3 0.05 . 1 . . . . . . . . 5387 1 215 . 1 1 16 16 GLU H H 1 8.26 0.01 . 1 . . . . . . . . 5387 1 216 . 1 1 16 16 GLU CA C 13 55.0 0.05 . 1 . . . . . . . . 5387 1 217 . 1 1 16 16 GLU HA H 1 4.88 0.01 . 1 . . . . . . . . 5387 1 218 . 1 1 16 16 GLU CB C 13 29.9 0.05 . 1 . . . . . . . . 5387 1 219 . 1 1 16 16 GLU HB2 H 1 1.93 0.01 . 2 . . . . . . . . 5387 1 220 . 1 1 16 16 GLU HB3 H 1 1.84 0.01 . 2 . . . . . . . . 5387 1 221 . 1 1 16 16 GLU CG C 13 35.7 0.05 . 1 . . . . . . . . 5387 1 222 . 1 1 16 16 GLU HG2 H 1 2.25 0.01 . 2 . . . . . . . . 5387 1 223 . 1 1 16 16 GLU HG3 H 1 2.09 0.01 . 2 . . . . . . . . 5387 1 224 . 1 1 16 16 GLU C C 13 175.8 0.05 . 1 . . . . . . . . 5387 1 225 . 1 1 17 17 VAL N N 15 117.8 0.05 . 1 . . . . . . . . 5387 1 226 . 1 1 17 17 VAL H H 1 8.96 0.01 . 1 . . . . . . . . 5387 1 227 . 1 1 17 17 VAL CA C 13 58.4 0.05 . 1 . . . . . . . . 5387 1 228 . 1 1 17 17 VAL HA H 1 4.71 0.01 . 1 . . . . . . . . 5387 1 229 . 1 1 17 17 VAL CB C 13 36.5 0.05 . 1 . . . . . . . . 5387 1 230 . 1 1 17 17 VAL HB H 1 2.32 0.01 . 1 . . . . . . . . 5387 1 231 . 1 1 17 17 VAL HG11 H 1 0.70 0.01 . 2 . . . . . . . . 5387 1 232 . 1 1 17 17 VAL HG12 H 1 0.70 0.01 . 2 . . . . . . . . 5387 1 233 . 1 1 17 17 VAL HG13 H 1 0.70 0.01 . 2 . . . . . . . . 5387 1 234 . 1 1 17 17 VAL HG21 H 1 0.42 0.01 . 2 . . . . . . . . 5387 1 235 . 1 1 17 17 VAL HG22 H 1 0.42 0.01 . 2 . . . . . . . . 5387 1 236 . 1 1 17 17 VAL HG23 H 1 0.42 0.01 . 2 . . . . . . . . 5387 1 237 . 1 1 17 17 VAL CG1 C 13 22.3 0.05 . 1 . . . . . . . . 5387 1 238 . 1 1 17 17 VAL CG2 C 13 19.7 0.05 . 1 . . . . . . . . 5387 1 239 . 1 1 17 17 VAL C C 13 174.0 0.05 . 1 . . . . . . . . 5387 1 240 . 1 1 18 18 GLU N N 15 119.4 0.05 . 1 . . . . . . . . 5387 1 241 . 1 1 18 18 GLU H H 1 8.72 0.01 . 1 . . . . . . . . 5387 1 242 . 1 1 18 18 GLU CA C 13 52.8 0.05 . 1 . . . . . . . . 5387 1 243 . 1 1 18 18 GLU HA H 1 5.07 0.01 . 1 . . . . . . . . 5387 1 244 . 1 1 18 18 GLU CB C 13 30.9 0.05 . 1 . . . . . . . . 5387 1 245 . 1 1 18 18 GLU HB2 H 1 2.16 0.01 . 2 . . . . . . . . 5387 1 246 . 1 1 18 18 GLU HB3 H 1 1.60 0.01 . 2 . . . . . . . . 5387 1 247 . 1 1 18 18 GLU CG C 13 35.4 0.05 . 1 . . . . . . . . 5387 1 248 . 1 1 18 18 GLU HG2 H 1 2.34 0.01 . 2 . . . . . . . . 5387 1 249 . 1 1 18 18 GLU HG3 H 1 2.23 0.01 . 2 . . . . . . . . 5387 1 250 . 1 1 19 19 PRO CD C 13 50.5 0.05 . 1 . . . . . . . . 5387 1 251 . 1 1 19 19 PRO CA C 13 65.4 0.05 . 1 . . . . . . . . 5387 1 252 . 1 1 19 19 PRO HA H 1 4.12 0.01 . 1 . . . . . . . . 5387 1 253 . 1 1 19 19 PRO CB C 13 32.0 0.05 . 1 . . . . . . . . 5387 1 254 . 1 1 19 19 PRO HB2 H 1 2.44 0.01 . 2 . . . . . . . . 5387 1 255 . 1 1 19 19 PRO HB3 H 1 2.03 0.01 . 2 . . . . . . . . 5387 1 256 . 1 1 19 19 PRO CG C 13 28.1 0.05 . 1 . . . . . . . . 5387 1 257 . 1 1 19 19 PRO HG2 H 1 2.24 0.01 . 2 . . . . . . . . 5387 1 258 . 1 1 19 19 PRO HG3 H 1 2.06 0.01 . 2 . . . . . . . . 5387 1 259 . 1 1 19 19 PRO HD2 H 1 4.00 0.01 . 2 . . . . . . . . 5387 1 260 . 1 1 19 19 PRO HD3 H 1 3.82 0.01 . 2 . . . . . . . . 5387 1 261 . 1 1 19 19 PRO C C 13 175.3 0.05 . 1 . . . . . . . . 5387 1 262 . 1 1 20 20 SER N N 15 103.8 0.05 . 1 . . . . . . . . 5387 1 263 . 1 1 20 20 SER H H 1 7.11 0.01 . 1 . . . . . . . . 5387 1 264 . 1 1 20 20 SER CA C 13 57.5 0.05 . 1 . . . . . . . . 5387 1 265 . 1 1 20 20 SER HA H 1 4.37 0.01 . 1 . . . . . . . . 5387 1 266 . 1 1 20 20 SER CB C 13 63.5 0.05 . 1 . . . . . . . . 5387 1 267 . 1 1 20 20 SER HB2 H 1 4.16 0.01 . 2 . . . . . . . . 5387 1 268 . 1 1 20 20 SER HB3 H 1 3.84 0.01 . 2 . . . . . . . . 5387 1 269 . 1 1 20 20 SER C C 13 174.9 0.05 . 1 . . . . . . . . 5387 1 270 . 1 1 21 21 ASP N N 15 124.2 0.05 . 1 . . . . . . . . 5387 1 271 . 1 1 21 21 ASP H H 1 8.12 0.01 . 1 . . . . . . . . 5387 1 272 . 1 1 21 21 ASP CA C 13 55.9 0.05 . 1 . . . . . . . . 5387 1 273 . 1 1 21 21 ASP HA H 1 4.72 0.01 . 1 . . . . . . . . 5387 1 274 . 1 1 21 21 ASP CB C 13 40.9 0.05 . 1 . . . . . . . . 5387 1 275 . 1 1 21 21 ASP HB2 H 1 2.95 0.01 . 2 . . . . . . . . 5387 1 276 . 1 1 21 21 ASP HB3 H 1 2.50 0.01 . 2 . . . . . . . . 5387 1 277 . 1 1 21 21 ASP C C 13 176.2 0.05 . 1 . . . . . . . . 5387 1 278 . 1 1 22 22 THR N N 15 108.9 0.05 . 1 . . . . . . . . 5387 1 279 . 1 1 22 22 THR H H 1 7.88 0.01 . 1 . . . . . . . . 5387 1 280 . 1 1 22 22 THR CA C 13 59.6 0.05 . 1 . . . . . . . . 5387 1 281 . 1 1 22 22 THR HA H 1 4.91 0.01 . 1 . . . . . . . . 5387 1 282 . 1 1 22 22 THR CB C 13 71.1 0.05 . 1 . . . . . . . . 5387 1 283 . 1 1 22 22 THR HB H 1 4.86 0.01 . 1 . . . . . . . . 5387 1 284 . 1 1 22 22 THR HG21 H 1 1.26 0.01 . 1 . . . . . . . . 5387 1 285 . 1 1 22 22 THR HG22 H 1 1.26 0.01 . 1 . . . . . . . . 5387 1 286 . 1 1 22 22 THR HG23 H 1 1.26 0.01 . 1 . . . . . . . . 5387 1 287 . 1 1 22 22 THR CG2 C 13 22.4 0.05 . 1 . . . . . . . . 5387 1 288 . 1 1 22 22 THR C C 13 176.6 0.05 . 1 . . . . . . . . 5387 1 289 . 1 1 23 23 ILE N N 15 122.1 0.05 . 1 . . . . . . . . 5387 1 290 . 1 1 23 23 ILE H H 1 8.66 0.01 . 1 . . . . . . . . 5387 1 291 . 1 1 23 23 ILE CA C 13 62.1 0.05 . 1 . . . . . . . . 5387 1 292 . 1 1 23 23 ILE HA H 1 3.65 0.01 . 1 . . . . . . . . 5387 1 293 . 1 1 23 23 ILE CB C 13 34.0 0.05 . 1 . . . . . . . . 5387 1 294 . 1 1 23 23 ILE HB H 1 2.67 0.01 . 1 . . . . . . . . 5387 1 295 . 1 1 23 23 ILE HG21 H 1 0.75 0.01 . 1 . . . . . . . . 5387 1 296 . 1 1 23 23 ILE HG22 H 1 0.75 0.01 . 1 . . . . . . . . 5387 1 297 . 1 1 23 23 ILE HG23 H 1 0.75 0.01 . 1 . . . . . . . . 5387 1 298 . 1 1 23 23 ILE CG2 C 13 17.9 0.05 . 1 . . . . . . . . 5387 1 299 . 1 1 23 23 ILE CG1 C 13 27.6 0.05 . 1 . . . . . . . . 5387 1 300 . 1 1 23 23 ILE HG12 H 1 1.88 0.01 . 2 . . . . . . . . 5387 1 301 . 1 1 23 23 ILE HG13 H 1 1.27 0.01 . 2 . . . . . . . . 5387 1 302 . 1 1 23 23 ILE HD11 H 1 0.54 0.01 . 1 . . . . . . . . 5387 1 303 . 1 1 23 23 ILE HD12 H 1 0.54 0.01 . 1 . . . . . . . . 5387 1 304 . 1 1 23 23 ILE HD13 H 1 0.54 0.01 . 1 . . . . . . . . 5387 1 305 . 1 1 23 23 ILE CD1 C 13 9.4 0.05 . 1 . . . . . . . . 5387 1 306 . 1 1 24 24 GLU H H 1 9.50 0.01 . 1 . . . . . . . . 5387 1 307 . 1 1 24 24 GLU CA C 13 60.3 0.05 . 1 . . . . . . . . 5387 1 308 . 1 1 24 24 GLU HA H 1 3.84 0.01 . 1 . . . . . . . . 5387 1 309 . 1 1 24 24 GLU CB C 13 29.3 0.05 . 1 . . . . . . . . 5387 1 310 . 1 1 24 24 GLU HB2 H 1 2.02 0.01 . 1 . . . . . . . . 5387 1 311 . 1 1 24 24 GLU HB3 H 1 2.02 0.01 . 1 . . . . . . . . 5387 1 312 . 1 1 24 24 GLU CG C 13 35.9 0.05 . 