data_17239 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 17239 _Entry.Title ; NMR structure of the UBA domain of S. cerevisiae Dcn1 bound to ubiquitin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2010-10-05 _Entry.Accession_date 2010-10-05 _Entry.Last_release_date 2012-07-25 _Entry.Original_release_date 2012-07-25 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.9.13 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Daniel Burschowsky . . . 17239 2 Daniel Mattle . . . 17239 3 Fabian Rudolf . . . 17239 4 Matthias Peter . . . 17239 5 Gerhard Wider . . . 17239 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 17239 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID neddylation . 17239 UBA . 17239 'ubiquitin binding' . 17239 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 17239 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 201 17239 '15N chemical shifts' 65 17239 '1H chemical shifts' 419 17239 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2012-07-25 2010-10-05 original author . 17239 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 17238 UBA 17239 PDB 2L4F 'BMRB Entry Tracking System' 17239 PDB 3BQ3 'Crystal structure of full-length Dcn1' 17239 stop_ save_ ############### # Citations # ############### save_UBA-Paper _Citation.Sf_category citations _Citation.Sf_framecode UBA-Paper _Citation.Entry_ID 17239 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title 'Structural analysis of the ubiquitin-associated domain (UBA) of yeast Dcn1 in complex with ubiquitin (WORKING TITLE)' _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev 'Not known' _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _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 . _Citation.Page_last . _Citation.Year . _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 Daniel Burschowsky . . . 17239 1 2 Fabian Rudolf . . . 17239 1 3 Daniel Mattle . . . 17239 1 4 Matthias Peter . . . 17239 1 5 Gerhard Wider . . . 17239 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 17239 _Assembly.ID 1 _Assembly.Name 'UBA+Ub complex' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass 15479 _Assembly.Enzyme_commission_number . _Assembly.Details 'Dcn1-UBA in complex with ubiquitin' _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 UBA 1 $Dcn1-UBA A . yes native yes no . . . 17239 1 2 ubi 2 $ubiquitin B . no native no yes . . . 17239 1 stop_ loop_ _Assembly_interaction.ID _Assembly_interaction.Entity_assembly_ID_1 _Assembly_interaction.Entity_assembly_ID_2 _Assembly_interaction.Mol_interaction_type _Assembly_interaction.Entry_ID _Assembly_interaction.Assembly_ID 1 1 2 'Fast exchange' 17239 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Dcn1-UBA _Entity.Sf_category entity _Entity.Sf_framecode Dcn1-UBA _Entity.Entry_ID 17239 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Dcn1-UBA _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; GSIKRKDASPEQEAIESFTS LTKCDPKVSRKYLQRNHWNI NYALNDYYDKEIGTFTDEV ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details 'N-terminal residues number 4 and 5 (GS) are non-native and leftovers from thrombin cleavage' _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 59 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment 'UBA domain of Dcn1 (Defective in cullin neddylation protein 1)' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 6780.567 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 17238 . Dcn1-UBA . . . . . 100.00 59 100.00 100.00 2.47e-35 . . . . 17239 1 2 no PDB 2L4E . "Nmr Structure Of The Uba Domain Of S. Cerevisiae Dcn1" . . . . . 100.00 59 100.00 100.00 2.47e-35 . . . . 17239 1 3 no PDB 2L4F . "Nmr Structure Of The Uba Domain Of S. Cerevisiae Dcn1 Bound To Ubiquitin" . . . . . 100.00 59 100.00 100.00 2.47e-35 . . . . 17239 1 4 no PDB 3BQ3 . "Crystal Structure Of S. Cerevisiae Dcn1" . . . . . 96.61 270 100.00 100.00 3.02e-31 . . . . 17239 1 5 no DBJ GAA25010 . "K7_Dcn1p [Saccharomyces cerevisiae Kyokai no. 7]" . . . . . 96.61 269 100.00 100.00 1.84e-31 . . . . 17239 1 6 no EMBL CAA61706 . "L3111 [Saccharomyces cerevisiae]" . . . . . 96.61 269 100.00 100.00 2.45e-31 . . . . 17239 1 7 no EMBL CAA62639 . "L3111 [Saccharomyces cerevisiae]" . . . . . 96.61 269 100.00 100.00 2.45e-31 . . . . 17239 1 8 no EMBL CAA97697 . "unnamed protein product [Saccharomyces cerevisiae]" . . . . . 96.61 269 100.00 100.00 2.45e-31 . . . . 17239 1 9 no EMBL CAY81363 . "Dcn1p [Saccharomyces cerevisiae EC1118]" . . . . . 96.61 269 100.00 100.00 2.45e-31 . . . . 17239 1 10 no GB AAB82374 . "Ylr128wp [Saccharomyces cerevisiae]" . . . . . 96.61 269 100.00 100.00 2.45e-31 . . . . 17239 1 11 no GB AHY78522 . "Dcn1p [Saccharomyces cerevisiae YJM993]" . . . . . 96.61 269 100.00 100.00 2.45e-31 . . . . 17239 1 12 no GB AJP40299 . "Dcn1p [Saccharomyces cerevisiae YJM1078]" . . . . . 96.61 269 98.25 98.25 5.14e-30 . . . . 17239 1 13 no GB AJV46201 . "Dcn1p [Saccharomyces cerevisiae YJM1083]" . . . . . 96.61 269 100.00 100.00 2.45e-31 . . . . 17239 1 14 no GB AJV46655 . "Dcn1p [Saccharomyces cerevisiae YJM1129]" . . . . . 96.61 269 100.00 100.00 2.70e-31 . . . . 17239 1 15 no REF NP_013229 . "NEDD8 ligase DCN1 [Saccharomyces cerevisiae S288c]" . . . . . 96.61 269 100.00 100.00 2.45e-31 . . . . 17239 1 16 no SP Q12395 . "RecName: Full=Defective in cullin neddylation protein 1" . . . . . 96.61 269 100.00 100.00 2.45e-31 . . . . 17239 1 17 no TPG DAA09439 . "TPA: NEDD8 ligase DCN1 [Saccharomyces cerevisiae S288c]" . . . . . 96.61 269 100.00 100.00 2.45e-31 . . . . 17239 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'ubiquitin binding' 17239 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 4 GLY . 17239 1 2 5 SER . 17239 1 3 6 ILE . 17239 1 4 7 LYS . 17239 1 5 8 ARG . 17239 1 6 9 LYS . 17239 1 7 10 ASP . 17239 1 8 11 ALA . 17239 1 9 12 SER . 17239 1 10 13 PRO . 17239 1 11 14 GLU . 17239 1 12 15 GLN . 17239 1 13 16 GLU . 17239 1 14 17 ALA . 17239 1 15 18 ILE . 17239 1 16 19 GLU . 17239 1 17 20 SER . 17239 1 18 21 PHE . 17239 1 19 22 THR . 17239 1 20 23 SER . 17239 1 21 24 LEU . 17239 1 22 25 THR . 17239 1 23 26 LYS . 17239 1 24 27 CYS . 17239 1 25 28 ASP . 17239 1 26 29 PRO . 17239 1 27 30 LYS . 17239 1 28 31 VAL . 17239 1 29 32 SER . 17239 1 30 33 ARG . 17239 1 31 34 LYS . 17239 1 32 35 TYR . 17239 1 33 36 LEU . 17239 1 34 37 GLN . 17239 1 35 38 ARG . 17239 1 36 39 ASN . 17239 1 37 40 HIS . 17239 1 38 41 TRP . 17239 1 39 42 ASN . 17239 1 40 43 ILE . 17239 1 41 44 ASN . 17239 1 42 45 TYR . 17239 1 43 46 ALA . 17239 1 44 47 LEU . 17239 1 45 48 ASN . 17239 1 46 49 ASP . 17239 1 47 50 TYR . 17239 1 48 51 TYR . 17239 1 49 52 ASP . 17239 1 50 53 LYS . 17239 1 51 54 GLU . 17239 1 52 55 ILE . 17239 1 53 56 GLY . 17239 1 54 57 THR . 17239 1 55 58 PHE . 17239 1 56 59 THR . 17239 1 57 60 ASP . 17239 1 58 61 GLU . 17239 1 59 62 VAL . 17239 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . GLY 1 1 17239 1 . SER 2 2 17239 1 . ILE 3 3 17239 1 . LYS 4 4 17239 1 . ARG 5 5 17239 1 . LYS 6 6 17239 1 . ASP 7 7 17239 1 . ALA 8 8 17239 1 . SER 9 9 17239 1 . PRO 10 10 17239 1 . GLU 11 11 17239 1 . GLN 12 12 17239 1 . GLU 13 13 17239 1 . ALA 14 14 17239 1 . ILE 15 15 17239 1 . GLU 16 16 17239 1 . SER 17 17 17239 1 . PHE 18 18 17239 1 . THR 19 19 17239 1 . SER 20 20 17239 1 . LEU 21 21 17239 1 . THR 22 22 17239 1 . LYS 23 23 17239 1 . CYS 24 24 17239 1 . ASP 25 25 17239 1 . PRO 26 26 17239 1 . LYS 27 27 17239 1 . VAL 28 28 17239 1 . SER 29 29 17239 1 . ARG 30 30 17239 1 . LYS 31 31 17239 1 . TYR 32 32 17239 1 . LEU 33 33 17239 1 . GLN 34 34 17239 1 . ARG 35 35 17239 1 . ASN 36 36 17239 1 . HIS 37 37 17239 1 . TRP 38 38 17239 1 . ASN 39 39 17239 1 . ILE 40 40 17239 1 . ASN 41 41 17239 1 . TYR 42 42 17239 1 . ALA 43 43 17239 1 . LEU 44 44 17239 1 . ASN 45 45 17239 1 . ASP 46 46 17239 1 . TYR 47 47 17239 1 . TYR 48 48 17239 1 . ASP 49 49 17239 1 . LYS 50 50 17239 1 . GLU 51 51 17239 1 . ILE 52 52 17239 1 . GLY 53 53 17239 1 . THR 54 54 17239 1 . PHE 55 55 17239 1 . THR 56 56 17239 1 . ASP 57 57 17239 1 . GLU 58 58 17239 1 . VAL 59 59 17239 1 stop_ save_ save_ubiquitin _Entity.Sf_category entity _Entity.Sf_framecode ubiquitin _Entity.Entry_ID 17239 _Entity.ID 2 _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 B _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 no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 76 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 8564.8 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-30 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 . . . . 17239 2 2 no BMRB 11547 . ubiquitin . . . . . 100.00 76 98.68 98.68 2.41e-45 . . . . 17239 2 3 no BMRB 15047 . denatured_ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 4 no BMRB 15410 . Ubi . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 5 no BMRB 15689 . UBB . . . . . 98.68 103 98.67 100.00 4.23e-44 . . . . 17239 2 6 no BMRB 15866 . ubiquitin . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 17239 2 7 no BMRB 15907 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 8 no BMRB 16228 . ubiquitin . . . . . 100.00 76 97.37 98.68 1.18e-44 . . . . 17239 2 9 no BMRB 16582 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 10 no BMRB 16626 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 11 no BMRB 16763 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 12 no BMRB 16880 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 13 no BMRB 16885 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 14 no BMRB 16895 . UBB+1 . . . . . 98.68 103 98.67 100.00 4.23e-44 . . . . 17239 2 15 no BMRB 17059 . ubiquitin . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 17239 2 16 no BMRB 17181 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 17 no BMRB 17333 . UB . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 18 no BMRB 17439 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 19 no BMRB 17769 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 20 no BMRB 17919 . entity . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 21 no BMRB 18582 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 22 no BMRB 18583 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 23 no BMRB 18584 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 24 no BMRB 18610 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 25 no BMRB 18611 . Ubiquitin_A_state . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 26 no BMRB 18737 . UBIQUITIN . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 27 no BMRB 19394 . ubiquitin . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 17239 2 28 no BMRB 19399 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 29 no BMRB 19406 . entity . . . . . 100.00 152 100.00 100.00 4.37e-45 . . . . 17239 2 30 no BMRB 19412 . entity . . . . . 100.00 152 100.00 100.00 4.37e-45 . . . . 17239 2 31 no BMRB 19447 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 32 no BMRB 25070 . Ubiquitin . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 17239 2 33 no BMRB 25230 . Ubiquitin . . . . . 100.00 78 100.00 100.00 3.66e-46 . . . . 17239 2 34 no BMRB 4245 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 35 no BMRB 4375 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 36 no BMRB 4983 . Ubiquitin . . . . . 98.68 76 97.33 100.00 3.66e-44 . . . . 17239 2 37 no BMRB 5101 . uq1_51 . . . . . 67.11 53 100.00 100.00 2.13e-26 . . . . 17239 2 38 no BMRB 5387 . ubq . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 39 no BMRB 6457 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 40 no BMRB 6466 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 41 no BMRB 6470 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 42 no BMRB 6488 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 43 no BMRB 68 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 44 no BMRB 7111 . human_ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 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 . . . . 17239 2 46 no PDB 1CMX . "Structural Basis For The Specificity Of Ubiquitin C- Terminal Hydrolases" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 17239 2 47 no PDB 1D3Z . "Ubiquitin Nmr Structure" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 48 no PDB 1F9J . "Structure Of A New Crystal Form Of Tetraubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 49 no PDB 1FXT . "Structure Of A Conjugating Enzyme-Ubiquitin Thiolester Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 50 no PDB 1G6J . "Structure Of Recombinant Human Ubiquitin In Aot Reverse Micelles" . . . . . 98.68 76 100.00 100.00 5.16e-45 . . . . 17239 2 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 . . . . 17239 2 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 . . . . 17239 2 53 no PDB 1OGW . "Synthetic Ubiquitin With Fluoro-Leu At 50 And 67" . . . . . 100.00 76 97.37 97.37 1.80e-44 . . . . 17239 2 54 no PDB 1P3Q . "Mechanism Of Ubiquitin Recognition By The Cue Domain Of Vps9" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 55 no PDB 1Q5W . "Ubiquitin Recognition By Npl4 Zinc-Fingers" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 56 no PDB 1S1Q . "Tsg101(Uev) Domain In Complex With Ubiquitin" . . . . . 98.68 76 100.00 100.00 5.16e-45 . . . . 17239 2 57 no PDB 1TBE . "Structure Of Tetraubiquitin Shows How Multiubiquitin Chains Can Be Formed" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 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 . . . . 17239 2 59 no PDB 1UBQ . "Structure Of Ubiquitin Refined At 1.8 Angstroms Resolution" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 60 no PDB 1UZX . "A Complex Of The Vps23 Uev With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 61 no PDB 1V80 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 62 no PDB 1V81 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 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 . . . . 17239 2 64 no PDB 1WR6 . "Crystal Structure Of Gga3 Gat Domain In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 65 no PDB 1WRD . "Crystal Structure Of Tom1 Gat Domain In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 66 no PDB 1XD3 . "Crystal Structure Of Uchl3-Ubvme Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 17239 2 67 no PDB 1XQQ . "Simultaneous Determination Of Protein Structure And Dynamics" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 68 no PDB 1YD8 . "Complex Of Human Gga3 Gat Domain And Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 69 no PDB 1YIW . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin" . . . . . 100.00 76 98.68 100.00 1.94e-45 . . . . 17239 2 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 . . . . 17239 2 71 no PDB 1YX5 . "Solution Structure Of S5a Uim-1UBIQUITIN COMPLEX" . . . . . 100.00 98 100.00 100.00 1.57e-46 . . . . 17239 2 72 no PDB 1YX6 . "Solution Structure Of S5a Uim-2UBIQUITIN COMPLEX" . . . . . 100.00 98 100.00 100.00 1.57e-46 . . . . 17239 2 73 no PDB 1ZGU . "Solution Structure Of The Human Mms2-Ubiquitin Complex" . . . . . 100.00 76 98.68 100.00 1.06e-45 . . . . 17239 2 74 no PDB 2AYO . "Structure Of Usp14 Bound To Ubquitin Aldehyde" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 17239 2 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 . . . . 17239 2 76 no PDB 2C7M . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 77 no PDB 2C7N . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 78 no PDB 2D3G . "Double Sided Ubiquitin Binding Of Hrs-Uim" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 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 . . . . 17239 2 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 . . . . 17239 2 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 . . . . 17239 2 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 . . . . 17239 2 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 . . . . 17239 2 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 . . . . 17239 2 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 . . . . 17239 2 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 . . . . 17239 2 87 no PDB 2FUH . "Solution Structure Of The Ubch5cUB NON-Covalent Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 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 . . . . 17239 2 89 no PDB 2GMI . Mms2UBC13~UBIQUITIN . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 90 no PDB 2HD5 . "Usp2 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 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 . . . . 17239 2 92 no PDB 2IBI . "Covalent Ubiquitin-Usp2 Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 17239 2 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 . . . . 17239 2 94 no PDB 2JF5 . "Crystal Structure Of Lys63-Linked Di-Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 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 . . . . 17239 2 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 . . . . 17239 2 97 no PDB 2JZZ . "Solid-State Nmr Structure Of Microcrystalline Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 98 no PDB 2K25 . "Automated Nmr Structure Of The Ubb By Fapsy" . . . . . 98.68 103 98.67 100.00 4.23e-44 . . . . 17239 2 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 . . . . 17239 2 100 no PDB 2K6D . "Cin85 Sh3-C Domain In Complex With Ubiquitin" . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 17239 2 101 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 . . . . 17239 2 102 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 . . . . 17239 2 103 no PDB 2KDE . "Nmr Structure Of Major S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 104 no PDB 2KDF . "Nmr Structure Of Minor S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 105 no PDB 2KHW . "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 17239 2 106 no PDB 2KJH . "Nmr Based Structural Model Of The Ubch8-Ubiquitin Complex" . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 17239 2 107 no PDB 2KLG . "Pere Nmr Structure Of Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 108 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 . . . . 17239 2 109 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 . . . . 17239 2 110 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 . . . . 17239 2 111 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 . . . . 17239 2 112 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 . . . . 17239 2 113 no PDB 2KX0 . "The Solution Structure Of Ubb+1, Frameshift Mutant Of Ubiquitin B" . . . . . 98.68 103 98.67 100.00 4.23e-44 . . . . 17239 2 114 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 . . . . 17239 2 115 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 . . . . 17239 2 116 no PDB 2L3Z . "Proton-Detected 4d Dream Solid-State Nmr Structure Of Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 117 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 . . . . 17239 2 118 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 . . . . 17239 2 119 no PDB 2LVO . "Structure Of The Gp78cue Domain Bound To Monubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 120 no PDB 2LVP . "Gp78cue Domain Bound To The Distal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 121 no PDB 2LVQ . "Gp78cue Domain Bound To The Proximal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 122 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 . . . . 17239 2 123 no PDB 2MBB . "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" . . . . . 100.00 78 100.00 100.00 3.66e-46 . . . . 17239 2 124 no PDB 2MBH . "Nmr Structure Of Eklf(22-40)/ubiquitin Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 125 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 . . . . 17239 2 126 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 . . . . 17239 2 127 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 . . . . 17239 2 128 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 . . . . 17239 2 129 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 . . . . 17239 2 130 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 . . . . 17239 2 131 no PDB 2MRE . "Nmr Structure Of The Rad18-ubz/ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 17239 2 132 no PDB 2MUR . "Solution Structure Of The Human Faap20 Ubz-ubiquitin Complex" . . . . . 