1 . . . . . . . . 5387 1 313 . 1 1 24 24 GLU HG2 H 1 2.29 0.01 . 1 . . . . . . . . 5387 1 314 . 1 1 24 24 GLU HG3 H 1 2.29 0.01 . 1 . . . . . . . . 5387 1 315 . 1 1 24 24 GLU C C 13 178.6 0.05 . 1 . . . . . . . . 5387 1 316 . 1 1 25 25 ASN N N 15 120.7 0.05 . 1 . . . . . . . . 5387 1 317 . 1 1 25 25 ASN H H 1 7.95 0.01 . 1 . . . . . . . . 5387 1 318 . 1 1 25 25 ASN CA C 13 56.0 0.05 . 1 . . . . . . . . 5387 1 319 . 1 1 25 25 ASN HA H 1 4.53 0.01 . 1 . . . . . . . . 5387 1 320 . 1 1 25 25 ASN CB C 13 38.4 0.05 . 1 . . . . . . . . 5387 1 321 . 1 1 25 25 ASN HB2 H 1 3.26 0.01 . 2 . . . . . . . . 5387 1 322 . 1 1 25 25 ASN HB3 H 1 2.83 0.01 . 2 . . . . . . . . 5387 1 323 . 1 1 25 25 ASN ND2 N 15 110.4 0.05 . 1 . . . . . . . . 5387 1 324 . 1 1 25 25 ASN HD21 H 1 7.90 0.01 . 2 . . . . . . . . 5387 1 325 . 1 1 25 25 ASN HD22 H 1 6.98 0.01 . 2 . . . . . . . . 5387 1 326 . 1 1 25 25 ASN C C 13 178.3 0.05 . 1 . . . . . . . . 5387 1 327 . 1 1 26 26 VAL N N 15 122.5 0.05 . 1 . . . . . . . . 5387 1 328 . 1 1 26 26 VAL H H 1 8.16 0.01 . 1 . . . . . . . . 5387 1 329 . 1 1 26 26 VAL CA C 13 67.7 0.05 . 1 . . . . . . . . 5387 1 330 . 1 1 26 26 VAL HA H 1 3.37 0.01 . 1 . . . . . . . . 5387 1 331 . 1 1 26 26 VAL CB C 13 30.9 0.05 . 1 . . . . . . . . 5387 1 332 . 1 1 26 26 VAL HB H 1 2.34 0.01 . 1 . . . . . . . . 5387 1 333 . 1 1 26 26 VAL HG11 H 1 0.97 0.01 . 2 . . . . . . . . 5387 1 334 . 1 1 26 26 VAL HG12 H 1 0.97 0.01 . 2 . . . . . . . . 5387 1 335 . 1 1 26 26 VAL HG13 H 1 0.97 0.01 . 2 . . . . . . . . 5387 1 336 . 1 1 26 26 VAL HG21 H 1 0.69 0.01 . 2 . . . . . . . . 5387 1 337 . 1 1 26 26 VAL HG22 H 1 0.69 0.01 . 2 . . . . . . . . 5387 1 338 . 1 1 26 26 VAL HG23 H 1 0.69 0.01 . 2 . . . . . . . . 5387 1 339 . 1 1 26 26 VAL CG1 C 13 23.7 0.05 . 1 . . . . . . . . 5387 1 340 . 1 1 26 26 VAL CG2 C 13 21.5 0.05 . 1 . . . . . . . . 5387 1 341 . 1 1 26 26 VAL C C 13 177.7 0.05 . 1 . . . . . . . . 5387 1 342 . 1 1 27 27 LYS N N 15 119.3 0.05 . 1 . . . . . . . . 5387 1 343 . 1 1 27 27 LYS H H 1 8.56 0.01 . 1 . . . . . . . . 5387 1 344 . 1 1 27 27 LYS CA C 13 59.3 0.05 . 1 . . . . . . . . 5387 1 345 . 1 1 27 27 LYS HA H 1 4.58 0.01 . 1 . . . . . . . . 5387 1 346 . 1 1 27 27 LYS CB C 13 33.6 0.05 . 1 . . . . . . . . 5387 1 347 . 1 1 27 27 LYS HB2 H 1 1.97 0.01 . 2 . . . . . . . . 5387 1 348 . 1 1 27 27 LYS HB3 H 1 1.45 0.01 . 2 . . . . . . . . 5387 1 349 . 1 1 27 27 LYS CG C 13 27.2 0.05 . 1 . . . . . . . . 5387 1 350 . 1 1 27 27 LYS HG2 H 1 1.50 0.01 . 1 . . . . . . . . 5387 1 351 . 1 1 27 27 LYS HG3 H 1 1.50 0.01 . 1 . . . . . . . . 5387 1 352 . 1 1 27 27 LYS CD C 13 29.9 0.05 . 1 . . . . . . . . 5387 1 353 . 1 1 27 27 LYS HD2 H 1 1.76 0.01 . 1 . . . . . . . . 5387 1 354 . 1 1 27 27 LYS HD3 H 1 1.76 0.01 . 1 . . . . . . . . 5387 1 355 . 1 1 27 27 LYS CE C 13 42.8 0.05 . 1 . . . . . . . . 5387 1 356 . 1 1 27 27 LYS HE2 H 1 2.65 0.01 . 2 . . . . . . . . 5387 1 357 . 1 1 27 27 LYS HE3 H 1 2.52 0.01 . 2 . . . . . . . . 5387 1 358 . 1 1 27 27 LYS C C 13 180.5 0.05 . 1 . . . . . . . . 5387 1 359 . 1 1 28 28 ALA N N 15 123.4 0.05 . 1 . . . . . . . . 5387 1 360 . 1 1 28 28 ALA H H 1 8.06 0.01 . 1 . . . . . . . . 5387 1 361 . 1 1 28 28 ALA CA C 13 55.2 0.05 . 1 . . . . . . . . 5387 1 362 . 1 1 28 28 ALA HA H 1 4.16 0.01 . 1 . . . . . . . . 5387 1 363 . 1 1 28 28 ALA HB1 H 1 1.63 0.01 . 1 . . . . . . . . 5387 1 364 . 1 1 28 28 ALA HB2 H 1 1.63 0.01 . 1 . . . . . . . . 5387 1 365 . 1 1 28 28 ALA HB3 H 1 1.63 0.01 . 1 . . . . . . . . 5387 1 366 . 1 1 28 28 ALA CB C 13 17.9 0.05 . 1 . . . . . . . . 5387 1 367 . 1 1 28 28 ALA C C 13 180.2 0.05 . 1 . . . . . . . . 5387 1 368 . 1 1 29 29 LYS N N 15 121.0 0.05 . 1 . . . . . . . . 5387 1 369 . 1 1 29 29 LYS H H 1 8.01 0.01 . 1 . . . . . . . . 5387 1 370 . 1 1 29 29 LYS CA C 13 59.8 0.05 . 1 . . . . . . . . 5387 1 371 . 1 1 29 29 LYS HA H 1 4.20 0.01 . 1 . . . . . . . . 5387 1 372 . 1 1 29 29 LYS CB C 13 33.3 0.05 . 1 . . . . . . . . 5387 1 373 . 1 1 29 29 LYS HB2 H 1 2.12 0.01 . 2 . . . . . . . . 5387 1 374 . 1 1 29 29 LYS HB3 H 1 1.95 0.01 . 2 . . . . . . . . 5387 1 375 . 1 1 29 29 LYS CG C 13 26.5 0.05 . 1 . . . . . . . . 5387 1 376 . 1 1 29 29 LYS HG2 H 1 1.77 0.01 . 2 . . . . . . . . 5387 1 377 . 1 1 29 29 LYS HG3 H 1 1.61 0.01 . 2 . . . . . . . . 5387 1 378 . 1 1 29 29 LYS CD C 13 30.3 0.05 . 1 . . . . . . . . 5387 1 379 . 1 1 29 29 LYS HD2 H 1 1.81 0.01 . 2 . . . . . . . . 5387 1 380 . 1 1 29 29 LYS HD3 H 1 1.45 0.01 . 2 . . . . . . . . 5387 1 381 . 1 1 29 29 LYS CE C 13 42.5 0.05 . 1 . . . . . . . . 5387 1 382 . 1 1 29 29 LYS HE2 H 1 3.19 0.01 . 2 . . . . . . . . 5387 1 383 . 1 1 29 29 LYS HE3 H 1 2.97 0.01 . 2 . . . . . . . . 5387 1 384 . 1 1 29 29 LYS C C 13 180.2 0.05 . 1 . . . . . . . . 5387 1 385 . 1 1 30 30 ILE N N 15 121.8 0.05 . 1 . . . . . . . . 5387 1 386 . 1 1 30 30 ILE H H 1 8.28 0.01 . 1 . . . . . . . . 5387 1 387 . 1 1 30 30 ILE CA C 13 66.3 0.05 . 1 . . . . . . . . 5387 1 388 . 1 1 30 30 ILE HA H 1 3.49 0.01 . 1 . . . . . . . . 5387 1 389 . 1 1 30 30 ILE CB C 13 36.9 0.05 . 1 . . . . . . . . 5387 1 390 . 1 1 30 30 ILE HB H 1 2.33 0.01 . 1 . . . . . . . . 5387 1 391 . 1 1 30 30 ILE HG21 H 1 0.69 0.01 . 1 . . . . . . . . 5387 1 392 . 1 1 30 30 ILE HG22 H 1 0.69 0.01 . 1 . . . . . . . . 5387 1 393 . 1 1 30 30 ILE HG23 H 1 0.69 0.01 . 1 . . . . . . . . 5387 1 394 . 1 1 30 30 ILE CG2 C 13 17.1 0.05 . 1 . . . . . . . . 5387 1 395 . 1 1 30 30 ILE CG1 C 13 31.2 0.05 . 1 . . . . . . . . 5387 1 396 . 1 1 30 30 ILE HG12 H 1 2.02 0.01 . 2 . . . . . . . . 5387 1 397 . 1 1 30 30 ILE HG13 H 1 0.68 0.01 . 2 . . . . . . . . 5387 1 398 . 1 1 30 30 ILE HD11 H 1 0.89 0.01 . 1 . . . . . . . . 5387 1 399 . 1 1 30 30 ILE HD12 H 1 0.89 0.01 . 1 . . . . . . . . 5387 1 400 . 1 1 30 30 ILE HD13 H 1 0.89 0.01 . 1 . . . . . . . . 5387 1 401 . 1 1 30 30 ILE CD1 C 13 15.0 0.05 . 1 . . . . . . . . 5387 1 402 . 1 1 30 30 ILE C C 13 178.2 0.05 . 1 . . . . . . . . 5387 1 403 . 1 1 31 31 GLN N N 15 123.5 0.05 . 1 . . . . . . . . 5387 1 404 . 1 1 31 31 GLN H H 1 8.45 0.01 . 1 . . . . . . . . 5387 1 405 . 1 1 31 31 GLN CA C 13 60.1 0.05 . 1 . . . . . . . . 5387 1 406 . 1 1 31 31 GLN HA H 1 3.84 0.01 . 1 . . . . . . . . 5387 1 407 . 1 1 31 31 GLN CB C 13 27.7 0.05 . 1 . . . . . . . . 5387 1 408 . 1 1 31 31 GLN HB2 H 1 2.50 0.01 . 2 . . . . . . . . 5387 1 409 . 1 1 31 31 GLN HB3 H 1 2.00 0.01 . 2 . . . . . . . . 5387 1 410 . 1 1 31 31 GLN CG C 13 33.9 0.05 . 1 . . . . . . . . 5387 1 411 . 1 1 31 31 GLN HG2 H 1 2.24 0.01 . 2 . . . . . . . . 5387 1 412 . 1 1 31 31 GLN HG3 H 1 1.96 0.01 . 2 . . . . . . . . 5387 1 413 . 1 1 31 31 GLN NE2 N 15 111.3 0.05 . 1 . . . . . . . . 5387 1 414 . 1 1 31 31 GLN HE21 H 1 6.90 0.01 . 2 . . . . . . . . 5387 1 415 . 1 1 31 31 GLN HE22 H 1 7.71 0.01 . 2 . . . . . . . . 5387 1 416 . 1 1 31 31 GLN C C 13 179.1 0.05 . 1 . . . . . . . . 5387 1 417 . 1 1 32 32 ASP N N 15 120.8 0.05 . 1 . . . . . . . . 5387 1 418 . 1 1 32 32 ASP H H 1 8.26 0.01 . 1 . . . . . . . . 5387 1 419 . 1 1 32 32 ASP CA C 13 57.4 0.05 . 1 . . . . . . . . 5387 1 420 . 1 1 32 32 ASP HA H 1 4.29 0.01 . 1 . . . . . . . . 5387 1 421 . 1 1 32 32 ASP CB C 13 41.1 0.05 . 1 . . . . . . . . 5387 1 422 . 1 1 32 32 ASP HB2 H 1 2.85 0.01 . 2 . . . . . . . . 5387 1 423 . 1 1 32 32 ASP HB3 H 1 2.78 0.01 . 2 . . . . . . . . 5387 1 424 . 1 1 32 32 ASP C C 13 177.5 0.05 . 1 . . . . . . . . 5387 1 425 . 1 1 33 33 LYS N N 15 116.2 0.05 . 1 . . . . . . . . 5387 1 426 . 1 1 33 33 LYS H H 1 7.67 0.01 . 1 . . . . . . . . 5387 1 427 . 1 1 33 33 LYS CA C 13 58.6 0.05 . 1 . . . . . . . . 5387 1 428 . 1 1 33 33 LYS HA H 1 4.29 0.01 . 1 . . . . . . . . 5387 1 429 . 1 1 33 33 LYS CB C 13 34.1 0.05 . 1 . . . . . . . . 5387 1 430 . 1 1 33 33 LYS HB2 H 1 1.98 0.01 . 2 . . . . . . . . 5387 1 431 . 1 1 33 33 LYS HB3 H 1 1.85 0.01 . 2 . . . . . . . . 5387 1 432 . 1 1 33 33 LYS CG C 13 25.4 0.05 . 1 . . . . . . . . 5387 1 433 . 1 1 33 33 LYS HG2 H 1 1.60 0.01 . 1 . . . . . . . . 5387 1 434 . 1 1 33 33 LYS HG3 H 1 1.60 0.01 . 1 . . . . . . . . 5387 1 435 . 1 1 33 33 LYS CD C 13 29.2 0.05 . 1 . . . . . . . . 5387 1 436 . 1 1 33 33 LYS HD2 H 1 1.71 0.01 . 1 . . . . . . . . 5387 1 437 . 1 1 33 33 LYS HD3 H 1 1.71 0.01 . 1 . . . . . . . . 5387 1 438 . 1 1 33 33 LYS CE C 13 42.3 0.05 . 1 . . . . . . . . 5387 1 439 . 1 1 33 33 LYS HE2 H 1 3.19 0.01 . 2 . . . . . . . . 5387 1 440 . 1 1 33 33 LYS HE3 H 1 3.15 0.01 . 2 . . . . . . . . 5387 1 441 . 1 1 33 33 LYS C C 13 178.0 0.05 . 1 . . . . . . . . 5387 1 442 . 1 1 34 34 GLU N N 15 113.8 0.05 . 1 . . . . . . . . 5387 1 443 . 1 1 34 34 GLU H H 1 8.64 0.01 . 1 . . . . . . . . 5387 1 444 . 1 1 34 34 GLU CA C 13 55.3 0.05 . 1 . . . . . . . . 5387 1 445 . 1 1 34 34 GLU HA H 1 4.63 0.01 . 1 . . . . . . . . 5387 1 446 . 1 1 34 34 GLU CB C 13 33.1 0.05 . 1 . . . . . . . . 5387 1 447 . 1 1 34 34 GLU HB2 H 1 2.32 0.01 . 2 . . . . . . . . 5387 1 448 . 1 1 34 34 GLU HB3 H 1 1.63 0.01 . 2 . . . . . . . . 5387 1 449 . 1 1 34 34 GLU CG C 13 36.0 0.05 . 1 . . . . . . . . 5387 1 450 . 1 1 34 34 GLU HG2 H 1 2.19 0.01 . 2 . . . . . . . . 5387 1 451 . 1 1 34 34 GLU HG3 H 1 2.07 0.01 . 2 . . . . . . . . 5387 1 452 . 1 1 34 34 GLU C C 13 177.9 0.05 . 1 . . . . . . . . 5387 1 453 . 1 1 35 35 GLY N N 15 109.5 0.05 . 1 . . . . . . . . 5387 1 454 . 1 1 35 35 GLY H H 1 8.51 0.01 . 1 . . . . . . . . 5387 1 455 . 1 1 35 35 GLY CA C 13 46.1 0.05 . 1 . . . . . . . . 5387 1 456 . 1 1 35 35 GLY HA2 H 1 4.18 0.01 . 2 . . . . . . . . 5387 1 457 . 1 1 35 35 GLY HA3 H 1 3.91 0.01 . 2 . . . . . . . . 5387 1 458 . 1 1 35 35 GLY C C 13 174.0 0.05 . 1 . . . . . . . . 5387 1 459 . 1 1 36 36 ILE N N 15 121.1 0.05 . 1 . . . . . . . . 5387 1 460 . 1 1 36 36 ILE H H 1 6.17 0.01 . 1 . . . . . . . . 5387 1 461 . 1 1 36 36 ILE CA C 13 58.1 0.05 . 1 . . . . . . . . 5387 1 462 . 1 1 36 36 ILE HA H 1 4.38 0.01 . 1 . . . . . . . . 5387 1 463 . 1 1 36 36 ILE CB C 13 40.6 0.05 . 1 . . . . . . . . 5387 1 464 . 1 1 36 36 ILE HB H 1 1.40 0.01 . 1 . . . . . . . . 5387 1 465 . 1 1 36 36 ILE HG21 H 1 0.92 0.01 . 1 . . . . . . . . 5387 1 466 . 1 1 36 36 ILE HG22 H 1 0.92 0.01 . 1 . . . . . . . . 5387 1 467 . 1 1 36 36 ILE HG23 H 1 0.92 0.01 . 1 . . . . . . . . 5387 1 468 . 1 1 36 36 ILE CG2 C 13 18.2 0.05 . 1 . . . . . . . . 5387 1 469 . 1 1 36 36 ILE CG1 C 13 27.0 0.05 . 1 . . . . . . . . 5387 1 470 . 1 1 36 36 ILE HG12 H 1 1.36 0.01 . 2 . . . . . . . . 5387 1 471 . 1 1 36 36 ILE HG13 H 1 1.06 0.01 . 2 . . . . . . . . 5387 1 472 . 1 1 36 36 ILE HD11 H 1 0.74 0.01 . 1 . . . . . . . . 5387 1 473 . 1 1 36 36 ILE HD12 H 1 0.74 0.01 . 1 . . . . . . . . 5387 1 474 . 1 1 36 36 ILE HD13 H 1 0.74 0.01 . 1 . . . . . . . . 5387 1 475 . 1 1 36 36 ILE CD1 C 13 13.7 0.05 . 1 . . . . . . . . 5387 1 476 . 1 1 37 37 PRO CD C 13 51.0 0.05 . 1 . . . . . . . . 5387 1 477 . 1 1 37 37 PRO CA C 13 61.6 0.05 . 1 . . . . . . . . 5387 1 478 . 1 1 37 37 PRO HA H 1 4.59 0.01 . 1 . . . . . . . . 5387 1 479 . 1 1 37 37 PRO CB C 13 32.0 0.05 . 1 . . . . . . . . 5387 1 480 . 1 1 37 37 PRO HB2 H 1 2.44 0.01 . 2 . . . . . . . . 5387 1 481 . 1 1 37 37 PRO HB3 H 1 1.93 0.01 . 2 . . . . . . . . 5387 1 482 . 1 1 37 37 PRO CG C 13 28.4 0.05 . 1 . . . . . . . . 5387 1 483 . 1 1 37 37 PRO HG2 H 1 2.17 0.01 . 2 . . . . . . . . 5387 1 484 . 1 1 37 37 PRO HG3 H 1 2.05 0.01 . 2 . . . . . . . . 5387 1 485 . 1 1 37 37 PRO HD2 H 1 4.24 0.01 . 2 . . . . . . . . 5387 1 486 . 1 1 37 37 PRO HD3 H 1 3.69 0.01 . 2 . . . . . . . . 5387 1 487 . 1 1 38 38 PRO CD C 13 51.2 0.05 . 1 . . . . . . . . 5387 1 488 . 1 1 38 38 PRO CA C 13 66.1 0.05 . 1 . . . . . . . . 5387 1 489 . 1 1 38 38 PRO HA H 1 4.15 0.01 . 1 . . . . . . . . 5387 1 490 . 1 1 38 38 PRO CB C 13 32.8 0.05 . 1 . . . . . . . . 5387 1 491 . 1 1 38 38 PRO HB2 H 1 2.23 0.01 . 2 . . . . . . . . 5387 1 492 . 1 1 38 38 PRO HB3 H 1 1.99 0.01 . 2 . . . . . . . . 5387 1 493 . 1 1 38 38 PRO CG C 13 27.8 0.05 . 1 . . . . . . . . 5387 1 494 . 1 1 38 38 PRO HG2 H 1 2.16 0.01 . 2 . . . . . . . . 5387 1 495 . 1 1 38 38 PRO HG3 H 1 1.61 0.01 . 2 . . . . . . . . 5387 1 496 . 1 1 38 38 PRO HD2 H 1 3.76 0.01 . 2 . . . . . . . . 5387 1 497 . 1 1 38 38 PRO HD3 H 1 3.70 0.01 . 2 . . . . . . . . 5387 1 498 . 1 1 38 38 PRO C C 13 178.5 0.05 . 1 . . . . . . . . 5387 1 499 . 1 1 39 39 ASP N N 15 114.1 0.05 . 1 . . . . . . . . 5387 1 500 . 1 1 39 39 ASP H H 1 8.63 0.01 . 1 . . . . . . . . 5387 1 501 . 1 1 39 39 ASP CA C 13 55.9 0.05 . 1 . . . . . . . . 5387 1 502 . 1 1 39 39 ASP HA H 1 4.41 0.01 . 1 . . . . . . . . 5387 1 503 . 1 1 39 39 ASP CB C 13 40.0 0.05 . 1 . . . . . . . . 5387 1 504 . 1 1 39 39 ASP HB2 H 1 2.70 0.01 . 1 . . . . . . . . 5387 1 505 . 1 1 39 39 ASP HB3 H 1 2.70 0.01 . 1 . . . . . . . . 5387 1 506 . 1 1 39 39 ASP C C 13 176.7 0.05 . 1 . . . . . . . . 5387 1 507 . 1 1 40 40 GLN N N 15 116.9 0.05 . 1 . . . . . . . . 5387 1 508 . 1 1 40 40 GLN H H 1 7.85 0.01 . 1 . . . . . . . . 