100.00 78 100.00 100.00 3.66e-46 . . . . 17239 2 133 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 . . . . 17239 2 134 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 . . . . 17239 2 135 no PDB 2OJR . "Structure Of Ubiquitin Solved By Sad Using The Lanthanide- Binding Tag" . . . . . 100.00 111 100.00 100.00 1.56e-45 . . . . 17239 2 136 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 . . . . 17239 2 137 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 . . . . 17239 2 138 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 . . . . 17239 2 139 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 . . . . 17239 2 140 no PDB 2RR9 . "The Solution Structure Of The K63-Ub2:tuims Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 141 no PDB 2RSU . "Alternative Structure Of Ubiquitin" . . . . . 100.00 76 98.68 98.68 2.41e-45 . . . . 17239 2 142 no PDB 2RU6 . "The Pure Alternative State Of Ubiquitin" . . . . . 100.00 76 98.68 98.68 2.41e-45 . . . . 17239 2 143 no PDB 2W9N . "Crystal Structure Of Linear Di-Ubiquitin" . . . . . 98.68 152 100.00 100.00 3.82e-44 . . . . 17239 2 144 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 . . . . 17239 2 145 no PDB 2WWZ . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P212121" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 146 no PDB 2WX0 . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P21" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 147 no PDB 2WX1 . "Tab2 Nzf Domain In Complex With Lys63-Linked Tri-Ubiquitin, P212121" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 148 no PDB 2XBB . "Nedd4 Hect:ub Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 149 no PDB 2XEW . "Crystal Structure Of K11-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 150 no PDB 2XK5 . "Crystal Structure Of K6-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 151 no PDB 2Y5B . "Structure Of Usp21 In Complex With Linear Diubiquitin-Aldehyde" . . . . . 98.68 152 100.00 100.00 2.82e-44 . . . . 17239 2 152 no PDB 2Z59 . "Complex Structures Of Mouse Rpn13 (22-130aa) And Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 153 no PDB 2ZCB . "Crystal Structure Of Ubiquitin P37aP38A" . . . . . 100.00 76 97.37 97.37 2.34e-44 . . . . 17239 2 154 no PDB 2ZCC . "Ubiquitin Crystallized Under High Pressure" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 155 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 . . . . 17239 2 156 no PDB 2ZVN . "Nemo Cozi Domain Incomplex With Diubiquitin In P212121 Space Group" . . . . . 100.00 154 100.00 100.00 4.07e-45 . . . . 17239 2 157 no PDB 2ZVO . "Nemo Cozi Domain In Complex With Diubiquitin In C2 Space Group" . . . . . 100.00 154 100.00 100.00 4.07e-45 . . . . 17239 2 158 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 . . . . 17239 2 159 no PDB 3A33 . "Ubch5b~ubiquitin Conjugate" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 160 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 . . . . 17239 2 161 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 . . . . 17239 2 162 no PDB 3AI5 . "Crystal Structure Of Yeast Enhanced Green Fluorescent Protein- Ubiquitin Fusion Protein" . . . . . 97.37 307 100.00 100.00 1.12e-41 . . . . 17239 2 163 no PDB 3ALB . "Cyclic Lys48-Linked Tetraubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 164 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 . . . . 17239 2 165 no PDB 3AXC . "Crystal Structure Of Linear Diubiquitin" . . . . . 100.00 154 100.00 100.00 4.07e-45 . . . . 17239 2 166 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 . . . . 17239 2 167 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 . . . . 17239 2 168 no PDB 3BY4 . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 17239 2 169 no PDB 3C0R . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 17239 2 170 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 . . . . 17239 2 171 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 . . . . 17239 2 172 no PDB 3EEC . "X-Ray Structure Of Human Ubiquitin Cd(Ii) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 173 no PDB 3EFU . "X-Ray Structure Of Human Ubiquitin-Hg(Ii) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 174 no PDB 3EHV . "X-Ray Structure Of Human Ubiquitin Zn(Ii) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 175 no PDB 3H1U . "Structure Of Ubiquitin In Complex With Cd Ions" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 176 no PDB 3H7P . "Crystal Structure Of K63-Linked Di-Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 177 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 . . . . 17239 2 178 no PDB 3HM3 . "The Structure And Conformation Of Lys-63 Linked Tetra-Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 179 no PDB 3I3T . "Crystal Structure Of Covalent Ubiquitin-usp21 Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 17239 2 180 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 . . . . 17239 2 181 no PDB 3IHP . "Covalent Ubiquitin-Usp5 Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 17239 2 182 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 . . . . 17239 2 183 no PDB 3JVZ . E2~ubiquitin-Hect . . . . . 100.00 81 100.00 100.00 5.23e-46 . . . . 17239 2 184 no PDB 3JW0 . E2~ubiquitin-Hect . . . . . 100.00 81 100.00 100.00 5.23e-46 . . . . 17239 2 185 no PDB 3K9O . "The Crystal Structure Of E2-25k And Ubb+1 Complex" . . . . . 98.68 96 100.00 100.00 8.68e-45 . . . . 17239 2 186 no PDB 3K9P . "The Crystal Structure Of E2-25k And Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 17239 2 187 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 . . . . 17239 2 188 no PDB 3KW5 . "Crystal Structure Of Ubiquitin Carboxy Terminal Hydrolase L1 Ubiquitin Vinylmethylester" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 17239 2 189 no PDB 3LDZ . "Crystal Structure Of Human Stam1 Vhs Domain In Complex With Ubiquitin" . . . . . 96.05 73 100.00 100.00 1.22e-43 . . . . 17239 2 190 no PDB 3M3J . "A New Crystal Form Of Lys48-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 191 no PDB 3MHS . "Structure Of The Saga Ubp8SGF11SUS1SGF73 DUB MODULE BOUND Ubiquitin Aldehyde" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 17239 2 192 no PDB 3MTN . "Usp21 In Complex With A Ubiquitin-based, Usp21-specific Inhibitor" . . . . . 88.16 85 98.51 98.51 1.00e-37 . . . . 17239 2 193 no PDB 3N30 . "Crystal Structure Of Cubic Zn3-Hub (Human Ubiquitin) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 194 no PDB 3N32 . "The Crystal Structure Of Human Ubiquitin Adduct With Zeise's Salt" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 195 no PDB 3NHE . "High Resolution Structure (1.26a) Of Usp2a In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 196 no PDB 3NOB . "Structure Of K11-linked Di-ubiquitin" . . . . . 100.00 78 100.00 100.00 3.66e-46 . . . . 17239 2 197 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 . . . . 17239 2 198 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 . . . . 17239 2 199 no PDB 3OFI . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 200 no PDB 3OJ3 . "Crystal Structure Of The A20 Znf4 And Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 17239 2 201 no PDB 3OJ4 . "Crystal Structure Of The A20 Znf4, Ubiquitin And Ubch5a Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 17239 2 202 no PDB 3ONS . "Crystal Structure Of Human Ubiquitin In A New Crystal Form" . . . . . 94.74 72 100.00 100.00 5.80e-43 . . . . 17239 2 203 no PDB 3PHD . "Crystal Structure Of Human Hdac6 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 204 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 . . . . 17239 2 205 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 . . . . 17239 2 206 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 . . . . 17239 2 207 no PDB 3PT2 . "Structure Of A Viral Otu Domain Protease Bound To Ubiquitin" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 17239 2 208 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 . . . . 17239 2 209 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 . . . . 17239 2 210 no PDB 3RUL . "New Strategy To Analyze Structures Of Glycopeptide-Target Complexes" . . . . . 98.68 79 100.00 100.00 2.70e-45 . . . . 17239 2 211 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 . . . . 17239 2 212 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 . . . . 17239 2 213 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 . . . . 17239 2 214 no PDB 3UGB . "Ubch5c~ubiquitin Conjugate" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 215 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 . . . . 17239 2 216 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 . . . . 17239 2 217 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 . . . . 17239 2 218 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 . . . . 17239 2 219 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 . . . . 17239 2 220 no PDB 3VUY . "Crystal Structure Of A20 Zf7 In Complex With Linear Tetraubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 221 no PDB 3ZLZ . "Lys6-linked Tri-ubiquitin" . . . . . 100.00 76 98.68 100.00 1.06e-45 . . . . 17239 2 222 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 . . . . 17239 2 223 no PDB 3ZNI . "Structure Of Phosphotyr363-cbl-b - Ubch5b-ub - Zap-70 Peptide Complex" . . . . . 100.00 81 100.00 100.00 5.23e-46 . . . . 17239 2 224 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 . . . . 17239 2 225 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 . . . . 17239 2 226 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 . . . . 17239 2 227 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 . . . . 17239 2 228 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 . . . . 17239 2 229 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 . . . . 17239 2 230 no PDB 4AP4 . "Rnf4 - Ubch5a - Ubiquitin Heterotrimeric Complex" . . . . . 100.00 80 100.00 100.00 4.66e-46 . . . . 17239 2 231 no PDB 4AUQ . "Structure Of Birc7-Ubch5b-Ub Complex." . . . . . 