5387 1 509 . 1 1 40 40 GLN CA C 13 55.6 0.05 . 1 . . . . . . . . 5387 1 510 . 1 1 40 40 GLN HA H 1 4.41 0.01 . 1 . . . . . . . . 5387 1 511 . 1 1 40 40 GLN CB C 13 30.4 0.05 . 1 . . . . . . . . 5387 1 512 . 1 1 40 40 GLN HB2 H 1 2.44 0.01 . 2 . . . . . . . . 5387 1 513 . 1 1 40 40 GLN HB3 H 1 1.82 0.01 . 2 . . . . . . . . 5387 1 514 . 1 1 40 40 GLN CG C 13 35.6 0.05 . 1 . . . . . . . . 5387 1 515 . 1 1 40 40 GLN HG2 H 1 2.42 0.01 . 2 . . . . . . . . 5387 1 516 . 1 1 40 40 GLN HG3 H 1 2.36 0.01 . 2 . . . . . . . . 5387 1 517 . 1 1 40 40 GLN NE2 N 15 110.1 0.05 . 1 . . . . . . . . 5387 1 518 . 1 1 40 40 GLN HE21 H 1 6.71 0.01 . 2 . . . . . . . . 5387 1 519 . 1 1 40 40 GLN HE22 H 1 7.35 0.01 . 2 . . . . . . . . 5387 1 520 . 1 1 40 40 GLN C C 13 174.7 0.05 . 1 . . . . . . . . 5387 1 521 . 1 1 41 41 GLN N N 15 117.1 0.05 . 1 . . . . . . . . 5387 1 522 . 1 1 41 41 GLN H H 1 7.47 0.01 . 1 . . . . . . . . 5387 1 523 . 1 1 41 41 GLN CA C 13 56.5 0.05 . 1 . . . . . . . . 5387 1 524 . 1 1 41 41 GLN HA H 1 4.16 0.01 . 1 . . . . . . . . 5387 1 525 . 1 1 41 41 GLN CB C 13 31.2 0.05 . 1 . . . . . . . . 5387 1 526 . 1 1 41 41 GLN HB2 H 1 1.96 0.01 . 2 . . . . . . . . 5387 1 527 . 1 1 41 41 GLN HB3 H 1 1.80 0.01 . 2 . . . . . . . . 5387 1 528 . 1 1 41 41 GLN CG C 13 33.3 0.05 . 1 . . . . . . . . 5387 1 529 . 1 1 41 41 GLN HG2 H 1 2.51 0.01 . 2 . . . . . . . . 5387 1 530 . 1 1 41 41 GLN HG3 H 1 1.61 0.01 . 2 . . . . . . . . 5387 1 531 . 1 1 41 41 GLN NE2 N 15 104.5 0.05 . 1 . . . . . . . . 5387 1 532 . 1 1 41 41 GLN HE21 H 1 5.93 0.01 . 2 . . . . . . . . 5387 1 533 . 1 1 41 41 GLN HE22 H 1 6.45 0.01 . 2 . . . . . . . . 5387 1 534 . 1 1 41 41 GLN C C 13 176.1 0.05 . 1 . . . . . . . . 5387 1 535 . 1 1 42 42 ARG N N 15 122.0 0.05 . 1 . . . . . . . . 5387 1 536 . 1 1 42 42 ARG H H 1 8.31 0.01 . 1 . . . . . . . . 5387 1 537 . 1 1 42 42 ARG CA C 13 55.1 0.05 . 1 . . . . . . . . 5387 1 538 . 1 1 42 42 ARG HA H 1 4.59 0.01 . 1 . . . . . . . . 5387 1 539 . 1 1 42 42 ARG CB C 13 31.3 0.05 . 1 . . . . . . . . 5387 1 540 . 1 1 42 42 ARG HB2 H 1 1.98 0.01 . 2 . . . . . . . . 5387 1 541 . 1 1 42 42 ARG HB3 H 1 1.55 0.01 . 2 . . . . . . . . 5387 1 542 . 1 1 42 42 ARG CG C 13 27.2 0.05 . 1 . . . . . . . . 5387 1 543 . 1 1 42 42 ARG HG2 H 1 1.55 0.01 . 1 . . . . . . . . 5387 1 544 . 1 1 42 42 ARG HG3 H 1 1.55 0.01 . 1 . . . . . . . . 5387 1 545 . 1 1 42 42 ARG CD C 13 43.9 0.05 . 1 . . . . . . . . 5387 1 546 . 1 1 42 42 ARG HD2 H 1 3.08 0.01 . 2 . . . . . . . . 5387 1 547 . 1 1 42 42 ARG HD3 H 1 2.75 0.01 . 2 . . . . . . . . 5387 1 548 . 1 1 42 42 ARG NE N 15 84.0 0.05 . 1 . . . . . . . . 5387 1 549 . 1 1 42 42 ARG HE H 1 7.68 0.01 . 1 . . . . . . . . 5387 1 550 . 1 1 42 42 ARG CZ C 13 159.3 0.05 . 1 . . . . . . . . 5387 1 551 . 1 1 42 42 ARG C C 13 174.8 0.05 . 1 . . . . . . . . 5387 1 552 . 1 1 43 43 LEU N N 15 123.2 0.05 . 1 . . . . . . . . 5387 1 553 . 1 1 43 43 LEU H H 1 8.64 0.01 . 1 . . . . . . . . 5387 1 554 . 1 1 43 43 LEU CA C 13 53.0 0.05 . 1 . . . . . . . . 5387 1 555 . 1 1 43 43 LEU HA H 1 5.42 0.01 . 1 . . . . . . . . 5387 1 556 . 1 1 43 43 LEU CB C 13 45.5 0.05 . 1 . . . . . . . . 5387 1 557 . 1 1 43 43 LEU HB2 H 1 1.52 0.01 . 2 . . . . . . . . 5387 1 558 . 1 1 43 43 LEU HB3 H 1 1.14 0.01 . 2 . . . . . . . . 5387 1 559 . 1 1 43 43 LEU CG C 13 27.1 0.05 . 1 . . . . . . . . 5387 1 560 . 1 1 43 43 LEU HG H 1 1.46 0.01 . 1 . . . . . . . . 5387 1 561 . 1 1 43 43 LEU HD11 H 1 0.75 0.01 . 2 . . . . . . . . 5387 1 562 . 1 1 43 43 LEU HD12 H 1 0.75 0.01 . 2 . . . . . . . . 5387 1 563 . 1 1 43 43 LEU HD13 H 1 0.75 0.01 . 2 . . . . . . . . 5387 1 564 . 1 1 43 43 LEU HD21 H 1 0.80 0.01 . 2 . . . . . . . . 5387 1 565 . 1 1 43 43 LEU HD22 H 1 0.80 0.01 . 2 . . . . . . . . 5387 1 566 . 1 1 43 43 LEU HD23 H 1 0.80 0.01 . 2 . . . . . . . . 5387 1 567 . 1 1 43 43 LEU CD1 C 13 26.8 0.05 . 1 . . . . . . . . 5387 1 568 . 1 1 43 43 LEU CD2 C 13 24.5 0.05 . 1 . . . . . . . . 5387 1 569 . 1 1 43 43 LEU C C 13 175.5 0.05 . 1 . . . . . . . . 5387 1 570 . 1 1 44 44 ILE N N 15 123.1 0.05 . 1 . . . . . . . . 5387 1 571 . 1 1 44 44 ILE H H 1 9.28 0.01 . 1 . . . . . . . . 5387 1 572 . 1 1 44 44 ILE CA C 13 59.3 0.05 . 1 . . . . . . . . 5387 1 573 . 1 1 44 44 ILE HA H 1 5.11 0.01 . 1 . . . . . . . . 5387 1 574 . 1 1 44 44 ILE CB C 13 42.1 0.05 . 1 . . . . . . . . 5387 1 575 . 1 1 44 44 ILE HB H 1 1.64 0.01 . 1 . . . . . . . . 5387 1 576 . 1 1 44 44 ILE HG21 H 1 0.77 0.01 . 1 . . . . . . . . 5387 1 577 . 1 1 44 44 ILE HG22 H 1 0.77 0.01 . 1 . . . . . . . . 5387 1 578 . 1 1 44 44 ILE HG23 H 1 0.77 0.01 . 1 . . . . . . . . 5387 1 579 . 1 1 44 44 ILE CG2 C 13 17.9 0.05 . 1 . . . . . . . . 5387 1 580 . 1 1 44 44 ILE CG1 C 13 28.6 0.05 . 1 . . . . . . . . 5387 1 581 . 1 1 44 44 ILE HG12 H 1 1.35 0.01 . 2 . . . . . . . . 5387 1 582 . 1 1 44 44 ILE HG13 H 1 0.94 0.01 . 2 . . . . . . . . 5387 1 583 . 1 1 44 44 ILE HD11 H 1 0.69 0.01 . 1 . . . . . . . . 5387 1 584 . 1 1 44 44 ILE HD12 H 1 0.69 0.01 . 1 . . . . . . . . 5387 1 585 . 1 1 44 44 ILE HD13 H 1 0.69 0.01 . 1 . . . . . . . . 5387 1 586 . 1 1 44 44 ILE CD1 C 13 14.2 0.05 . 1 . . . . . . . . 5387 1 587 . 1 1 44 44 ILE C C 13 175.4 0.05 . 1 . . . . . . . . 5387 1 588 . 1 1 45 45 PHE N N 15 125.5 0.05 . 1 . . . . . . . . 5387 1 589 . 1 1 45 45 PHE H H 1 8.76 0.01 . 1 . . . . . . . . 5387 1 590 . 1 1 45 45 PHE CA C 13 57.8 0.05 . 1 . . . . . . . . 5387 1 591 . 1 1 45 45 PHE HA H 1 4.94 0.01 . 1 . . . . . . . . 5387 1 592 . 1 1 45 45 PHE CB C 13 44.4 0.05 . 1 . . . . . . . . 5387 1 593 . 1 1 45 45 PHE HB2 H 1 3.17 0.01 . 2 . . . . . . . . 5387 1 594 . 1 1 45 45 PHE HB3 H 1 2.72 0.01 . 2 . . . . . . . . 5387 1 595 . 1 1 45 45 PHE HD1 H 1 7.35 0.01 . 1 . . . . . . . . 5387 1 596 . 1 1 45 45 PHE HD2 H 1 7.35 0.01 . 1 . . . . . . . . 5387 1 597 . 1 1 45 45 PHE HE1 H 1 7.54 0.01 . 1 . . . . . . . . 5387 1 598 . 1 1 45 45 PHE HE2 H 1 7.54 0.01 . 1 . . . . . . . . 5387 1 599 . 1 1 45 45 PHE CD1 C 13 132.4 0.05 . 1 . . . . . . . . 5387 1 600 . 1 1 45 45 PHE CE1 C 13 132.4 0.05 . 1 . . . . . . . . 5387 1 601 . 1 1 45 45 PHE CZ C 13 130.1 0.05 . 1 . . . . . . . . 5387 1 602 . 1 1 45 45 PHE HZ H 1 7.47 0.01 . 1 . . . . . . . . 5387 1 603 . 1 1 45 45 PHE C C 13 173.9 0.05 . 1 . . . . . . . . 5387 1 604 . 1 1 46 46 ALA N N 15 131.4 0.05 . 1 . . . . . . . . 5387 1 605 . 1 1 46 46 ALA H H 1 8.45 0.01 . 1 . . . . . . . . 5387 1 606 . 1 1 46 46 ALA CA C 13 52.5 0.05 . 1 . . . . . . . . 5387 1 607 . 1 1 46 46 ALA HA H 1 3.73 0.01 . 1 . . . . . . . . 5387 1 608 . 1 1 46 46 ALA HB1 H 1 0.99 0.01 . 1 . . . . . . . . 5387 1 609 . 1 1 46 46 ALA HB2 H 1 0.99 0.01 . 1 . . . . . . . . 5387 1 610 . 1 1 46 46 ALA HB3 H 1 0.99 0.01 . 1 . . . . . . . . 5387 1 611 . 1 1 46 46 ALA CB C 13 17.0 0.05 . 1 . . . . . . . . 5387 1 612 . 1 1 46 46 ALA C C 13 177.0 0.05 . 1 . . . . . . . . 5387 1 613 . 1 1 47 47 GLY N N 15 102.4 0.05 . 1 . . . . . . . . 5387 1 614 . 1 1 47 47 GLY H H 1 8.11 0.01 . 1 . . . . . . . . 5387 1 615 . 1 1 47 47 GLY CA C 13 46.0 0.05 . 1 . . . . . . . . 5387 1 616 . 1 1 47 47 GLY HA2 H 1 3.99 0.01 . 2 . . . . . . . . 5387 1 617 . 1 1 47 47 GLY HA3 H 1 3.32 0.01 . 2 . . . . . . . . 5387 1 618 . 1 1 47 47 GLY C C 13 171.8 0.05 . 1 . . . . . . . . 5387 1 619 . 1 1 48 48 LYS N N 15 115.3 0.05 . 1 . . . . . . . . 5387 1 620 . 1 1 48 48 LYS H H 1 7.49 0.01 . 1 . . . . . . . . 5387 1 621 . 1 1 48 48 LYS CA C 13 53.8 0.05 . 1 . . . . . . . . 5387 1 622 . 1 1 48 48 LYS HA H 1 4.80 0.01 . 1 . . . . . . . . 5387 1 623 . 1 1 48 48 LYS CB C 13 35.2 0.05 . 1 . . . . . . . . 5387 1 624 . 1 1 48 48 LYS HB2 H 1 1.82 0.01 . 1 . . . . . . . . 5387 1 625 . 1 1 48 48 LYS HB3 H 1 1.82 0.01 . 1 . . . . . . . . 5387 1 626 . 1 1 48 48 LYS CG C 13 24.0 0.05 . 1 . . . . . . . . 5387 1 627 . 1 1 48 48 LYS HG2 H 1 1.53 0.01 . 1 . . . . . . . . 5387 1 628 . 1 1 48 48 LYS HG3 H 1 1.53 0.01 . 1 . . . . . . . . 5387 1 629 . 1 1 48 48 LYS CD C 13 29.1 0.05 . 1 . . . . . . . . 5387 1 630 . 1 1 48 48 LYS HD2 H 1 1.91 0.01 . 2 . . . . . . . . 5387 1 631 . 1 1 48 48 LYS HD3 H 1 1.86 0.01 . 2 . . . . . . . . 5387 1 632 . 1 1 48 48 LYS CE C 13 42.5 0.05 . 1 . . . . . . . . 5387 1 633 . 1 1 48 48 LYS HE2 H 1 3.24 0.01 . 2 . . . . . . . . 5387 1 634 . 1 1 48 48 LYS HE3 H 1 3.18 0.01 . 2 . . . . . . . . 5387 1 635 . 1 1 48 48 LYS C C 13 175.7 0.05 . 1 . . . . . . . . 5387 1 636 . 1 1 49 49 GLN N N 15 119.3 0.05 . 1 . . . . . . . . 5387 1 637 . 1 1 49 49 GLN H H 1 8.32 0.01 . 1 . . . . . . . . 5387 1 638 . 1 1 49 49 GLN CA C 13 55.9 0.05 . 1 . . . . . . . . 5387 1 639 . 1 1 49 49 GLN HA H 1 4.68 0.01 . 1 . . . . . . . . 5387 1 640 . 1 1 49 49 GLN CB C 13 29.9 0.05 . 1 . . . . . . . . 5387 1 641 . 1 1 49 49 GLN HB2 H 1 2.06 0.01 . 2 . . . . . . . . 5387 1 642 . 1 1 49 49 GLN HB3 H 1 1.97 0.01 . 2 . . . . . . . . 5387 1 643 . 1 1 49 49 GLN CG C 13 36.3 0.05 . 1 . . . . . . . . 5387 1 644 . 1 1 49 49 GLN HG2 H 1 2.41 0.01 . 2 . . . . . . . . 5387 1 645 . 1 1 49 49 GLN HG3 H 1 2.00 0.01 . 2 . . . . . . . . 5387 1 646 . 1 1 49 49 GLN NE2 N 15 111.9 0.05 . 1 . . . . . . . . 5387 1 647 . 1 1 49 49 GLN HE21 H 1 6.88 0.01 . 2 . . . . . . . . 5387 1 648 . 1 1 49 49 GLN HE22 H 1 7.58 0.01 . 2 . . . . . . . . 5387 1 649 . 1 1 49 49 GLN C C 13 176.1 0.05 . 1 . . . . . . . . 5387 1 650 . 1 1 50 50 LEU N N 15 124.9 0.05 . 1 . . . . . . . . 5387 1 651 . 1 1 50 50 LEU H H 1 8.71 0.01 . 1 . . . . . . . . 5387 1 652 . 1 1 50 50 LEU CA C 13 54.5 0.05 . 1 . . . . . . . . 5387 1 653 . 1 1 50 50 LEU HA H 1 4.05 0.01 . 1 . . . . . . . . 5387 1 654 . 1 1 50 50 LEU CB C 13 41.6 0.05 . 1 . . . . . . . . 5387 1 655 . 1 1 50 50 LEU HB2 H 1 1.43 0.01 . 2 . . . . . . . . 5387 1 656 . 1 1 50 50 LEU HB3 H 1 1.04 0.01 . 2 . . . . . . . . 5387 1 657 . 1 1 50 50 LEU CG C 13 25.7 0.05 . 1 . . . . . . . . 5387 1 658 . 1 1 50 50 LEU HG H 1 1.50 0.01 . 1 . . . . . . . . 5387 1 659 . 1 1 50 50 LEU HD11 H 1 0.51 0.01 . 2 . . . . . . . . 5387 1 660 . 1 1 50 50 LEU HD12 H 1 0.51 0.01 . 2 . . . . . . . . 5387 1 661 . 1 1 50 50 LEU HD13 H 1 0.51 0.01 . 2 . . . . . . . . 5387 1 662 . 1 1 50 50 LEU HD21 H 1 -0.17 0.01 . 2 . . . . . . . . 5387 1 663 . 1 1 50 50 LEU HD22 H 1 -0.17 0.01 . 2 . . . . . . . . 5387 1 664 . 1 1 50 50 LEU HD23 H 1 -0.17 0.01 . 2 . . . . . . . . 5387 1 665 . 1 1 50 50 LEU CD1 C 13 26.0 0.05 . 1 . . . . . . . . 5387 1 666 . 1 1 50 50 LEU CD2 C 13 19.3 0.05 . 1 . . . . . . . . 5387 1 667 . 1 1 50 50 LEU C C 13 176.7 0.05 . 1 . . . . . . . . 5387 1 668 . 1 1 51 51 GLU N N 15 124.0 0.05 . 1 . . . . . . . . 5387 1 669 . 1 1 51 51 GLU H H 1 8.58 0.01 . 1 . . . . . . . . 5387 1 670 . 1 1 51 51 GLU CA C 13 56.3 0.05 . 1 . . . . . . . . 5387 1 671 . 1 1 51 51 GLU HA H 1 4.41 0.01 . 1 . . . . . . . . 5387 1 672 . 1 1 51 51 GLU CB C 13 31.7 0.05 . 1 . . . . . . . . 5387 1 673 . 1 1 51 51 GLU HB2 H 1 2.24 0.01 . 2 . . . . . . . . 5387 1 674 . 1 1 51 51 GLU HB3 H 1 2.03 0.01 . 2 . . . . . . . . 5387 1 675 . 1 1 51 51 GLU CG C 13 36.7 0.05 . 1 . . . . . . . . 5387 1 676 . 1 1 51 51 GLU HG2 H 1 2.48 0.01 . 2 . . . . . . . . 5387 1 677 . 1 1 51 51 GLU HG3 H 1 2.37 0.01 . 2 . . . . . . . . 5387 1 678 . 1 1 51 51 GLU C C 13 176.3 0.05 . 1 . . . . . . . . 5387 1 679 . 1 1 52 52 ASP N N 15 121.3 0.05 . 1 . . . . . . . . 5387 1 680 . 1 1 52 52 ASP H H 1 8.18 0.01 . 1 . . . . . . . . 5387 1 681 . 1 1 52 52 ASP CA C 13 57.2 0.05 . 1 . . . . . . . . 5387 1 682 . 1 1 52 52 ASP HA H 1 4.33 0.01 . 1 . . . . . . . . 5387 1 683 . 1 1 52 52 ASP CB C 13 41.1 0.05 . 1 . . . . . . . . 5387 1 684 . 1 1 52 52 ASP HB2 H 1 2.58 0.01 . 1 . . . . . . . . 5387 1 685 . 1 1 52 52 ASP HB3 H 1 2.58 0.01 . 1 . . . . . . . . 5387 1 686 . 1 1 53 53 GLY H H 1 9.01 0.01 . 1 . . . . . . . . 5387 1 687 . 1 1 53 53 GLY CA C 13 45.4 0.05 . 1 . . . . . . . . 5387 1 688 . 1 1 53 53 GLY HA2 H 1 4.20 0.01 . 2 . . . . . . . . 5387 1 689 . 1 1 53 53 GLY HA3 H 1 3.88 0.01 . 2 . . . . . . . . 5387 1 690 . 1 1 53 53 GLY C C 13 175.0 0.05 . 1 . . . . . . . . 5387 1 691 . 1 1 54 54 ARG N N 15 119.8 0.05 . 1 . . . . . . . . 5387 1 692 . 1 1 54 54 ARG H H 1 7.50 0.01 . 1 . . . . . . . . 5387 1 693 . 1 1 54 54 ARG CA C 13 54.6 0.05 . 1 . . . . . . . . 5387 1 694 . 1 1 54 54 ARG HA H 1 4.65 0.01 . 1 . . . . . . . . 5387 1 695 . 1 1 54 54 ARG CB C 13 32.6 0.05 . 1 . . . . . . . . 5387 1 696 . 1 1 54 54 ARG HB2 H 1 2.17 0.01 . 2 . . . . . . . . 5387 1 697 . 1 1 54 54 ARG HB3 H 1 2.02 0.01 . 2 . . . . . . . . 5387 1 698 . 1 1 54 54 ARG CG C 13 27.8 0.05 . 1 . . . . . . . . 5387 1 699 . 1 1 54 54 ARG HG2 H 1 1.80 0.01 . 2 . . . . . . . . 5387 1 700 . 1 1 54 54 ARG HG3 H 1 1.61 0.01 . 2 . . . . . . . . 5387 1 701 . 1 1 54 54 ARG CD C 13 43.0 0.05 . 1 . . . . . . . . 5387 1 702 . 1 1 54 54 ARG HD2 H 1 3.12 0.01 . 2 . . . . . . . . 5387 1 703 . 1 1 54 54 ARG HD3 H 1 3.04 0.01 . 2 . . . . . . . . 5387 1 704 . 1 1 54 54 ARG NE N 15 85.2 0.05 . 1 . . . . . . . . 5387 1 705 . 