100.00 81 100.00 100.00 5.23e-46 . . . . 17239 2 232 no PDB 4BBN . "Nedd4 Hect-ub:ub Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 233 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 . . . . 17239 2 234 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 . . . . 17239 2 235 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 . . . . 17239 2 236 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 . . . . 17239 2 237 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 . . . . 17239 2 238 no PDB 4DDG . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 239 no PDB 4DDI . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 240 no PDB 4DHJ . "The Structure Of A Ceotub1 Ubiquitin Aldehyde Ubc13~ub Complex" . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 17239 2 241 no PDB 4DHZ . "The Structure Of HCEOTUB1-Ubiquitin Aldehyde-Ubc13~ub" . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 17239 2 242 no PDB 4FJV . "Crystal Structure Of Human Otubain2 And Ubiquitin Complex" . . . . . 100.00 86 100.00 100.00 6.71e-46 . . . . 17239 2 243 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 . . . . 17239 2 244 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 . . . . 17239 2 245 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 . . . . 17239 2 246 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 . . . . 17239 2 247 no PDB 4JIO . "Bro1 V Domain And Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.30e-45 . . . . 17239 2 248 no PDB 4JQW . "Crystal Structure Of A Complex Of Nod1 Card And Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 249 no PDB 4K1R . "Crystal Structure Of Schizosaccharomyces Pombe Sst2 Catalytic Domain And Ubiquitin" . . . . . 100.00 81 100.00 100.00 7.82e-46 . . . . 17239 2 250 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 . . . . 17239 2 251 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 . . . . 17239 2 252 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 . . . . 17239 2 253 no PDB 4KSK . "Gumby/fam105b In Complex With Ubiquitin" . . . . . 100.00 80 100.00 100.00 4.66e-46 . . . . 17239 2 254 no PDB 4KSL . "Gumby/fam105b In Complex With Linear Di-ubiquitin" . . . . . 100.00 156 100.00 100.00 4.31e-45 . . . . 17239 2 255 no PDB 4KZX . "Rabbit 40s Ribosomal Subunit In Complex With Eif1." . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 17239 2 256 no PDB 4KZY . "Rabbit 40s Ribosomal Subunit In Complex With Eif1 And Eif1a." . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 17239 2 257 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 . . . . 17239 2 258 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 . . . . 17239 2 259 no PDB 4LDT . "The Structure Of H/ceotub1-ubiquitin Aldehyde-ubch5b~ub" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 260 no PDB 4LJO . "Structure Of An Active Ligase (hoip)/ubiquitin Transfer Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 261 no PDB 4LJP . "Structure Of An Active Ligase (hoip-h889a)/ubiquitin Transfer Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 262 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 . . . . 17239 2 263 no PDB 4MDK . "Cdc34-ubiquitin-cc0651 Complex" . . . . . 100.00 80 100.00 100.00 4.66e-46 . . . . 17239 2 264 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 . . . . 17239 2 265 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 . . . . 17239 2 266 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 . . . . 17239 2 267 no PDB 4NQK . "Structure Of An Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 8.16e-46 . . . . 17239 2 268 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 . . . . 17239 2 269 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 . . . . 17239 2 270 no PDB 4PIG . "Crystal Structure Of The Ubiquitin K11s Mutant" . . . . . 100.00 76 98.68 98.68 1.92e-45 . . . . 17239 2 271 no PDB 4PIH . "X-ray Crystal Structure Of The K33s Mutant Of Ubiquitin" . . . . . 100.00 76 98.68 98.68 1.92e-45 . . . . 17239 2 272 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 . . . . 17239 2 273 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 . . . . 17239 2 274 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 . . . . 17239 2 275 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 . . . . 17239 2 276 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 . . . . 17239 2 277 no PDB 4UPX . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 17239 2 278 no PDB 4UQ1 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 17239 2 279 no PDB 4UQ4 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 17239 2 280 no PDB 4UQ5 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 17239 2 281 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 . . . . 17239 2 282 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 . . . . 17239 2 283 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 . . . . 17239 2 284 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 . . . . 17239 2 285 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 . . . . 17239 2 286 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 . . . . 17239 2 287 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 . . . . 17239 2 288 no PDB 4WZP . "Ser65 Phosphorylated Ubiquitin, Major Conformation" . . . . . 100.00 76 98.68 98.68 3.16e-45 . . . . 17239 2 289 no DBJ BAA03983 . "polyubiquitin [Rattus norvegicus]" . . . . . 100.00 305 100.00 100.00 2.21e-43 . . . . 17239 2 290 no DBJ BAA09860 . "polyubiquitin [Homo sapiens]" . . . . . 100.00 611 98.68 98.68 1.04e-40 . . . . 17239 2 291 no DBJ BAA11842 . "ubiquitin [Cavia porcellus]" . . . . . 100.00 311 100.00 100.00 2.40e-43 . . . . 17239 2 292 no DBJ BAA11843 . "ubiquitin extention protein [Cavia porcellus]" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 17239 2 293 no DBJ BAA23486 . "polyubiquitin [Homo sapiens]" . . . . . 100.00 609 98.68 98.68 5.60e-41 . . . . 17239 2 294 no EMBL CAA25706 . "unnamed protein product [Saccharomyces cerevisiae]" . . . . . 50.00 191 100.00 100.00 2.98e-16 . . . . 17239 2 295 no EMBL CAA26488 . "unnamed protein product [Gallus gallus]" . . . . . 100.00 157 98.68 98.68 2.66e-44 . . . . 17239 2 296 no EMBL CAA28495 . "ubiquitin [Homo sapiens]" . . . . . 100.00 229 100.00 100.00 3.53e-44 . . . . 17239 2 297 no EMBL CAA30183 . "unnamed protein product [Dictyostelium discoideum]" . . . . . 100.00 128 97.37 97.37 5.38e-44 . . . . 17239 2 298 no EMBL CAA30815 . "unnamed protein product [Cricetulus sp.]" . . . . . 93.42 223 100.00 100.00 3.70e-40 . . . . 17239 2 299 no GB AAA02769 . "polyprotein [Bovine viral diarrhea virus 1-Osloss]" . . . . . 98.68 3975 97.33 100.00 1.83e-39 . . . . 17239 2 300 no GB AAA28154 . "polyubiquitin [Caenorhabditis elegans]" . . . . . 100.00 838 97.37 98.68 7.19e-40 . . . . 17239 2 301 no GB AAA28997 . "ubiquitin [Drosophila melanogaster]" . . . . . 100.00 231 100.00 100.00 3.30e-44 . . . . 17239 2 302 no GB AAA28998 . "ubiquitin-hybrid protein precursor [Drosophila melanogaster]" . . . . . 100.00 156 100.00 100.00 9.66e-46 . . . . 17239 2 303 no GB AAA28999 . "ubiquitin, partial [Drosophila melanogaster]" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 304 no PIR I50437 . "polyubiquitin 4 - chicken [Gallus gallus]" . . . . . 100.00 305 100.00 100.00 2.21e-43 . . . . 17239 2 305 no PIR I51568 . "polyubiquitin - African clawed frog (fragment)" . . . . . 100.00 167 100.00 100.00 6.83e-45 . . . . 17239 2 306 no PIR I65237 . "ubiquitin / ribosomal protein L40, cytosolic [validated] - rat" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 17239 2 307 no PIR JN0790 . "ubiquitin/ribosomal protein CEP52 fusion protein - Leishmania major" . . . . . 100.00 128 97.37 98.68 2.33e-45 . . . . 17239 2 308 no PIR S13928 . "ubiquitin precursor - chicken [Gallus gallus]" . . . . . 100.00 229 100.00 100.00 3.64e-44 . . . . 17239 2 309 no PRF 0412265A . ubiquitin . . . . . 98.68 75 98.67 98.67 1.22e-44 . . . . 17239 2 310 no PRF 1101405A . "ubiquitin precursor" . . . . . 50.00 191 100.00 100.00 2.95e-16 . . . . 17239 2 311 no PRF 1212243A . "ubiquitin S1" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 312 no PRF 1212243B . "ubiquitin S5" . . . . . 92.11 77 98.57 98.57 7.61e-41 . . . . 17239 2 313 no PRF 1212243C . "ubiquitin S3" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 17239 2 314 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 . . . . 17239 2 315 no REF NP_001006688 . "ubiquitin C [Xenopus (Silurana) tropicalis]" . . . . . 100.00 609 100.00 100.00 9.87e-42 . . . . 17239 2 316 no REF NP_001009117 . "polyubiquitin-B [Pan troglodytes]" . . . . . 100.00 229 100.00 100.00 3.53e-44 . . . . 17239 2 317 no REF NP_001009202 . "polyubiquitin-B [Ovis aries]" . . . . . 100.00 305 98.68 100.00 3.89e-43 . . . . 17239 2 318 no REF NP_001009286 . "ubiquitin-60S ribosomal protein L40 [Ovis aries]" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 17239 2 319 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 . . . . 17239 2 320 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 . . . . 17239 2 321 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 . . . . 17239 2 322 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 . . . . 17239 2 323 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 . . . . 17239 2 324 no TPD FAA00319 . "TPA: polyubiquitin [Cryptococcus neoformans var. neoformans B-3501A]" . . . . . 100.00 456 97.37 98.68 7.53e-41 . . . . 17239 2 325 no TPG DAA18802 . "TPA: polyubiquitin [Bos taurus]" . . . . . 100.00 305 100.00 100.00 2.33e-43 . . . . 17239 2 326 no TPG DAA20663 . "TPA: ubiquitin C [Bos taurus]" . . . . . 98.68 314 98.67 100.00 8.85e-42 . . . . 17239 2 327 no TPG DAA20672 . "TPA: ubiquitin B-like [Bos taurus]" . . . . . 100.00 77 98.68 98.68 3.32e-45 . . . . 17239 2 328 no TPG DAA24675 . "TPA: 40S ribosomal protein S27a [Bos taurus]" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 17239 2 329 no TPG DAA28295 . "TPA: ubiquitin and ribosomal protein L40 [Bos taurus]" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 17239 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . MET . 