1 1 54 54 ARG HE H 1 7.02 0.01 . 1 . . . . . . . . 5387 1 706 . 1 1 54 54 ARG CZ C 13 159.5 0.05 . 1 . . . . . . . . 5387 1 707 . 1 1 54 54 ARG C C 13 175.2 0.05 . 1 . . . . . . . . 5387 1 708 . 1 1 55 55 THR N N 15 108.6 0.05 . 1 . . . . . . . . 5387 1 709 . 1 1 55 55 THR H H 1 8.83 0.01 . 1 . . . . . . . . 5387 1 710 . 1 1 55 55 THR CA C 13 59.7 0.05 . 1 . . . . . . . . 5387 1 711 . 1 1 55 55 THR HA H 1 5.21 0.01 . 1 . . . . . . . . 5387 1 712 . 1 1 55 55 THR CB C 13 72.3 0.05 . 1 . . . . . . . . 5387 1 713 . 1 1 55 55 THR HB H 1 4.57 0.01 . 1 . . . . . . . . 5387 1 714 . 1 1 55 55 THR HG21 H 1 1.13 0.01 . 1 . . . . . . . . 5387 1 715 . 1 1 55 55 THR HG22 H 1 1.13 0.01 . 1 . . . . . . . . 5387 1 716 . 1 1 55 55 THR HG23 H 1 1.13 0.01 . 1 . . . . . . . . 5387 1 717 . 1 1 55 55 THR CG2 C 13 22.5 0.05 . 1 . . . . . . . . 5387 1 718 . 1 1 55 55 THR C C 13 176.4 0.05 . 1 . . . . . . . . 5387 1 719 . 1 1 56 56 LEU N N 15 118.4 0.05 . 1 . . . . . . . . 5387 1 720 . 1 1 56 56 LEU H H 1 8.16 0.01 . 1 . . . . . . . . 5387 1 721 . 1 1 56 56 LEU CA C 13 58.7 0.05 . 1 . . . . . . . . 5387 1 722 . 1 1 56 56 LEU HA H 1 4.05 0.01 . 1 . . . . . . . . 5387 1 723 . 1 1 56 56 LEU CB C 13 40.2 0.05 . 1 . . . . . . . . 5387 1 724 . 1 1 56 56 LEU HB2 H 1 2.10 0.01 . 2 . . . . . . . . 5387 1 725 . 1 1 56 56 LEU HB3 H 1 1.21 0.01 . 2 . . . . . . . . 5387 1 726 . 1 1 56 56 LEU CG C 13 26.9 0.05 . 1 . . . . . . . . 5387 1 727 . 1 1 56 56 LEU HG H 1 1.70 0.01 . 1 . . . . . . . . 5387 1 728 . 1 1 56 56 LEU HD11 H 1 0.74 0.01 . 2 . . . . . . . . 5387 1 729 . 1 1 56 56 LEU HD12 H 1 0.74 0.01 . 2 . . . . . . . . 5387 1 730 . 1 1 56 56 LEU HD13 H 1 0.74 0.01 . 2 . . . . . . . . 5387 1 731 . 1 1 56 56 LEU HD21 H 1 0.61 0.01 . 2 . . . . . . . . 5387 1 732 . 1 1 56 56 LEU HD22 H 1 0.61 0.01 . 2 . . . . . . . . 5387 1 733 . 1 1 56 56 LEU HD23 H 1 0.61 0.01 . 2 . . . . . . . . 5387 1 734 . 1 1 56 56 LEU CD1 C 13 26.9 0.05 . 1 . . . . . . . . 5387 1 735 . 1 1 56 56 LEU CD2 C 13 23.5 0.05 . 1 . . . . . . . . 5387 1 736 . 1 1 56 56 LEU C C 13 180.7 0.05 . 1 . . . . . . . . 5387 1 737 . 1 1 57 57 SER N N 15 113.4 0.05 . 1 . . . . . . . . 5387 1 738 . 1 1 57 57 SER H H 1 8.51 0.01 . 1 . . . . . . . . 5387 1 739 . 1 1 57 57 SER CA C 13 60.9 0.05 . 1 . . . . . . . . 5387 1 740 . 1 1 57 57 SER HA H 1 4.25 0.01 . 1 . . . . . . . . 5387 1 741 . 1 1 57 57 SER CB C 13 62.6 0.05 . 1 . . . . . . . . 5387 1 742 . 1 1 57 57 SER HB2 H 1 3.87 0.01 . 2 . . . . . . . . 5387 1 743 . 1 1 57 57 SER HB3 H 1 3.75 0.01 . 2 . . . . . . . . 5387 1 744 . 1 1 57 57 SER C C 13 178.5 0.05 . 1 . . . . . . . . 5387 1 745 . 1 1 58 58 ASP N N 15 124.9 0.05 . 1 . . . . . . . . 5387 1 746 . 1 1 58 58 ASP H H 1 8.02 0.01 . 1 . . . . . . . . 5387 1 747 . 1 1 58 58 ASP CA C 13 57.4 0.05 . 1 . . . . . . . . 5387 1 748 . 1 1 58 58 ASP HA H 1 4.28 0.01 . 1 . . . . . . . . 5387 1 749 . 1 1 58 58 ASP CB C 13 40.4 0.05 . 1 . . . . . . . . 5387 1 750 . 1 1 58 58 ASP HB2 H 1 3.02 0.01 . 2 . . . . . . . . 5387 1 751 . 1 1 58 58 ASP HB3 H 1 2.30 0.01 . 2 . . . . . . . . 5387 1 752 . 1 1 58 58 ASP C C 13 177.5 0.05 . 1 . . . . . . . . 5387 1 753 . 1 1 59 59 TYR N N 15 116.0 0.05 . 1 . . . . . . . . 5387 1 754 . 1 1 59 59 TYR H H 1 7.27 0.01 . 1 . . . . . . . . 5387 1 755 . 1 1 59 59 TYR CA C 13 58.4 0.05 . 1 . . . . . . . . 5387 1 756 . 1 1 59 59 TYR HA H 1 4.69 0.01 . 1 . . . . . . . . 5387 1 757 . 1 1 59 59 TYR CB C 13 40.1 0.05 . 1 . . . . . . . . 5387 1 758 . 1 1 59 59 TYR HB2 H 1 3.50 0.01 . 2 . . . . . . . . 5387 1 759 . 1 1 59 59 TYR HB3 H 1 2.54 0.01 . 2 . . . . . . . . 5387 1 760 . 1 1 59 59 TYR HD1 H 1 7.24 0.01 . 1 . . . . . . . . 5387 1 761 . 1 1 59 59 TYR HD2 H 1 7.24 0.01 . 1 . . . . . . . . 5387 1 762 . 1 1 59 59 TYR HE1 H 1 6.89 0.01 . 1 . . . . . . . . 5387 1 763 . 1 1 59 59 TYR HE2 H 1 6.89 0.01 . 1 . . . . . . . . 5387 1 764 . 1 1 59 59 TYR CD1 C 13 133.5 0.05 . 1 . . . . . . . . 5387 1 765 . 1 1 59 59 TYR CE1 C 13 118.6 0.05 . 1 . . . . . . . . 5387 1 766 . 1 1 59 59 TYR C C 13 174.5 0.05 . 1 . . . . . . . . 5387 1 767 . 1 1 60 60 ASN N N 15 115.8 0.05 . 1 . . . . . . . . 5387 1 768 . 1 1 60 60 ASN H H 1 8.15 0.01 . 1 . . . . . . . . 5387 1 769 . 1 1 60 60 ASN CA C 13 54.3 0.05 . 1 . . . . . . . . 5387 1 770 . 1 1 60 60 ASN HA H 1 4.38 0.01 . 1 . . . . . . . . 5387 1 771 . 1 1 60 60 ASN CB C 13 37.3 0.05 . 1 . . . . . . . . 5387 1 772 . 1 1 60 60 ASN HB2 H 1 3.26 0.01 . 2 . . . . . . . . 5387 1 773 . 1 1 60 60 ASN HB3 H 1 2.93 0.01 . 2 . . . . . . . . 5387 1 774 . 1 1 60 60 ASN ND2 N 15 113.2 0.05 . 1 . . . . . . . . 5387 1 775 . 1 1 60 60 ASN HD21 H 1 7.57 0.01 . 2 . . . . . . . . 5387 1 776 . 1 1 60 60 ASN HD22 H 1 6.91 0.01 . 2 . . . . . . . . 5387 1 777 . 1 1 60 60 ASN C C 13 174.3 0.05 . 1 . . . . . . . . 5387 1 778 . 1 1 61 61 ILE N N 15 119.2 0.05 . 1 . . . . . . . . 5387 1 779 . 1 1 61 61 ILE H H 1 7.40 0.01 . 1 . . . . . . . . 5387 1 780 . 1 1 61 61 ILE CA C 13 62.7 0.05 . 1 . . . . . . . . 5387 1 781 . 1 1 61 61 ILE HA H 1 3.40 0.01 . 1 . . . . . . . . 5387 1 782 . 1 1 61 61 ILE CB C 13 36.8 0.05 . 1 . . . . . . . . 5387 1 783 . 1 1 61 61 ILE HB H 1 1.38 0.01 . 1 . . . . . . . . 5387 1 784 . 1 1 61 61 ILE HG21 H 1 0.47 0.01 . 1 . . . . . . . . 5387 1 785 . 1 1 61 61 ILE HG22 H 1 0.47 0.01 . 1 . . . . . . . . 5387 1 786 . 1 1 61 61 ILE HG23 H 1 0.47 0.01 . 1 . . . . . . . . 5387 1 787 . 1 1 61 61 ILE CG2 C 13 17.6 0.05 . 1 . . . . . . . . 5387 1 788 . 1 1 61 61 ILE CG1 C 13 28.5 0.05 . 1 . . . . . . . . 5387 1 789 . 1 1 61 61 ILE HG12 H 1 1.16 0.01 . 2 . . . . . . . . 5387 1 790 . 1 1 61 61 ILE HG13 H 1 -0.40 0.01 . 2 . . . . . . . . 5387 1 791 . 1 1 61 61 ILE HD11 H 1 0.43 0.01 . 1 . . . . . . . . 5387 1 792 . 1 1 61 61 ILE HD12 H 1 0.43 0.01 . 1 . . . . . . . . 5387 1 793 . 1 1 61 61 ILE HD13 H 1 0.43 0.01 . 1 . . . . . . . . 5387 1 794 . 1 1 61 61 ILE CD1 C 13 14.8 0.05 . 1 . . . . . . . . 5387 1 795 . 1 1 61 61 ILE C C 13 174.4 0.05 . 1 . . . . . . . . 5387 1 796 . 1 1 62 62 GLN N N 15 125.4 0.05 . 1 . . . . . . . . 5387 1 797 . 1 1 62 62 GLN H H 1 7.71 0.01 . 1 . . . . . . . . 5387 1 798 . 1 1 62 62 GLN CA C 13 53.8 0.05 . 1 . . . . . . . . 5387 1 799 . 1 1 62 62 GLN HA H 1 4.50 0.01 . 1 . . . . . . . . 5387 1 800 . 1 1 62 62 GLN CB C 13 32.0 0.05 . 1 . . . . . . . . 5387 1 801 . 1 1 62 62 GLN HB2 H 1 2.22 0.01 . 2 . . . . . . . . 5387 1 802 . 1 1 62 62 GLN HB3 H 1 1.91 0.01 . 2 . . . . . . . . 5387 1 803 . 