17239 2 2 . GLN . 17239 2 3 . ILE . 17239 2 4 . PHE . 17239 2 5 . VAL . 17239 2 6 . LYS . 17239 2 7 . THR . 17239 2 8 . LEU . 17239 2 9 . THR . 17239 2 10 . GLY . 17239 2 11 . LYS . 17239 2 12 . THR . 17239 2 13 . ILE . 17239 2 14 . THR . 17239 2 15 . LEU . 17239 2 16 . GLU . 17239 2 17 . VAL . 17239 2 18 . GLU . 17239 2 19 . PRO . 17239 2 20 . SER . 17239 2 21 . ASP . 17239 2 22 . THR . 17239 2 23 . ILE . 17239 2 24 . GLU . 17239 2 25 . ASN . 17239 2 26 . VAL . 17239 2 27 . LYS . 17239 2 28 . ALA . 17239 2 29 . LYS . 17239 2 30 . ILE . 17239 2 31 . GLN . 17239 2 32 . ASP . 17239 2 33 . LYS . 17239 2 34 . GLU . 17239 2 35 . GLY . 17239 2 36 . ILE . 17239 2 37 . PRO . 17239 2 38 . PRO . 17239 2 39 . ASP . 17239 2 40 . GLN . 17239 2 41 . GLN . 17239 2 42 . ARG . 17239 2 43 . LEU . 17239 2 44 . ILE . 17239 2 45 . PHE . 17239 2 46 . ALA . 17239 2 47 . GLY . 17239 2 48 . LYS . 17239 2 49 . GLN . 17239 2 50 . LEU . 17239 2 51 . GLU . 17239 2 52 . ASP . 17239 2 53 . GLY . 17239 2 54 . ARG . 17239 2 55 . THR . 17239 2 56 . LEU . 17239 2 57 . SER . 17239 2 58 . ASP . 17239 2 59 . TYR . 17239 2 60 . ASN . 17239 2 61 . ILE . 17239 2 62 . GLN . 17239 2 63 . LYS . 17239 2 64 . GLU . 17239 2 65 . SER . 17239 2 66 . THR . 17239 2 67 . LEU . 17239 2 68 . HIS . 17239 2 69 . LEU . 17239 2 70 . VAL . 17239 2 71 . LEU . 17239 2 72 . ARG . 17239 2 73 . LEU . 17239 2 74 . ARG . 17239 2 75 . GLY . 17239 2 76 . GLY . 17239 2 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 17239 2 . GLN 2 2 17239 2 . ILE 3 3 17239 2 . PHE 4 4 17239 2 . VAL 5 5 17239 2 . LYS 6 6 17239 2 . THR 7 7 17239 2 . LEU 8 8 17239 2 . THR 9 9 17239 2 . GLY 10 10 17239 2 . LYS 11 11 17239 2 . THR 12 12 17239 2 . ILE 13 13 17239 2 . THR 14 14 17239 2 . LEU 15 15 17239 2 . GLU 16 16 17239 2 . VAL 17 17 17239 2 . GLU 18 18 17239 2 . PRO 19 19 17239 2 . SER 20 20 17239 2 . ASP 21 21 17239 2 . THR 22 22 17239 2 . ILE 23 23 17239 2 . GLU 24 24 17239 2 . ASN 25 25 17239 2 . VAL 26 26 17239 2 . LYS 27 27 17239 2 . ALA 28 28 17239 2 . LYS 29 29 17239 2 . ILE 30 30 17239 2 . GLN 31 31 17239 2 . ASP 32 32 17239 2 . LYS 33 33 17239 2 . GLU 34 34 17239 2 . GLY 35 35 17239 2 . ILE 36 36 17239 2 . PRO 37 37 17239 2 . PRO 38 38 17239 2 . ASP 39 39 17239 2 . GLN 40 40 17239 2 . GLN 41 41 17239 2 . ARG 42 42 17239 2 . LEU 43 43 17239 2 . ILE 44 44 17239 2 . PHE 45 45 17239 2 . ALA 46 46 17239 2 . GLY 47 47 17239 2 . LYS 48 48 17239 2 . GLN 49 49 17239 2 . LEU 50 50 17239 2 . GLU 51 51 17239 2 . ASP 52 52 17239 2 . GLY 53 53 17239 2 . ARG 54 54 17239 2 . THR 55 55 17239 2 . LEU 56 56 17239 2 . SER 57 57 17239 2 . ASP 58 58 17239 2 . TYR 59 59 17239 2 . ASN 60 60 17239 2 . ILE 61 61 17239 2 . GLN 62 62 17239 2 . LYS 63 63 17239 2 . GLU 64 64 17239 2 . SER 65 65 17239 2 . THR 66 66 17239 2 . LEU 67 67 17239 2 . HIS 68 68 17239 2 . LEU 69 69 17239 2 . VAL 70 70 17239 2 . LEU 71 71 17239 2 . ARG 72 72 17239 2 . LEU 73 73 17239 2 . ARG 74 74 17239 2 . GLY 75 75 17239 2 . GLY 76 76 17239 2 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 17239 _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 $Dcn1-UBA . 4932 organism . 'Saccharomyces cerevisiae' 'baker's yeast' . . Eukaryota Fungi Saccharomyces cerevisiae . . . . . . . . . . . . . . . . 'DCN1 YLR128W' . . . . 17239 1 2 2 $ubiquitin . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 17239 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 17239 _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 $Dcn1-UBA . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21 DE3 Star' . . . . . . . . . . . . . . . pGEX-4T . . . . . . 17239 1 2 2 $ubiquitin . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21DE3 Star' . . . . . . . . . . . . . . . pET19b . . . . . . 17239 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_UBA-13C15N+Ub _Sample.Sf_category sample _Sample.Sf_framecode UBA-13C15N+Ub _Sample.Entry_ID 17239 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Dcn1-UBA '[U-80% 13C; U-90% 15N]' . . 1 $Dcn1-UBA . . 0.8 . . mM . . . . 17239 1 2 'sodium chloride' 'natural abundance' . . . . . . 15 . . mM . . . . 17239 1 3 'potassium phosphate' 'natural abundance' . . . . . . 110 . . mM . . . . 17239 1 4 DTT 'natural abundance' . . . . . . 2 . . mM . . . . 17239 1 5 CHAPS 'natural abundance' . . . . . . 2 . . mM . . . . 17239 1 6 'sodium azide' 'natural abundance' . . . . . . 0.02 . . % . . . . 17239 1 7 'sodium chloride' 'natural abundance' . . . . . . 25 . . mM . . . . 17239 1 8 ubiquitin 'natural abundance' . . 2 $ubiquitin . . 3.2 . . mM . . . . 17239 1 9 H2O 'natural abundance' . . . . . . 95 . . % . . . . 17239 1 10 D2O 'natural abundance' . . . . . . 5 . . % . . . . 17239 1 stop_ save_ save_UBA-15N+Ub _Sample.Sf_category sample _Sample.Sf_framecode UBA-15N+Ub _Sample.Entry_ID 17239 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Dcn1-UBA '[U-90% 15N]' . . 1 $Dcn1-UBA . . 0.5 . . mM . . . . 17239 2 2 'sodium phosphate' 'natural abundance' . . . . . . 15 . . mM . . . . 17239 2 3 'potassium phosphate' 'natural abundance' . . . . . . 110 . . mM . . . . 17239 2 4 DTT 'natural abundance' . . . . . . 2 . . mM . . . . 17239 2 5 CHAPS 'natural abundance' . . . . . . 2 . . mM . . . . 17239 2 6 'sodium azide' 'natural abundance' . . . . . . 0.02 . . % . . . . 17239 2 7 'sodium chloride' 'natural abundance' . . . . . . 25 . . mM . . . . 17239 2 8 ubiquitin 'natural abundance' . . 2 $ubiquitin . . 2 . . mM . . . . 17239 2 9 H2O 'natural abundance' . . . . . . 95 . . % . . . . 17239 2 10 D2O 'natural abundance' . . . . . . 5 . . % . . . . 17239 2 stop_ save_ ####################### # Sample conditions # ####################### save_NMR_Standard_Conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode NMR_Standard_Conditions _Sample_condition_list.Entry_ID 17239 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 182 . mM 17239 1 pH 6.15 . pH 17239 1 pressure 1 . atm 17239 1 temperature 288 . K 17239 1 stop_ save_ ############################ # Computer software used # ############################ save_Unio08 _Software.Sf_category software _Software.Sf_framecode Unio08 _Software.Entry_ID 17239 _Software.ID 1 _Software.Name UNIO _Software.Version 1.0.4 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Herrmann . . 17239 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 17239 1 'peak picking' 17239 1 stop_ save_ save_AMBER _Software.Sf_category software _Software.Sf_framecode AMBER _Software.Entry_ID 17239 _Software.ID 2 _Software.Name AMBER _Software.Version 9 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm' . . 17239 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 17239 2 stop_ save_ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 17239 _Software.ID 3 _Software.Name CYANA _Software.Version 2 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 17239 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 17239 3 stop_ save_ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 17239 _Software.ID 4 _Software.Name TOPSPIN _Software.Version 2.0 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 17239 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 17239 4 stop_ save_ save_CARA _Software.Sf_category software _Software.Sf_framecode CARA _Software.Entry_ID 17239 _Software.ID 5 _Software.Name CARA _Software.Version 1.8.4 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Keller . . 17239 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 17239 5 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 17239 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 17239 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_3 _NMR_spectrometer.Entry_ID 17239 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 17239 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 700 . . . 17239 1 2 spectrometer_2 Bruker Avance . 750 . . . 17239 1 3 spectrometer_3 Bruker Avance . 900 . . . 17239 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 17239 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '3D HCCH-COSY' no . . . . . . . . . . 1 $UBA-13C15N+Ub isotropic . . 1 $NMR_Standard_Conditions . . . . . . . . . . . . . . . . . . . . . 17239 1 2 '3D HNCA' no . . . . . . . . . . 1 $UBA-13C15N+Ub isotropic . . 1 $NMR_Standard_Conditions . . . . . . . . . . . . . . . . . . . . . 17239 1 3 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $UBA-13C15N+Ub isotropic . . 1 $NMR_Standard_Conditions . . . . . . . . . . . . . . . . . . . . . 17239 1 4 '3D 1H-13Caro NOESY' no . . . . . . . . . . 1 $UBA-13C15N+Ub isotropic . . 1 $NMR_Standard_Conditions . . . . . . . . . . . . . . . . . . . . . 17239 1 5 '3D 1H-15N TOCSY' no . . . . . . . . . . 2 $UBA-15N+Ub isotropic . . 1 $NMR_Standard_Conditions . . . . . . . . . . . . . . . . . . . . . 17239 1 6 '3D HNHB' no . . . . . . . . . . 2 $UBA-15N+Ub isotropic . . 1 $NMR_Standard_Conditions . . . . . . . . . . . . . . . . . . . . . 17239 1 7 '3D 1H-15N NOESY' no . . . . . . . . . . 2 $UBA-15N+Ub isotropic . . 1 $NMR_Standard_Conditions . . . . . . . . . . . . . . . . . . . . . 17239 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference _Chem_shift_reference.Entry_ID 17239 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0 internal indirect 0.25144954 . . . . . . . . . 17239 1 H 1 DSS 'methyl protons' . . . . ppm 0 internal direct 1.00000000 . . . . . . . . . 17239 1 N 15 DSS 'methyl protons' . . . . ppm 0 internal indirect 0.10132900 . . . . . . . . . 17239 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_Assignment _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode Assignment _Assigned_chem_shift_list.Entry_ID 17239 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $NMR_Standard_Conditions _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '3D HCCH-COSY' . . . 17239 1 2 '3D HNCA' . . . 17239 1 3 '3D 1H-13C NOESY' . . . 17239 1 5 '3D 1H-15N TOCSY' . . . 17239 1 6 '3D HNHB' . . . 17239 1 7 '3D 1H-15N NOESY' . . . 17239 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 GLY HA2 H 1 3.902 0.020 . 2 . . . . 4 G QA . 17239 1 2 . 