1 1 62 62 GLN CG C 13 33.7 0.05 . 1 . . . . . . . . 5387 1 804 . 1 1 62 62 GLN HG2 H 1 2.32 0.01 . 1 . . . . . . . . 5387 1 805 . 1 1 62 62 GLN HG3 H 1 2.32 0.01 . 1 . . . . . . . . 5387 1 806 . 1 1 62 62 GLN NE2 N 15 112.8 0.05 . 1 . . . . . . . . 5387 1 807 . 1 1 62 62 GLN HE21 H 1 6.90 0.01 . 2 . . . . . . . . 5387 1 808 . 1 1 62 62 GLN HE22 H 1 7.36 0.01 . 2 . . . . . . . . 5387 1 809 . 1 1 62 62 GLN C C 13 175.5 0.05 . 1 . . . . . . . . 5387 1 810 . 1 1 63 63 LYS N N 15 120.7 0.05 . 1 . . . . . . . . 5387 1 811 . 1 1 63 63 LYS H H 1 8.45 0.01 . 1 . . . . . . . . 5387 1 812 . 1 1 63 63 LYS CA C 13 58.1 0.05 . 1 . . . . . . . . 5387 1 813 . 1 1 63 63 LYS HA H 1 3.94 0.01 . 1 . . . . . . . . 5387 1 814 . 1 1 63 63 LYS CB C 13 32.7 0.05 . 1 . . . . . . . . 5387 1 815 . 1 1 63 63 LYS HB2 H 1 2.04 0.01 . 2 . . . . . . . . 5387 1 816 . 1 1 63 63 LYS HB3 H 1 1.89 0.01 . 2 . . . . . . . . 5387 1 817 . 1 1 63 63 LYS CG C 13 24.3 0.05 . 1 . . . . . . . . 5387 1 818 . 1 1 63 63 LYS HG2 H 1 1.48 0.01 . 1 . . . . . . . . 5387 1 819 . 1 1 63 63 LYS HG3 H 1 1.48 0.01 . 1 . . . . . . . . 5387 1 820 . 1 1 63 63 LYS CD C 13 29.9 0.05 . 1 . . . . . . . . 5387 1 821 . 1 1 63 63 LYS HD2 H 1 1.76 0.01 . 1 . . . . . . . . 5387 1 822 . 1 1 63 63 LYS HD3 H 1 1.76 0.01 . 1 . . . . . . . . 5387 1 823 . 1 1 63 63 LYS CE C 13 42.3 0.05 . 1 . . . . . . . . 5387 1 824 . 1 1 63 63 LYS HE2 H 1 3.06 0.01 . 1 . . . . . . . . 5387 1 825 . 1 1 63 63 LYS HE3 H 1 3.06 0.01 . 1 . . . . . . . . 5387 1 826 . 1 1 63 63 LYS C C 13 176.0 0.05 . 1 . . . . . . . . 5387 1 827 . 1 1 64 64 GLU N N 15 115.4 0.05 . 1 . . . . . . . . 5387 1 828 . 1 1 64 64 GLU H H 1 9.35 0.01 . 1 . . . . . . . . 5387 1 829 . 1 1 64 64 GLU CA C 13 58.4 0.05 . 1 . . . . . . . . 5387 1 830 . 1 1 64 64 GLU HA H 1 3.36 0.01 . 1 . . . . . . . . 5387 1 831 . 1 1 64 64 GLU CB C 13 26.2 0.05 . 1 . . . . . . . . 5387 1 832 . 1 1 64 64 GLU HB2 H 1 2.54 0.01 . 2 . . . . . . . . 5387 1 833 . 1 1 64 64 GLU HB3 H 1 2.39 0.01 . 2 . . . . . . . . 5387 1 834 . 1 1 64 64 GLU CG C 13 37.4 0.05 . 1 . . . . . . . . 5387 1 835 . 1 1 64 64 GLU HG2 H 1 2.28 0.01 . 2 . . . . . . . . 5387 1 836 . 1 1 64 64 GLU HG3 H 1 2.21 0.01 . 2 . . . . . . . . 5387 1 837 . 1 1 64 64 GLU C C 13 175.2 0.05 . 1 . . . . . . . . 5387 1 838 . 1 1 65 65 SER N N 15 115.5 0.05 . 1 . . . . . . . . 5387 1 839 . 1 1 65 65 SER H H 1 7.78 0.01 . 1 . . . . . . . . 5387 1 840 . 1 1 65 65 SER CA C 13 61.1 0.05 . 1 . . . . . . . . 5387 1 841 . 1 1 65 65 SER HA H 1 4.62 0.01 . 1 . . . . . . . . 5387 1 842 . 1 1 65 65 SER CB C 13 64.9 0.05 . 1 . . . . . . . . 5387 1 843 . 1 1 65 65 SER HB2 H 1 3.86 0.01 . 2 . . . . . . . . 5387 1 844 . 1 1 65 65 SER HB3 H 1 3.60 0.01 . 2 . . . . . . . . 5387 1 845 . 1 1 65 65 SER HG H 1 5.97 0.01 . 1 . . . . . . . . 5387 1 846 . 1 1 65 65 SER C C 13 171.9 0.05 . 1 . . . . . . . . 5387 1 847 . 1 1 66 66 THR N N 15 117.9 0.05 . 1 . . . . . . . . 5387 1 848 . 1 1 66 66 THR H H 1 8.71 0.01 . 1 . . . . . . . . 5387 1 849 . 1 1 66 66 THR CA C 13 62.2 0.05 . 1 . . . . . . . . 5387 1 850 . 1 1 66 66 THR HA H 1 5.24 0.01 . 1 . . . . . . . . 5387 1 851 . 1 1 66 66 THR CB C 13 70.0 0.05 . 1 . . . . . . . . 5387 1 852 . 1 1 66 66 THR HB H 1 4.06 0.01 . 1 . . . . . . . . 5387 1 853 . 1 1 66 66 THR HG21 H 1 0.89 0.01 . 1 . . . . . . . . 5387 1 854 . 1 1 66 66 THR HG22 H 1 0.89 0.01 . 1 . . . . . . . . 5387 1 855 . 1 1 66 66 THR HG23 H 1 0.89 0.01 . 1 . . . . . . . . 5387 1 856 . 1 1 66 66 THR CG2 C 13 21.6 0.05 . 1 . . . . . . . . 5387 1 857 . 1 1 66 66 THR C C 13 173.7 0.05 . 1 . . . . . . . . 5387 1 858 . 1 1 67 67 LEU N N 15 127.2 0.05 . 1 . . . . . . . . 5387 1 859 . 1 1 67 67 LEU H H 1 9.35 0.01 . 1 . . . . . . . . 5387 1 860 . 1 1 67 67 LEU CA C 13 53.9 0.05 . 1 . . . . . . . . 5387 1 861 . 1 1 67 67 LEU HA H 1 4.96 0.01 . 1 . . . . . . . . 5387 1 862 . 1 1 67 67 LEU CB C 13 44.1 0.05 . 1 . . . . . . . . 5387 1 863 . 1 1 67 67 LEU HB2 H 1 1.60 0.01 . 1 . . . . . . . . 5387 1 864 . 1 1 67 67 LEU HB3 H 1 1.60 0.01 . 1 . . . . . . . . 5387 1 865 . 1 1 67 67 LEU CG C 13 29.7 0.05 . 1 . . . . . . . . 5387 1 866 . 1 1 67 67 LEU HG H 1 1.72 0.01 . 1 . . . . . . . . 5387 1 867 . 1 1 67 67 LEU HD11 H 1 0.57 0.01 . 2 . . . . . . . . 5387 1 868 . 1 1 67 67 LEU HD12 H 1 0.57 0.01 . 2 . . . . . . . . 5387 1 869 . 1 1 67 67 LEU HD13 H 1 0.57 0.01 . 2 . . . . . . . . 5387 1 870 . 1 1 67 67 LEU HD21 H 1 0.64 0.01 . 2 . . . . . . . . 5387 1 871 . 1 1 67 67 LEU HD22 H 1 0.64 0.01 . 2 . . . . . . . . 5387 1 872 . 1 1 67 67 LEU HD23 H 1 0.64 0.01 . 2 . . . . . . . . 5387 1 873 . 1 1 67 67 LEU CD1 C 13 25.4 0.05 . 1 . . . . . . . . 5387 1 874 . 1 1 67 67 LEU CD2 C 13 24.9 0.05 . 1 . . . . . . . . 5387 1 875 . 1 1 67 67 LEU C C 13 175.7 0.05 . 1 . . . . . . . . 5387 1 876 . 1 1 68 68 HIS N N 15 117.8 0.05 . 1 . . . . . . . . 5387 1 877 . 1 1 68 68 HIS H H 1 9.10 0.01 . 1 . . . . . . . . 5387 1 878 . 1 1 68 68 HIS CA C 13 55.3 0.05 . 1 . . . . . . . . 5387 1 879 . 1 1 68 68 HIS HA H 1 5.45 0.01 . 1 . . . . . . . . 5387 1 880 . 1 1 68 68 HIS CD2 C 13 120.4 0.05 . 1 . . . . . . . . 5387 1 881 . 1 1 68 68 HIS CE1 C 13 137.4 0.05 . 1 . . . . . . . . 5387 1 882 . 1 1 68 68 HIS HD2 H 1 7.16 0.01 . 1 . . . . . . . . 5387 1 883 . 1 1 68 68 HIS HE1 H 1 8.76 0.01 . 1 . . . . . . . . 5387 1 884 . 1 1 68 68 HIS C C 13 172.8 0.05 . 1 . . . . . . . . 5387 1 885 . 1 1 69 69 LEU N N 15 125.8 0.05 . 1 . . . . . . . . 5387 1 886 . 1 1 69 69 LEU H H 1 8.50 0.01 . 1 . . . . . . . . 5387 1 887 . 1 1 69 69 LEU CA C 13 53.3 0.05 . 1 . . . . . . . . 5387 1 888 . 1 1 69 69 LEU HA H 1 5.28 0.01 . 1 . . . . . . . . 5387 1 889 . 1 1 69 69 LEU CB C 13 44.7 0.05 . 1 . . . . . . . . 5387 1 890 . 1 1 69 69 LEU HB2 H 1 1.42 0.01 . 2 . . . . . . . . 5387 1 891 . 1 1 69 69 LEU HB3 H 1 1.05 0.01 . 2 . . . . . . . . 5387 1 892 . 1 1 69 69 LEU CG C 13 27.5 0.05 . 1 . . . . . . . . 5387 1 893 . 1 1 69 69 LEU HG H 1 1.30 0.01 . 1 . . . . . . . . 5387 1 894 . 1 1 69 69 LEU HD11 H 1 0.65 0.01 . 2 . . . . . . . . 5387 1 895 . 1 1 69 69 LEU HD12 H 1 0.65 0.01 . 2 . . . . . . . . 5387 1 896 . 1 1 69 69 LEU HD13 H 1 0.65 0.01 . 2 . . . . . . . . 5387 1 897 . 1 1 69 69 LEU HD21 H 1 0.80 0.01 . 2 . . . . . . . . 5387 1 898 . 1 1 69 69 LEU HD22 H 1 0.80 0.01 . 2 . . . . . . . . 5387 1 899 . 1 1 69 69 LEU HD23 H 1 0.80 0.01 . 2 . . . . . . . . 5387 1 900 . 1 1 69 69 LEU CD1 C 13 25.9 0.05 . 1 . . . . . . . . 5387 1 901 . 