1 1 1 1 GLY HA3 H 1 3.902 0.020 . 2 . . . . 4 G QA . 17239 1 3 . 1 1 1 1 GLY CA C 13 43.390 0.300 . 1 . . . . 4 G CA . 17239 1 4 . 1 1 2 2 SER HA H 1 4.545 0.020 . 1 . . . . 5 S HA . 17239 1 5 . 1 1 2 2 SER HB2 H 1 3.852 0.020 . 2 . . . . 5 S QB . 17239 1 6 . 1 1 2 2 SER HB3 H 1 3.852 0.020 . 2 . . . . 5 S QB . 17239 1 7 . 1 1 2 2 SER CA C 13 58.200 0.300 . 1 . . . . 5 S CA . 17239 1 8 . 1 1 2 2 SER CB C 13 64.032 0.300 . 1 . . . . 5 S CB . 17239 1 9 . 1 1 3 3 ILE H H 1 8.395 0.020 . 1 . . . . 6 I HN . 17239 1 10 . 1 1 3 3 ILE HA H 1 4.187 0.020 . 1 . . . . 6 I HA . 17239 1 11 . 1 1 3 3 ILE HB H 1 1.853 0.020 . 1 . . . . 6 I HB . 17239 1 12 . 1 1 3 3 ILE HD11 H 1 0.867 0.020 . 1 . . . . 6 I QD1 . 17239 1 13 . 1 1 3 3 ILE HD12 H 1 0.867 0.020 . 1 . . . . 6 I QD1 . 17239 1 14 . 1 1 3 3 ILE HD13 H 1 0.867 0.020 . 1 . . . . 6 I QD1 . 17239 1 15 . 1 1 3 3 ILE HG12 H 1 1.481 0.020 . 1 . . . . 6 I HG12 . 17239 1 16 . 1 1 3 3 ILE HG13 H 1 1.189 0.020 . 1 . . . . 6 I HG13 . 17239 1 17 . 1 1 3 3 ILE HG21 H 1 0.896 0.020 . 1 . . . . 6 I QG2 . 17239 1 18 . 1 1 3 3 ILE HG22 H 1 0.896 0.020 . 1 . . . . 6 I QG2 . 17239 1 19 . 1 1 3 3 ILE HG23 H 1 0.896 0.020 . 1 . . . . 6 I QG2 . 17239 1 20 . 1 1 3 3 ILE CA C 13 61.159 0.300 . 1 . . . . 6 I CA . 17239 1 21 . 1 1 3 3 ILE CB C 13 38.757 0.300 . 1 . . . . 6 I CB . 17239 1 22 . 1 1 3 3 ILE CD1 C 13 12.970 0.300 . 1 . . . . 6 I CD1 . 17239 1 23 . 1 1 3 3 ILE CG1 C 13 27.366 0.300 . 1 . . . . 6 I CG1 . 17239 1 24 . 1 1 3 3 ILE CG2 C 13 17.423 0.300 . 1 . . . . 6 I CG2 . 17239 1 25 . 1 1 3 3 ILE N N 15 122.671 0.300 . 1 . . . . 6 I N . 17239 1 26 . 1 1 4 4 LYS H H 1 8.518 0.020 . 1 . . . . 7 K HN . 17239 1 27 . 1 1 4 4 LYS HA H 1 4.318 0.020 . 1 . . . . 7 K HA . 17239 1 28 . 1 1 4 4 LYS HB2 H 1 1.793 0.020 . 2 . . . . 7 K HB2 . 17239 1 29 . 1 1 4 4 LYS HB3 H 1 1.738 0.020 . 2 . . . . 7 K HB3 . 17239 1 30 . 1 1 4 4 LYS HD2 H 1 1.682 0.020 . 2 . . . . 7 K QD . 17239 1 31 . 1 1 4 4 LYS HD3 H 1 1.682 0.020 . 2 . . . . 7 K QD . 17239 1 32 . 1 1 4 4 LYS HE2 H 1 2.998 0.020 . 2 . . . . 7 K QE . 17239 1 33 . 1 1 4 4 LYS HE3 H 1 2.998 0.020 . 2 . . . . 7 K QE . 17239 1 34 . 1 1 4 4 LYS HG2 H 1 1.445 0.020 . 2 . . . . 7 K HG2 . 17239 1 35 . 1 1 4 4 LYS HG3 H 1 1.413 0.020 . 2 . . . . 7 K HG3 . 17239 1 36 . 1 1 4 4 LYS CA C 13 56.071 0.300 . 1 . . . . 7 K CA . 17239 1 37 . 1 1 4 4 LYS CB C 13 33.025 0.300 . 1 . . . . 7 K CB . 17239 1 38 . 1 1 4 4 LYS CD C 13 29.133 0.300 . 1 . . . . 7 K CD . 17239 1 39 . 1 1 4 4 LYS CE C 13 42.138 0.300 . 1 . . . . 7 K CE . 17239 1 40 . 1 1 4 4 LYS CG C 13 24.708 0.300 . 1 . . . . 7 K CG . 17239 1 41 . 1 1 4 4 LYS N N 15 126.342 0.300 . 1 . . . . 7 K N . 17239 1 42 . 1 1 5 5 ARG H H 1 8.524 0.020 . 1 . . . . 8 R HN . 17239 1 43 . 1 1 5 5 ARG HA H 1 4.305 0.020 . 1 . . . . 8 R HA . 17239 1 44 . 1 1 5 5 ARG HB2 H 1 1.850 0.020 . 2 . . . . 8 R HB2 . 17239 1 45 . 1 1 5 5 ARG HB3 H 1 1.766 0.020 . 2 . . . . 8 R HB3 . 17239 1 46 . 1 1 5 5 ARG HD2 H 1 3.204 0.020 . 2 . . . . 8 R QD . 17239 1 47 . 1 1 5 5 ARG HD3 H 1 3.204 0.020 . 2 . . . . 8 R QD . 17239 1 48 . 1 1 5 5 ARG HE H 1 7.422 0.020 . 1 . . . . 8 R HE . 17239 1 49 . 1 1 5 5 ARG HG2 H 1 1.652 0.020 . 2 . . . . 8 R HG2 . 17239 1 50 . 1 1 5 5 ARG HG3 H 1 1.614 0.020 . 2 . . . . 8 R HG3 . 17239 1 51 . 1 1 5 5 ARG CA C 13 56.047 0.300 . 1 . . . . 8 R CA . 17239 1 52 . 1 1 5 5 ARG CB C 13 31.078 0.300 . 1 . . . . 8 R CB . 17239 1 53 . 1 1 5 5 ARG CD C 13 43.347 0.300 . 1 . . . . 8 R CD . 17239 1 54 . 1 1 5 5 ARG CG C 13 27.166 0.300 . 1 . . . . 8 R CG . 17239 1 55 . 1 1 5 5 ARG N N 15 123.678 0.300 . 1 . . . . 8 R N . 17239 1 56 . 1 1 5 5 ARG NE N 15 84.184 0.300 . 1 . . . . 8 R NE . 17239 1 57 . 1 1 6 6 LYS H H 1 8.580 0.020 . 1 . . . . 9 K HN . 17239 1 58 . 1 1 6 6 LYS HA H 1 4.273 0.020 . 1 . . . . 9 K HA . 17239 1 59 . 1 1 6 6 LYS HB2 H 1 1.819 0.020 . 2 . . . . 9 K HB2 . 17239 1 60 . 1 1 6 6 LYS HB3 H 1 1.762 0.020 . 2 . . . . 9 K HB3 . 17239 1 61 . 1 1 6 6 LYS HD2 H 1 1.682 0.020 . 2 . . . . 9 K QD . 17239 1 62 . 1 1 6 6 LYS HD3 H 1 1.682 0.020 . 2 . . . . 9 K QD . 17239 1 63 . 1 1 6 6 LYS HE2 H 1 2.999 0.020 . 2 . . . . 9 K QE . 17239 1 64 . 1 1 6 6 LYS HE3 H 1 2.999 0.020 . 2 . . . . 9 K QE . 17239 1 65 . 1 1 6 6 LYS HG2 H 1 1.447 0.020 . 2 . . . . 9 K HG2 . 17239 1 66 . 1 1 6 6 LYS HG3 H 1 1.413 0.020 . 2 . . . . 9 K HG3 . 17239 1 67 . 1 1 6 6 LYS CA C 13 56.576 0.300 . 1 . . . . 9 K CA . 17239 1 68 . 1 1 6 6 LYS CB C 13 32.988 0.300 . 1 . . . . 9 K CB . 17239 1 69 . 1 1 6 6 LYS CD C 13 29.105 0.300 . 1 . . . . 9 K CD . 17239 1 70 . 1 1 6 6 LYS CE C 13 41.970 0.300 . 1 . . . . 9 K CE . 17239 1 71 . 1 1 6 6 LYS CG C 13 24.636 0.300 . 1 . . . . 9 K CG . 17239 1 72 . 1 1 6 6 LYS N N 15 123.315 0.300 . 1 . . . . 9 K N . 17239 1 73 . 1 1 7 7 ASP H H 1 8.449 0.020 . 1 . . . . 10 D HN . 17239 1 74 . 1 1 7 7 ASP HA H 1 4.563 0.020 . 1 . . . . 10 D HA . 17239 1 75 . 1 1 7 7 ASP HB2 H 1 2.683 0.020 . 2 . . . . 10 D HB2 . 17239 1 76 . 1 1 7 7 ASP HB3 H 1 2.607 0.020 . 2 . . . . 10 D HB3 . 17239 1 77 . 1 1 7 7 ASP CA C 13 54.199 0.300 . 1 . . . . 10 D CA . 17239 1 78 . 1 1 7 7 ASP CB C 13 41.045 0.300 . 1 . . . . 10 D CB . 17239 1 79 . 1 1 7 7 ASP N N 15 121.108 0.300 . 1 . . . . 10 D N . 17239 1 80 . 1 1 8 8 ALA H H 1 8.189 0.020 . 1 . . . . 11 A HN . 17239 1 81 . 1 1 8 8 ALA HA H 1 4.382 0.020 . 1 . . . . 11 A HA . 17239 1 82 . 1 1 8 8 ALA HB1 H 1 1.361 0.020 . 1 . . . . 11 A QB . 17239 1 83 . 1 1 8 8 ALA HB2 H 1 1.361 0.020 . 1 . . . . 11 A QB . 17239 1 84 . 1 1 8 8 ALA HB3 H 1 1.361 0.020 . 1 . . . . 11 A QB . 17239 1 85 . 1 1 8 8 ALA CA C 13 52.050 0.300 . 1 . . . . 11 A CA . 17239 1 86 . 1 1 8 8 ALA CB C 13 19.720 0.300 . 1 . . . . 11 A CB . 17239 1 87 . 1 1 8 8 ALA N N 15 123.848 0.300 . 1 . . . . 11 A N . 17239 1 88 . 1 1 9 9 SER H H 1 8.532 0.020 . 1 . . . . 12 S HN . 17239 1 89 . 1 1 9 9 SER HA H 1 4.743 0.020 . 1 . . . . 12 S HA . 17239 1 90 . 1 1 9 9 SER HB2 H 1 4.135 0.020 . 2 . . . . 12 S HB2 . 17239 1 91 . 1 1 9 9 SER HB3 H 1 3.941 0.020 . 2 . . . . 12 S HB3 . 17239 1 92 . 1 1 9 9 SER CA C 13 56.507 0.300 . 1 . . . . 12 S CA . 17239 1 93 . 1 1 9 9 SER CB C 13 63.166 0.300 . 1 . . . . 12 S CB . 17239 1 94 . 1 1 9 9 SER N N 15 117.014 0.300 . 1 . . . . 12 S N . 17239 1 95 . 1 1 10 10 PRO HA H 1 4.370 0.020 . 1 . . . . 13 P HA . 17239 1 96 . 1 1 10 10 PRO HB2 H 1 2.368 0.020 . 2 . . . . 13 P HB2 . 17239 1 97 . 1 1 10 10 PRO HB3 H 1 1.860 0.020 . 2 . . . . 13 P HB3 . 17239 1 98 . 1 1 10 10 PRO HD2 H 1 3.823 0.020 . 2 . . . . 13 P HD2 . 17239 1 99 . 1 1 10 10 PRO HD3 H 1 3.772 0.020 . 2 . . . . 13 P HD3 . 17239 1 100 . 1 1 10 10 PRO HG2 H 1 2.073 0.020 . 2 . . . . 13 P HG2 . 17239 1 101 . 1 1 10 10 PRO HG3 H 1 2.017 0.020 . 2 . . . . 13 P HG3 . 17239 1 102 . 1 1 10 10 PRO CA C 13 65.109 0.300 . 1 . . . . 13 P CA . 17239 1 103 . 1 1 10 10 PRO CB C 13 31.829 0.300 . 1 . . . . 13 P CB . 17239 1 104 . 1 1 10 10 PRO CD C 13 50.608 0.300 . 1 . . . . 13 P CD . 17239 1 105 . 1 1 10 10 PRO CG C 13 27.815 0.300 . 1 . . . . 13 P CG . 17239 1 106 . 1 1 11 11 GLU H H 1 8.243 0.020 . 1 . . . . 14 E HN . 17239 1 107 . 1 1 11 11 GLU HA H 1 3.744 0.020 . 1 . . . . 14 E HA . 17239 1 108 . 1 1 11 11 GLU HB2 H 1 1.627 0.020 . 2 . . . . 14 E HB2 . 17239 1 109 . 1 1 11 11 GLU HB3 H 1 1.396 0.020 . 2 . . . . 14 E HB3 . 17239 1 110 . 1 1 11 11 GLU HG2 H 1 1.317 0.020 . 2 . . . . 14 E HG2 . 17239 1 111 . 1 1 11 11 GLU HG3 H 1 0.842 0.020 . 2 . . . . 14 E HG3 . 17239 1 112 . 1 1 11 11 GLU CA C 13 59.815 0.300 . 1 . . . . 14 E CA . 17239 1 113 . 1 1 11 11 GLU CB C 13 29.050 0.300 . 1 . . . . 14 E CB . 17239 1 114 . 1 1 11 11 GLU CG C 13 35.761 0.300 . 1 . . . . 14 E CG . 17239 1 115 . 1 1 11 11 GLU N N 15 118.079 0.300 . 1 . . . . 14 E N . 17239 1 116 . 1 1 12 12 GLN H H 1 7.777 0.020 . 1 . . . . 15 Q HN . 17239 1 117 . 1 1 12 12 GLN HA H 1 3.983 0.020 . 1 . . . . 15 Q HA . 17239 1 118 . 1 1 12 12 GLN HB2 H 1 2.106 0.020 . 2 . . . . 15 Q HB2 . 17239 1 119 . 1 1 12 12 GLN HB3 H 1 2.196 0.020 . 2 . . . . 15 Q HB3 . 17239 1 120 . 1 1 12 12 GLN HE21 H 1 7.894 0.020 . 2 . . . . 15 Q HE21 . 17239 1 121 . 1 1 12 12 GLN HE22 H 1 6.903 0.020 . 2 . . . . 15 Q HE22 . 17239 1 122 . 1 1 12 12 GLN HG2 H 1 2.435 0.020 . 2 . . . . 15 Q QG . 17239 1 123 . 1 1 12 12 GLN HG3 H 1 2.435 0.020 . 2 . . . . 15 Q QG . 17239 1 124 . 1 1 12 12 GLN CA C 13 58.720 0.300 . 1 . . . . 15 Q CA . 17239 1 125 . 1 1 12 12 GLN CB C 13 27.913 0.300 . 1 . . . . 15 Q CB . 17239 1 126 . 1 1 12 12 GLN CG C 13 33.365 0.300 . 1 . . . . 15 Q CG . 17239 1 127 . 1 1 12 12 GLN N N 15 118.523 0.300 . 1 . . . . 15 Q N . 17239 1 128 . 1 1 12 12 GLN NE2 N 15 112.159 0.300 . 1 . . . . 15 Q NE2 . 17239 1 129 . 1 1 13 13 GLU H H 1 8.363 0.020 . 1 . . . . 16 E HN . 17239 1 130 . 1 1 13 13 GLU HA H 1 4.063 0.020 . 1 . . . . 16 E HA . 17239 1 131 . 1 1 13 13 GLU HB2 H 1 2.085 0.020 . 2 . . . . 16 E QB . 17239 1 132 . 1 1 13 13 GLU HB3 H 1 2.085 0.020 . 2 . . . . 16 E QB . 17239 1 133 . 1 1 13 13 GLU HG2 H 1 2.399 0.020 . 2 . . . . 16 E HG2 . 17239 1 134 . 1 1 13 13 GLU HG3 H 1 2.229 0.020 . 2 . . . . 16 E HG3 . 17239 1 135 . 1 1 13 13 GLU CA C 13 59.508 0.300 . 1 . . . . 16 E CA . 17239 1 136 . 1 1 13 13 GLU CB C 13 29.593 0.300 . 1 . . . . 16 E CB . 17239 1 137 . 1 1 13 13 GLU CG C 13 36.571 0.300 . 1 . . . . 16 E CG . 17239 1 138 . 1 1 13 13 GLU N N 15 118.531 0.300 . 1 . . . . 16 E N . 17239 1 139 . 1 1 14 14 ALA H H 1 8.004 0.020 . 1 . . . . 17 A HN . 17239 1 140 . 1 1 14 14 ALA HA H 1 4.311 0.020 . 1 . . . . 17 A HA . 17239 1 141 . 1 1 14 14 ALA HB1 H 1 1.845 0.020 . 1 . . . . 17 A QB . 17239 1 142 . 1 1 14 14 ALA HB2 H 1 1.845 0.020 . 1 . . . . 17 A QB . 17239 1 143 . 1 1 14 14 ALA HB3 H 1 1.845 0.020 . 1 . . . . 17 A QB . 17239 1 144 . 1 1 14 14 ALA CA C 13 55.525 0.300 . 1 . . . . 17 A CA . 17239 1 145 . 1 1 14 14 ALA CB C 13 18.435 0.300 . 1 . . . . 17 A CB . 17239 1 146 . 1 1 14 14 ALA N N 15 122.294 0.300 . 1 . . . . 17 A N . 17239 1 147 . 1 1 15 15 ILE H H 1 8.479 0.020 . 1 . . . . 18 I HN . 17239 1 148 . 1 1 15 15 ILE HA H 1 3.440 0.020 . 1 . . . . 18 I HA . 17239 1 149 . 1 1 15 15 ILE HB H 1 2.077 0.020 . 1 . . . . 18 I HB . 17239 1 150 . 