1 1 69 69 LEU CD2 C 13 23.5 0.05 . 1 . . . . . . . . 5387 1 902 . 1 1 69 69 LEU C C 13 174.2 0.05 . 1 . . . . . . . . 5387 1 903 . 1 1 70 70 VAL N N 15 127.2 0.05 . 1 . . . . . . . . 5387 1 904 . 1 1 70 70 VAL H H 1 8.98 0.01 . 1 . . . . . . . . 5387 1 905 . 1 1 70 70 VAL CA C 13 60.9 0.05 . 1 . . . . . . . . 5387 1 906 . 1 1 70 70 VAL HA H 1 4.35 0.01 . 1 . . . . . . . . 5387 1 907 . 1 1 70 70 VAL CB C 13 35.0 0.05 . 1 . . . . . . . . 5387 1 908 . 1 1 70 70 VAL HB H 1 1.82 0.01 . 1 . . . . . . . . 5387 1 909 . 1 1 70 70 VAL HG11 H 1 1.00 0.01 . 2 . . . . . . . . 5387 1 910 . 1 1 70 70 VAL HG12 H 1 1.00 0.01 . 2 . . . . . . . . 5387 1 911 . 1 1 70 70 VAL HG13 H 1 1.00 0.01 . 2 . . . . . . . . 5387 1 912 . 1 1 70 70 VAL HG21 H 1 0.88 0.01 . 2 . . . . . . . . 5387 1 913 . 1 1 70 70 VAL HG22 H 1 0.88 0.01 . 2 . . . . . . . . 5387 1 914 . 1 1 70 70 VAL HG23 H 1 0.88 0.01 . 2 . . . . . . . . 5387 1 915 . 1 1 70 70 VAL CG1 C 13 21.4 0.05 . 1 . . . . . . . . 5387 1 916 . 1 1 70 70 VAL CG2 C 13 21.4 0.05 . 1 . . . . . . . . 5387 1 917 . 1 1 70 70 VAL C C 13 174.3 0.05 . 1 . . . . . . . . 5387 1 918 . 1 1 71 71 LEU N N 15 126.9 0.05 . 1 . . . . . . . . 5387 1 919 . 1 1 71 71 LEU H H 1 8.19 0.01 . 1 . . . . . . . . 5387 1 920 . 1 1 71 71 LEU CA C 13 54.4 0.05 . 1 . . . . . . . . 5387 1 921 . 1 1 71 71 LEU HA H 1 4.93 0.01 . 1 . . . . . . . . 5387 1 922 . 1 1 71 71 LEU CB C 13 42.3 0.05 . 1 . . . . . . . . 5387 1 923 . 1 1 71 71 LEU HB2 H 1 1.81 0.01 . 2 . . . . . . . . 5387 1 924 . 1 1 71 71 LEU HB3 H 1 1.46 0.01 . 2 . . . . . . . . 5387 1 925 . 1 1 71 71 LEU CG C 13 28.0 0.05 . 1 . . . . . . . . 5387 1 926 . 1 1 71 71 LEU HG H 1 1.71 0.01 . 1 . . . . . . . . 5387 1 927 . 1 1 71 71 LEU HD11 H 1 0.94 0.01 . 2 . . . . . . . . 5387 1 928 . 1 1 71 71 LEU HD12 H 1 0.94 0.01 . 2 . . . . . . . . 5387 1 929 . 1 1 71 71 LEU HD13 H 1 0.94 0.01 . 2 . . . . . . . . 5387 1 930 . 1 1 71 71 LEU HD21 H 1 0.82 0.01 . 2 . . . . . . . . 5387 1 931 . 1 1 71 71 LEU HD22 H 1 0.82 0.01 . 2 . . . . . . . . 5387 1 932 . 1 1 71 71 LEU HD23 H 1 0.82 0.01 . 2 . . . . . . . . 5387 1 933 . 1 1 71 71 LEU CD1 C 13 25.1 0.05 . 1 . . . . . . . . 5387 1 934 . 1 1 71 71 LEU CD2 C 13 24.6 0.05 . 1 . . . . . . . . 5387 1 935 . 1 1 71 71 LEU C C 13 176.9 0.05 . 1 . . . . . . . . 5387 1 936 . 1 1 72 72 ARG N N 15 119.0 0.05 . 1 . . . . . . . . 5387 1 937 . 1 1 72 72 ARG H H 1 8.36 0.01 . 1 . . . . . . . . 5387 1 938 . 1 1 72 72 ARG CA C 13 55.0 0.05 . 1 . . . . . . . . 5387 1 939 . 1 1 72 72 ARG HA H 1 4.57 0.01 . 1 . . . . . . . . 5387 1 940 . 1 1 72 72 ARG CB C 13 32.3 0.05 . 1 . . . . . . . . 5387 1 941 . 1 1 72 72 ARG HB2 H 1 2.00 0.01 . 2 . . . . . . . . 5387 1 942 . 1 1 72 72 ARG HB3 H 1 1.59 0.01 . 2 . . . . . . . . 5387 1 943 . 1 1 72 72 ARG CG C 13 28.0 0.05 . 1 . . . . . . . . 5387 1 944 . 1 1 72 72 ARG HG2 H 1 1.57 0.01 . 1 . . . . . . . . 5387 1 945 . 1 1 72 72 ARG HG3 H 1 1.57 0.01 . 1 . . . . . . . . 5387 1 946 . 1 1 72 72 ARG CD C 13 43.6 0.05 . 1 . . . . . . . . 5387 1 947 . 1 1 72 72 ARG HD2 H 1 3.19 0.01 . 1 . . . . . . . . 5387 1 948 . 1 1 72 72 ARG HD3 H 1 3.19 0.01 . 1 . . . . . . . . 5387 1 949 . 1 1 72 72 ARG NE N 15 84.6 0.05 . 1 . . . . . . . . 5387 1 950 . 1 1 72 72 ARG HE H 1 7.01 0.01 . 1 . . . . . . . . 5387 1 951 . 1 1 72 72 ARG CZ C 13 159.5 0.05 . 1 . . . . . . . . 5387 1 952 . 1 1 72 72 ARG C C 13 176.3 0.05 . 1 . . . . . . . . 5387 1 953 . 1 1 73 73 LEU N N 15 122.9 0.05 . 1 . . . . . . . . 5387 1 954 . 1 1 73 73 LEU H H 1 8.23 0.01 . 1 . . . . . . . . 5387 1 955 . 1 1 73 73 LEU CA C 13 57.0 0.05 . 1 . . . . . . . . 5387 1 956 . 1 1 73 73 LEU HA H 1 4.17 0.01 . 1 . . . . . . . . 5387 1 957 . 1 1 73 73 LEU CB C 13 42.4 0.05 . 1 . . . . . . . . 5387 1 958 . 1 1 73 73 LEU HB2 H 1 1.73 0.01 . 2 . . . . . . . . 5387 1 959 . 1 1 73 73 LEU HB3 H 1 1.60 0.01 . 2 . . . . . . . . 5387 1 960 . 1 1 73 73 LEU CG C 13 27.3 0.05 . 1 . . . . . . . . 5387 1 961 . 1 1 73 73 LEU HG H 1 1.77 0.01 . 1 . . . . . . . . 5387 1 962 . 1 1 73 73 LEU HD11 H 1 0.96 0.01 . 2 . . . . . . . . 5387 1 963 . 1 1 73 73 LEU HD12 H 1 0.96 0.01 . 2 . . . . . . . . 5387 1 964 . 1 1 73 73 LEU HD13 H 1 0.96 0.01 . 2 . . . . . . . . 5387 1 965 . 1 1 73 73 LEU HD21 H 1 0.91 0.01 . 2 . . . . . . . . 5387 1 966 . 1 1 73 73 LEU HD22 H 1 0.91 0.01 . 2 . . . . . . . . 5387 1 967 . 1 1 73 73 LEU HD23 H 1 0.91 0.01 . 2 . . . . . . . . 5387 1 968 . 1 1 73 73 LEU CD1 C 13 25.4 0.05 . 1 . . . . . . . . 5387 1 969 . 1 1 73 73 LEU CD2 C 13 24.0 0.05 . 1 . . . . . . . . 5387 1 970 . 1 1 73 73 LEU C C 13 177.3 0.05 . 1 . . . . . . . . 5387 1 971 . 1 1 74 74 ARG N N 15 115.4 0.05 . 1 . . . . . . . . 5387 1 972 . 1 1 74 74 ARG H H 1 7.70 0.01 . 1 . . . . . . . . 5387 1 973 . 1 1 74 74 ARG CA C 13 55.3 0.05 . 1 . . . . . . . . 5387 1 974 . 1 1 74 74 ARG HA H 1 4.41 0.01 . 1 . . . . . . . . 5387 1 975 . 1 1 74 74 ARG CB C 13 31.1 0.05 . 1 . . . . . . . . 5387 1 976 . 1 1 74 74 ARG HB2 H 1 1.91 0.01 . 2 . . . . . . . . 5387 1 977 . 1 1 74 74 ARG HB3 H 1 1.73 0.01 . 2 . . . . . . . . 5387 1 978 . 1 1 74 74 ARG CG C 13 27.2 0.05 . 1 . . . . . . . . 5387 1 979 . 1 1 74 74 ARG HG2 H 1 1.64 0.01 . 1 . . . . . . . . 5387 1 980 . 1 1 74 74 ARG HG3 H 1 1.64 0.01 . 1 . . . . . . . . 5387 1 981 . 1 1 74 74 ARG CD C 13 43.4 0.05 . 1 . . . . . . . . 5387 1 982 . 1 1 74 74 ARG HD2 H 1 3.19 0.01 . 1 . . . . . . . . 5387 1 983 . 1 1 74 74 ARG HD3 H 1 3.19 0.01 . 1 . . . . . . . . 5387 1 984 . 1 1 74 74 ARG NE N 15 83.6 0.05 . 1 . . . . . . . . 5387 1 985 . 1 1 74 74 ARG HE H 1 7.09 0.01 . 1 . . . . . . . . 5387 1 986 . 1 1 74 74 ARG CZ C 13 159.7 0.05 . 1 . . . . . . . . 5387 1 987 . 1 1 74 74 ARG C C 13 176.0 0.05 . 1 . . . . . . . . 5387 1 988 . 1 1 75 75 GLY N N 15 108.8 0.05 . 1 . . . . . . . . 5387 1 989 . 1 1 75 75 GLY H H 1 8.16 0.01 . 1 . . . . . . . . 5387 1 990 . 1 1 75 75 GLY CA C 13 45.3 0.05 . 1 . . . . . . . . 5387 1 991 . 1 1 75 75 GLY HA2 H 1 3.92 0.01 . 2 . . . . . . . . 5387 1 992 . 1 1 75 75 GLY HA3 H 1 3.84 0.01 . 2 . . . . . . . . 5387 1 993 . 1 1 75 75 GLY C C 13 173.9 0.05 . 1 . . . . . . . . 5387 1 994 . 1 1 76 76 GLY N N 15 115.2 0.05 . 1 . . . . . . . . 5387 1 995 . 1 1 76 76 GLY H H 1 8.16 0.01 . 1 . . . . . . . . 5387 1 996 . 1 1 76 76 GLY CA C 13 46.2 0.05 . 1 . . . . . . . . 5387 1 997 . 1 1 76 76 GLY HA2 H 1 3.78 0.01 . 2 . . . . . . . . 5387 1 998 . 1 1 76 76 GLY HA3 H 1 3.70 0.01 . 2 . . . . . . . . 5387 1 stop_ save_