1 1 15 15 ILE HD11 H 1 1.008 0.020 . 1 . . . . 18 I QD1 . 17239 1 151 . 1 1 15 15 ILE HD12 H 1 1.008 0.020 . 1 . . . . 18 I QD1 . 17239 1 152 . 1 1 15 15 ILE HD13 H 1 1.008 0.020 . 1 . . . . 18 I QD1 . 17239 1 153 . 1 1 15 15 ILE HG12 H 1 2.132 0.020 . 1 . . . . 18 I HG12 . 17239 1 154 . 1 1 15 15 ILE HG13 H 1 0.814 0.020 . 1 . . . . 18 I HG13 . 17239 1 155 . 1 1 15 15 ILE HG21 H 1 0.979 0.020 . 1 . . . . 18 I QG2 . 17239 1 156 . 1 1 15 15 ILE HG22 H 1 0.979 0.020 . 1 . . . . 18 I QG2 . 17239 1 157 . 1 1 15 15 ILE HG23 H 1 0.979 0.020 . 1 . . . . 18 I QG2 . 17239 1 158 . 1 1 15 15 ILE CA C 13 65.791 0.300 . 1 . . . . 18 I CA . 17239 1 159 . 1 1 15 15 ILE CB C 13 38.305 0.300 . 1 . . . . 18 I CB . 17239 1 160 . 1 1 15 15 ILE CD1 C 13 14.180 0.300 . 1 . . . . 18 I CD1 . 17239 1 161 . 1 1 15 15 ILE CG1 C 13 30.718 0.300 . 1 . . . . 18 I CG1 . 17239 1 162 . 1 1 15 15 ILE CG2 C 13 16.917 0.300 . 1 . . . . 18 I CG2 . 17239 1 163 . 1 1 15 15 ILE N N 15 118.979 0.300 . 1 . . . . 18 I N . 17239 1 164 . 1 1 16 16 GLU H H 1 8.654 0.020 . 1 . . . . 19 E HN . 17239 1 165 . 1 1 16 16 GLU HA H 1 4.091 0.020 . 1 . . . . 19 E HA . 17239 1 166 . 1 1 16 16 GLU HB2 H 1 2.175 0.020 . 2 . . . . 19 E HB2 . 17239 1 167 . 1 1 16 16 GLU HB3 H 1 2.124 0.020 . 2 . . . . 19 E HB3 . 17239 1 168 . 1 1 16 16 GLU HG2 H 1 2.511 0.020 . 2 . . . . 19 E HG2 . 17239 1 169 . 1 1 16 16 GLU HG3 H 1 2.338 0.020 . 2 . . . . 19 E HG3 . 17239 1 170 . 1 1 16 16 GLU CA C 13 59.758 0.300 . 1 . . . . 19 E CA . 17239 1 171 . 1 1 16 16 GLU CB C 13 28.941 0.300 . 1 . . . . 19 E CB . 17239 1 172 . 1 1 16 16 GLU CG C 13 36.462 0.300 . 1 . . . . 19 E CG . 17239 1 173 . 1 1 16 16 GLU N N 15 121.689 0.300 . 1 . . . . 19 E N . 17239 1 174 . 1 1 17 17 SER H H 1 8.471 0.020 . 1 . . . . 20 S HN . 17239 1 175 . 1 1 17 17 SER HA H 1 4.215 0.020 . 1 . . . . 20 S HA . 17239 1 176 . 1 1 17 17 SER HB2 H 1 4.104 0.020 . 2 . . . . 20 S HB2 . 17239 1 177 . 1 1 17 17 SER HB3 H 1 3.901 0.020 . 2 . . . . 20 S HB3 . 17239 1 178 . 1 1 17 17 SER CA C 13 61.836 0.300 . 1 . . . . 20 S CA . 17239 1 179 . 1 1 17 17 SER CB C 13 63.057 0.300 . 1 . . . . 20 S CB . 17239 1 180 . 1 1 17 17 SER N N 15 116.529 0.300 . 1 . . . . 20 S N . 17239 1 181 . 1 1 18 18 PHE H H 1 8.771 0.020 . 1 . . . . 21 F HN . 17239 1 182 . 1 1 18 18 PHE HA H 1 3.742 0.020 . 1 . . . . 21 F HA . 17239 1 183 . 1 1 18 18 PHE HB2 H 1 3.272 0.020 . 2 . . . . 21 F HB2 . 17239 1 184 . 1 1 18 18 PHE HB3 H 1 2.924 0.020 . 2 . . . . 21 F HB3 . 17239 1 185 . 1 1 18 18 PHE HD1 H 1 6.955 0.020 . 3 . . . . 21 F QD . 17239 1 186 . 1 1 18 18 PHE HD2 H 1 6.955 0.020 . 3 . . . . 21 F QD . 17239 1 187 . 1 1 18 18 PHE HE1 H 1 6.749 0.020 . 3 . . . . 21 F QE . 17239 1 188 . 1 1 18 18 PHE HE2 H 1 6.749 0.020 . 3 . . . . 21 F QE . 17239 1 189 . 1 1 18 18 PHE HZ H 1 6.416 0.020 . 1 . . . . 21 F HZ . 17239 1 190 . 1 1 18 18 PHE CA C 13 62.240 0.300 . 1 . . . . 21 F CA . 17239 1 191 . 1 1 18 18 PHE CB C 13 41.012 0.300 . 1 . . . . 21 F CB . 17239 1 192 . 1 1 18 18 PHE CD1 C 13 131.428 0.300 . 3 . . . . 21 F CD1 . 17239 1 193 . 1 1 18 18 PHE CE1 C 13 131.293 0.300 . 3 . . . . 21 F CE1 . 17239 1 194 . 1 1 18 18 PHE CZ C 13 129.424 0.300 . 1 . . . . 21 F CZ . 17239 1 195 . 1 1 18 18 PHE N N 15 121.956 0.300 . 1 . . . . 21 F N . 17239 1 196 . 1 1 19 19 THR H H 1 8.934 0.020 . 1 . . . . 22 T HN . 17239 1 197 . 1 1 19 19 THR HA H 1 3.996 0.020 . 1 . . . . 22 T HA . 17239 1 198 . 1 1 19 19 THR HB H 1 4.262 0.020 . 1 . . . . 22 T HB . 17239 1 199 . 1 1 19 19 THR HG21 H 1 1.340 0.020 . 1 . . . . 22 T QG2 . 17239 1 200 . 1 1 19 19 THR HG22 H 1 1.340 0.020 . 1 . . . . 22 T QG2 . 17239 1 201 . 1 1 19 19 THR HG23 H 1 1.340 0.020 . 1 . . . . 22 T QG2 . 17239 1 202 . 1 1 19 19 THR CA C 13 66.700 0.300 . 1 . . . . 22 T CA . 17239 1 203 . 1 1 19 19 THR CB C 13 69.632 0.300 . 1 . . . . 22 T CB . 17239 1 204 . 1 1 19 19 THR CG2 C 13 21.510 0.300 . 1 . . . . 22 T CG2 . 17239 1 205 . 1 1 19 19 THR N N 15 117.289 0.300 . 1 . . . . 22 T N . 17239 1 206 . 1 1 20 20 SER H H 1 8.244 0.020 . 1 . . . . 23 S HN . 17239 1 207 . 1 1 20 20 SER HA H 1 4.128 0.020 . 1 . . . . 23 S HA . 17239 1 208 . 1 1 20 20 SER HB2 H 1 3.983 0.020 . 2 . . . . 23 S HB2 . 17239 1 209 . 1 1 20 20 SER HB3 H 1 3.934 0.020 . 2 . . . . 23 S HB3 . 17239 1 210 . 1 1 20 20 SER CA C 13 61.378 0.300 . 1 . . . . 23 S CA . 17239 1 211 . 1 1 20 20 SER CB C 13 62.967 0.300 . 1 . . . . 23 S CB . 17239 1 212 . 1 1 20 20 SER N N 15 116.340 0.300 . 1 . . . . 23 S N . 17239 1 213 . 1 1 21 21 LEU H H 1 7.358 0.020 . 1 . . . . 24 L HN . 17239 1 214 . 1 1 21 21 LEU HA H 1 3.680 0.020 . 1 . . . . 24 L HA . 17239 1 215 . 1 1 21 21 LEU HB2 H 1 1.497 0.020 . 2 . . . . 24 L HB2 . 17239 1 216 . 1 1 21 21 LEU HB3 H 1 1.117 0.020 . 2 . . . . 24 L HB3 . 17239 1 217 . 1 1 21 21 LEU HD11 H 1 0.503 0.020 . 2 . . . . 24 L QD1 . 17239 1 218 . 1 1 21 21 LEU HD12 H 1 0.503 0.020 . 2 . . . . 24 L QD1 . 17239 1 219 . 1 1 21 21 LEU HD13 H 1 0.503 0.020 . 2 . . . . 24 L QD1 . 17239 1 220 . 1 1 21 21 LEU HD21 H 1 0.387 0.020 . 2 . . . . 24 L QD2 . 17239 1 221 . 1 1 21 21 LEU HD22 H 1 0.387 0.020 . 2 . . . . 24 L QD2 . 17239 1 222 . 1 1 21 21 LEU HD23 H 1 0.387 0.020 . 2 . . . . 24 L QD2 . 17239 1 223 . 1 1 21 21 LEU HG H 1 1.104 0.020 . 1 . . . . 24 L HG . 17239 1 224 . 1 1 21 21 LEU CA C 13 58.112 0.300 . 1 . . . . 24 L CA . 17239 1 225 . 1 1 21 21 LEU CB C 13 43.322 0.300 . 1 . . . . 24 L CB . 17239 1 226 . 1 1 21 21 LEU CD1 C 13 25.963 0.300 . 2 . . . . 24 L CD1 . 17239 1 227 . 1 1 21 21 LEU CD2 C 13 24.287 0.300 . 2 . . . . 24 L CD2 . 17239 1 228 . 1 1 21 21 LEU CG C 13 28.231 0.300 . 1 . . . . 24 L CG . 17239 1 229 . 1 1 21 21 LEU N N 15 119.449 0.300 . 1 . . . . 24 L N . 17239 1 230 . 1 1 22 22 THR H H 1 7.480 0.020 . 1 . . . . 25 T HN . 17239 1 231 . 1 1 22 22 THR HA H 1 4.073 0.020 . 1 . . . . 25 T HA . 17239 1 232 . 1 1 22 22 THR HB H 1 3.528 0.020 . 1 . . . . 25 T HB . 17239 1 233 . 1 1 22 22 THR HG21 H 1 -0.063 0.020 . 1 . . . . 25 T QG2 . 17239 1 234 . 1 1 22 22 THR HG22 H 1 -0.063 0.020 . 1 . . . . 25 T QG2 . 17239 1 235 . 1 1 22 22 THR HG23 H 1 -0.063 0.020 . 1 . . . . 25 T QG2 . 17239 1 236 . 1 1 22 22 THR CA C 13 62.904 0.300 . 1 . . . . 25 T CA . 17239 1 237 . 1 1 22 22 THR CB C 13 71.441 0.300 . 1 . . . . 25 T CB . 17239 1 238 . 1 1 22 22 THR CG2 C 13 20.618 0.300 . 1 . . . . 25 T CG2 . 17239 1 239 . 1 1 22 22 THR N N 15 104.931 0.300 . 1 . . . . 25 T N . 17239 1 240 . 1 1 23 23 LYS H H 1 8.175 0.020 . 1 . . . . 26 K HN . 17239 1 241 . 1 1 23 23 LYS HA H 1 4.016 0.020 . 1 . . . . 26 K HA . 17239 1 242 . 1 1 23 23 LYS HB2 H 1 2.159 0.020 . 2 . . . . 26 K HB2 . 17239 1 243 . 1 1 23 23 LYS HB3 H 1 1.968 0.020 . 2 . . . . 26 K HB3 . 17239 1 244 . 1 1 23 23 LYS HD2 H 1 1.501 0.020 . 2 . . . . 26 K QD . 17239 1 245 . 1 1 23 23 LYS HD3 H 1 1.501 0.020 . 2 . . . . 26 K QD . 17239 1 246 . 1 1 23 23 LYS HE2 H 1 2.853 0.020 . 2 . . . . 26 K HE2 . 17239 1 247 . 1 1 23 23 LYS HE3 H 1 2.783 0.020 . 2 . . . . 26 K HE3 . 17239 1 248 . 1 1 23 23 LYS HG2 H 1 1.184 0.020 . 2 . . . . 26 K HG2 . 17239 1 249 . 1 1 23 23 LYS HG3 H 1 1.040 0.020 . 2 . . . . 26 K HG3 . 17239 1 250 . 1 1 23 23 LYS CA C 13 56.438 0.300 . 1 . . . . 26 K CA . 17239 1 251 . 1 1 23 23 LYS CB C 13 28.470 0.300 . 1 . . . . 26 K CB . 17239 1 252 . 1 1 23 23 LYS CD C 13 28.247 0.300 . 1 . . . . 26 K CD . 17239 1 253 . 1 1 23 23 LYS CE C 13 42.365 0.300 . 1 . . . . 26 K CE . 17239 1 254 . 1 1 23 23 LYS CG C 13 24.680 0.300 . 1 . . . . 26 K CG . 17239 1 255 . 1 1 23 23 LYS N N 15 114.359 0.300 . 1 . . . . 26 K N . 17239 1 256 . 1 1 24 24 CYS H H 1 7.730 0.020 . 1 . . . . 27 C HN . 17239 1 257 . 1 1 24 24 CYS HA H 1 4.610 0.020 . 1 . . . . 27 C HA . 17239 1 258 . 1 1 24 24 CYS HB2 H 1 3.156 0.020 . 2 . . . . 27 C HB2 . 17239 1 259 . 1 1 24 24 CYS HB3 H 1 2.613 0.020 . 2 . . . . 27 C HB3 . 17239 1 260 . 1 1 24 24 CYS CA C 13 57.142 0.300 . 1 . . . . 27 C CA . 17239 1 261 . 1 1 24 24 CYS CB C 13 29.871 0.300 . 1 . . . . 27 C CB . 17239 1 262 . 1 1 24 24 CYS N N 15 116.088 0.300 . 1 . . . . 27 C N . 17239 1 263 . 1 1 25 25 ASP H H 1 8.482 0.020 . 1 . . . . 28 D HN . 17239 1 264 . 1 1 25 25 ASP HA H 1 4.841 0.020 . 1 . . . . 28 D HA . 17239 1 265 . 1 1 25 25 ASP HB2 H 1 2.804 0.020 . 2 . . . . 28 D HB2 . 17239 1 266 . 1 1 25 25 ASP HB3 H 1 2.702 0.020 . 2 . . . . 28 D HB3 . 17239 1 267 . 1 1 25 25 ASP CA C 13 52.368 0.300 . 1 . . . . 28 D CA . 17239 1 268 . 1 1 25 25 ASP CB C 13 42.907 0.300 . 1 . . . . 28 D CB . 17239 1 269 . 1 1 25 25 ASP N N 15 120.537 0.300 . 1 . . . . 28 D N . 17239 1 270 . 1 1 26 26 PRO HA H 1 4.279 0.020 . 1 . . . . 29 P HA . 17239 1 271 . 1 1 26 26 PRO HB2 H 1 2.361 0.020 . 2 . . . . 29 P HB2 . 17239 1 272 . 1 1 26 26 PRO HB3 H 1 1.983 0.020 . 2 . . . . 29 P HB3 . 17239 1 273 . 1 1 26 26 PRO HD2 H 1 3.956 0.020 . 2 . . . . 29 P HD2 . 17239 1 274 . 1 1 26 26 PRO HD3 H 1 3.871 0.020 . 2 . . . . 29 P HD3 . 17239 1 275 . 1 1 26 26 PRO HG2 H 1 2.161 0.020 . 2 . . . . 29 P HG2 . 17239 1 276 . 1 1 26 26 PRO HG3 H 1 2.106 0.020 . 2 . . . . 29 P HG3 . 17239 1 277 . 1 1 26 26 PRO CA C 13 65.889 0.300 . 1 . . . . 29 P CA . 17239 1 278 . 1 1 26 26 PRO CB C 13 32.279 0.300 . 1 . . . . 29 P CB . 17239 1 279 . 1 1 26 26 PRO CD C 13 51.092 0.300 . 1 . . . . 29 P CD . 17239 1 280 . 1 1 26 26 PRO CG C 13 27.762 0.300 . 1 . . . . 29 P CG . 17239 1 281 . 1 1 27 27 LYS H H 1 9.158 0.020 . 1 . . . . 30 K HN . 17239 1 282 . 1 1 27 27 LYS HA H 1 4.062 0.020 . 1 . . . . 30 K HA . 17239 1 283 . 1 1 27 27 LYS HB2 H 1 1.894 0.020 . 2 . . . . 30 K HB2 . 17239 1 284 . 1 1 27 27 LYS HB3 H 1 1.804 0.020 . 2 . . . . 30 K HB3 . 17239 1 285 . 1 1 27 27 LYS HD2 H 1 1.728 0.020 . 2 . . . . 30 K QD . 17239 1 286 . 1 1 27 27 LYS HD3 H 1 1.728 0.020 . 2 . . . . 30 K QD . 17239 1 287 . 1 1 27 27 LYS HE2 H 1 3.019 0.020 . 2 . . . . 30 K QE . 17239 1 288 . 1 1 27 27 LYS HE3 H 1 3.019 0.020 . 2 . . . . 30 K QE . 17239 1 289 . 1 1 27 27 LYS HG2 H 1 1.570 0.020 . 2 . . . . 30 K HG2 . 17239 1 290 . 1 1 27 27 LYS HG3 H 1 1.460 0.020 . 2 . . . . 30 K HG3 . 17239 1 291 . 1 1 27 27 LYS CA C 13 60.024 0.300 . 1 . . . . 30 K CA . 17239 1 292 . 1 1 27 27 LYS CB C 13 32.123 0.300 . 1 . . . . 30 K CB . 17239 1 293 . 1 1 27 27 LYS CD C 13 29.250 0.300 . 1 . . . . 30 K CD . 17239 1 294 . 1 1 27 27 LYS CE C 13 41.734 0.300 . 1 . . . . 30 K CE . 17239 1 295 . 1 1 27 27 LYS CG C 13 25.456 0.300 . 1 . . . . 30 K CG . 17239 1 296 . 1 1 27 27 LYS N N 15 118.803 0.300 . 1 . . . . 30 K N . 17239 1 297 . 1 1 28 28 VAL H H 1 7.987 0.020 . 1 . . . . 31 V HN . 17239 1 298 . 1 1 28 28 VAL HA H 1 3.741 0.020 . 1 . . . . 31 V HA . 17239 1 299 . 1 1 28 28 VAL HB H 1 2.603 0.020 . 1 . . . . 31 V HB . 17239 1 300 . 1 1 28 28 VAL HG11 H 1 1.364 0.020 . 2 . . . . 31 V QG1 . 17239 1 301 . 1 1 28 28 VAL HG12 H 1 1.364 0.020 . 2 . . . . 31 V QG1 . 17239 1 302 . 1 1 28 28 VAL HG13 H 1 1.364 0.020 . 2 . . . . 31 V QG1 . 17239 1 303 . 1 1 28 28 VAL HG21 H 1 1.232 0.020 . 2 . . . . 31 V QG2 . 17239 1 304 . 1 1 28 28 VAL HG22 H 1 1.232 0.020 . 2 . . . . 31 V QG2 . 17239 1 305 . 1 1 28 28 VAL HG23 H 1 1.232 0.020 . 2 . . . . 31 V QG2 . 17239 1 306 . 1 1 28 28 VAL CA C 13 65.951 0.300 . 1 . . . . 31 V CA . 17239 1 307 . 1 1 28 28 VAL CB C 13 31.788 0.300 . 1 . . . . 31 V CB . 17239 1 308 . 1 1 28 28 VAL CG1 C 13 22.015 0.300 . 2 . . . . 31 V CG1 . 17239 1 309 . 1 1 28 28 VAL CG2 C 13 23.097 0.300 . 2 . . . . 31 V CG2 . 17239 1 310 . 1 1 28 28 VAL N N 15 122.733 0.300 . 1 . . . . 31 V N . 17239 1 311 . 1 1 29 29 SER H H 1 7.743 0.020 . 1 . . . . 32 S HN . 17239 1 312 . 1 1 29 29 SER HA H 1 3.383 0.020 . 1 . . . . 32 S HA . 17239 1 313 . 1 1 29 29 SER HB2 H 1 3.461 0.020 . 2 . . . . 32 S HB2 . 17239 1 314 . 1 1 29 29 SER HB3 H 1 3.939 0.020 . 2 . . . . 32 S HB3 . 17239 1 315 . 1 1 29 29 SER CA C 13 60.590 0.300 . 1 . . . . 32 S CA . 17239 1 316 . 1 1 29 29 SER CB C 13 62.255 0.300 . 1 . . . . 32 S CB . 17239 1 317 . 1 1 29 29 SER N N 15 116.053 0.300 . 1 . . . . 32 S N . 17239 1 318 . 1 1 30 30 ARG H H 1 7.743 0.020 . 1 . . . . 33 R HN . 17239 1 319 . 1 1 30 30 ARG HA H 1 3.392 0.020 . 1 . . . . 33 R HA . 17239 1 320 . 1 1 30 30 ARG HB2 H 1 1.832 0.020 . 2 . . . . 33 R HB2 . 17239 1 321 . 1 1 30 30 ARG HB3 H 1 1.778 0.020 . 2 . . . . 33 R HB3 . 17239 1 322 . 1 1 30 30 ARG HD2 H 1 3.402 0.020 . 2 . . . . 33 R HD2 . 17239 1 323 . 1 1 30 30 ARG HD3 H 1 3.206 0.020 . 2 . . . . 33 R HD3 . 17239 1 324 . 1 1 30 30 ARG HE H 1 7.527 0.020 . 1 . . . . 33 R HE . 17239 1 325 . 1 1 30 30 ARG HG2 H 1 1.653 0.020 . 2 . . . . 33 R HG2 . 17239 1 326 . 1 1 30 30 ARG HG3 H 1 1.560 0.020 . 2 . . . . 33 R HG3 . 17239 1 327 . 1 1 30 30 ARG CA C 13 60.296 0.300 . 1 . . . . 33 R CA . 17239 1 328 . 1 1 30 30 ARG CB C 13 30.027 0.300 . 1 . . . . 33 R CB . 17239 1 329 . 1 1 30 30 ARG CD C 13 43.151 0.300 . 1 . . . . 33 R CD . 17239 1 330 . 1 1 30 30 ARG CG C 13 28.289 0.300 . 1 . . . . 33 R CG . 17239 1 331 . 1 1 30 30 ARG N N 15 118.020 0.300 . 1 . . . . 33 R N . 17239 1 332 . 1 1 30 30 ARG NE N 15 83.201 0.300 . 1 . . . . 33 R NE . 17239 1 333 . 1 1 31 31 LYS H H 1 7.201 0.020 . 1 . . . . 34 K HN . 17239 1 334 . 1 1 31 31 LYS HA H 1 3.841 0.020 . 1 . . . . 34 K HA . 17239 1 335 . 1 1 31 31 LYS HB2 H 1 1.835 0.020 . 2 . . . . 34 K QB . 17239 1 336 . 1 1 31 31 LYS HB3 H 1 1.835 0.020 . 2 . . . . 34 K QB . 17239 1 337 . 1 1 31 31 LYS HD2 H 1 1.566 0.020 . 2 . . . . 34 K HD2 . 17239 1 338 . 1 1 31 31 LYS HD3 H 1 1.511 0.020 . 2 . . . . 34 K HD3 . 17239 1 339 . 1 1 31 31 LYS HE2 H 1 2.698 0.020 . 2 . . . . 34 K HE2 . 17239 1 340 . 1 1 31 31 LYS HE3 H 1 2.654 0.020 . 2 . . . . 34 K HE3 . 17239 1 341 . 1 1 31 31 LYS HG2 H 1 1.358 0.020 . 2 . . . . 34 K HG2 . 17239 1 342 . 1 1 31 31 LYS HG3 H 1 0.779 0.020 . 2 . . . . 34 K HG3 . 17239 1 343 . 1 1 31 31 LYS CA C 13 59.509 0.300 . 1 . . . . 34 K CA . 17239 1 344 . 1 1 31 31 LYS CB C 13 31.880 0.300 . 1 . . . . 34 K CB . 17239 1 345 . 1 1 31 31 LYS CD C 13 29.496 0.300 . 1 . . . . 34 K CD . 17239 1 346 . 1 1 31 31 LYS CE C 13 41.877 0.300 . 1 . . . . 34 K CE . 17239 1 347 . 1 1 31 31 LYS CG C 13 24.410 0.300 . 1 . . . . 34 K CG . 17239 1 348 . 1 1 31 31 LYS N N 15 118.056 0.300 . 1 . . . . 34 K N . 17239 1 349 . 1 1 32 32 TYR H H 1 7.750 0.020 . 1 . . . . 35 Y HN . 17239 1 350 . 1 1 32 32 TYR HA H 1 3.640 0.020 . 1 . . . . 35 Y HA . 17239 1 351 . 1 1 32 32 TYR HB2 H 1 2.622 0.020 . 2 . . . . 35 Y HB2 . 17239 1 352 . 1 1 32 32 TYR HB3 H 1 2.382 0.020 . 2 . . . . 35 Y HB3 . 17239 1 353 . 1 1 32 32 TYR HD1 H 1 7.312 0.020 . 3 . . . . 35 Y QD . 17239 1 354 . 1 1 32 32 TYR HD2 H 1 7.312 0.020 . 3 . . . . 35 Y QD . 17239 1 355 . 1 1 32 32 TYR HE1 H 1 6.758 0.020 . 3 . . . . 35 Y QE . 17239 1 356 . 1 1 32 32 TYR HE2 H 1 6.758 0.020 . 3 . . . . 35 Y QE . 17239 1 357 . 1 1 32 32 TYR CA C 13 63.648 0.300 . 1 . . . . 35 Y CA . 17239 1 358 . 1 1 32 32 TYR CB C 13 39.138 0.300 . 1 . . . . 35 Y CB . 17239 1 359 . 1 1 32 32 TYR CD1 C 13 132.747 0.300 . 3 . . . . 35 Y CD1 . 17239 1 360 . 1 1 32 32 TYR CE1 C 13 119.094 0.300 . 3 . . . . 35 Y CE1 . 17239 1 361 . 1 1 32 32 TYR N N 15 115.507 0.300 . 1 . . . . 35 Y N . 17239 1 362 . 1 1 33 33 LEU H H 1 8.006 0.020 . 1 . . . . 36 L HN . 17239 1 363 . 1 1 33 33 LEU HA H 1 3.273 0.020 . 1 . . . . 36 L HA . 17239 1 364 . 1 1 33 33 LEU HB2 H 1 0.807 0.020 . 2 . . . . 36 L HB2 . 17239 1 365 . 1 1 33 33 LEU HB3 H 1 0.004 0.020 . 2 . . . . 36 L HB3 . 17239 1 366 . 1 1 33 33 LEU HD11 H 1 0.570 0.020 . 2 . . . . 36 L QD1 . 17239 1 367 . 1 1 33 33 LEU HD12 H 1 0.570 0.020 . 2 . . . . 36 L QD1 . 17239 1 368 . 1 1 33 33 LEU HD13 H 1 0.570 0.020 . 2 . . . . 36 L QD1 . 17239 1 369 . 1 1 33 33 LEU HD21 H 1 0.559 0.020 . 2 . . . . 36 L QD2 . 17239 1 370 . 1 1 33 33 LEU HD22 H 1 0.559 0.020 . 2 . . . . 36 L QD2 . 17239 1 371 . 1 1 33 33 LEU HD23 H 1 0.559 0.020 . 2 . . . . 36 L QD2 . 17239 1 372 . 1 1 33 33 LEU HG H 1 0.842 0.020 . 1 . . . . 36 L HG . 17239 1 373 . 1 1 33 33 LEU CA C 13 58.535 0.300 . 1 . . . . 36 L CA . 17239 1 374 . 1 1 33 33 LEU CB C 13 40.582 0.300 . 1 . . . . 36 L CB . 17239 1 375 . 1 1 33 33 LEU CD1 C 13 26.037 0.300 . 2 . . . . 36 L CD1 . 17239 1 376 . 1 1 33 33 LEU CD2 C 13 23.574 0.300 . 2 . . . . 36 L CD2 . 17239 1 377 . 1 1 33 33 LEU CG C 13 27.941 0.300 . 1 . . . . 36 L CG . 17239 1 378 . 1 1 33 33 LEU N N 15 120.835 0.300 . 1 . . . . 36 L N . 17239 1 379 . 1 1 34 34 GLN H H 1 8.315 0.020 . 1 . . . . 37 Q HN . 17239 1 380 . 1 1 34 34 GLN HA H 1 3.085 0.020 . 1 . . . . 37 Q HA . 17239 1 381 . 1 1 34 34 GLN HB2 H 1 2.013 0.020 . 2 . . . . 37 Q HB2 . 17239 1 382 . 1 1 34 34 GLN HB3 H 1 1.853 0.020 . 2 . . . . 37 Q HB3 . 17239 1 383 . 1 1 34 34 GLN HE21 H 1 7.565 0.020 . 2 . . . . 37 Q HE21 . 17239 1 384 . 1 1 34 34 GLN HE22 H 1 7.002 0.020 . 2 . . . . 37 Q HE22 . 17239 1 385 . 1 1 34 34 GLN HG2 H 1 2.433 0.020 . 2 . . . . 37 Q HG2 . 17239 1 386 . 1 1 34 34 GLN HG3 H 1 2.372 0.020 . 2 . . . . 37 Q HG3 . 17239 1 387 . 1 1 34 34 GLN CA C 13 58.990 0.300 . 1 . . . . 37 Q CA . 17239 1 388 . 1 1 34 34 GLN CB C 13 27.977 0.300 . 1 . . . . 37 Q CB . 17239 1 389 . 1 1 34 34 GLN CG C 13 34.022 0.300 . 1 . . . . 37 Q CG . 17239 1 390 . 1 1 34 34 GLN N N 15 119.012 0.300 . 1 . . . . 37 Q N . 17239 1 391 . 1 1 34 34 GLN NE2 N 15 111.624 0.300 . 1 . . . . 37 Q NE2 . 17239 1 392 . 1 1 35 35 ARG H H 1 7.173 0.020 . 1 . . . . 38 R HN . 17239 1 393 . 1 1 35 35 ARG HA H 1 4.215 0.020 . 1 . . . . 38 R HA . 17239 1 394 . 1 1 35 35 ARG HB2 H 1 1.902 0.020 . 2 . . . . 38 R HB2 . 17239 1 395 . 1 1 35 35 ARG HB3 H 1 1.626 0.020 . 2 . . . . 38 R HB3 . 17239 1 396 . 1 1 35 35 ARG HD2 H 1 2.886 0.020 . 2 . . . . 38 R HD2 . 17239 1 397 . 1 1 35 35 ARG HD3 H 1 2.801 0.020 . 2 . . . . 38 R HD3 . 17239 1 398 . 1 1 35 35 ARG HE H 1 7.824 0.020 . 1 . . . . 38 R HE . 17239 1 399 . 1 1 35 35 ARG HG2 H 1 1.655 0.020 . 2 . . . . 38 R HG2 . 17239 1 400 . 1 1 35 35 ARG HG3 H 1 1.504 0.020 . 2 . . . . 38 R HG3 . 17239 1 401 . 1 1 35 35 ARG CA C 13 57.111 0.300 . 1 . . . . 38 R CA . 17239 1 402 . 1 1 35 35 ARG CB C 13 30.277 0.300 . 1 . . . . 38 R CB . 17239 1 403 . 1 1 35 35 ARG CD C 13 44.040 0.300 . 1 . . . . 38 R CD . 17239 1 404 . 1 1 35 35 ARG CG C 13 26.146 0.300 . 1 . . . . 38 R CG . 17239 1 405 . 1 1 35 35 ARG N N 15 115.784 0.300 . 1 . . . . 38 R N . 17239 1 406 . 1 1 35 35 ARG NE N 15 83.273 0.300 . 1 . . . . 38 R NE . 17239 1 407 . 1 1 36 36 ASN H H 1 7.007 0.020 . 1 . . . . 39 N HN . 17239 1 408 . 1 1 36 36 ASN HA H 1 4.944 0.020 . 1 . . . . 39 N HA . 17239 1 409 . 1 1 36 36 ASN HB2 H 1 3.217 0.020 . 2 . . . . 39 N HB2 . 17239 1 410 . 1 1 36 36 ASN HB3 H 1 2.358 0.020 . 2 . . . . 39 N HB3 . 17239 1 411 . 1 1 36 36 ASN HD21 H 1 9.354 0.020 . 2 . . . . 39 N HD21 . 17239 1 412 . 1 1 36 36 ASN HD22 H 1 8.417 0.020 . 2 . . . . 39 N HD22 . 17239 1 413 . 1 1 36 36 ASN CA C 13 53.654 0.300 . 1 . . . . 39 N CA . 17239 1 414 . 1 1 36 36 ASN CB C 13 40.068 0.300 . 1 . . . . 39 N CB . 17239 1 415 . 1 1 36 36 ASN N N 15 116.640 0.300 . 1 . . . . 39 N N . 17239 1 416 . 1 1 36 36 ASN ND2 N 15 119.927 0.300 . 1 . . . . 39 N ND2 . 17239 1 417 . 1 1 37 37 HIS H H 1 7.847 0.020 . 1 . . . . 40 H HN . 17239 1 418 . 1 1 37 37 HIS HA H 1 4.366 0.020 . 1 . . . . 40 H HA . 17239 1 419 . 1 1 37 37 HIS HB2 H 1 3.497 0.020 . 2 . . . . 40 H HB2 . 17239 1 420 . 1 1 37 37 HIS HB3 H 1 3.454 0.020 . 2 . . . . 40 H HB3 . 17239 1 421 . 1 1 37 37 HIS HD2 H 1 7.293 0.020 . 1 . . . . 40 H HD2 . 17239 1 422 . 1 1 37 37 HIS HE1 H 1 8.487 0.020 . 1 . . . . 40 H HE1 . 17239 1 423 . 1 1 37 37 HIS CA C 13 57.342 0.300 . 1 . . . . 40 H CA . 17239 1 424 . 1 1 37 37 HIS CB C 13 26.290 0.300 . 1 . . . . 40 H CB . 17239 1 425 . 1 1 37 37 HIS CD2 C 13 119.947 0.300 . 1 . . . . 40 H CD2 . 17239 1 426 . 1 1 37 37 HIS CE1 C 13 136.483 0.300 . 1 . . . . 40 H CE1 . 17239 1 427 . 1 1 37 37 HIS N N 15 112.902 0.300 . 1 . . . . 40 H N . 17239 1 428 . 1 1 38 38 TRP H H 1 8.603 0.020 . 1 . . . . 41 W HN . 17239 1 429 . 1 1 38 38 TRP HA H 1 3.160 0.020 . 1 . . . . 41 W HA . 17239 1 430 . 1 1 38 38 TRP HB2 H 1 3.603 0.020 . 2 . . . . 41 W HB2 . 17239 1 431 . 1 1 38 38 TRP HB3 H 1 3.300 0.020 . 2 . . . . 41 W HB3 . 17239 1 432 . 1 1 38 38 TRP HD1 H 1 7.160 0.020 . 1 . . . . 41 W HD1 . 17239 1 433 . 1 1 38 38 TRP HE1 H 1 10.203 0.020 . 1 . . . . 41 W HE1 . 17239 1 434 . 1 1 38 38 TRP HE3 H 1 7.366 0.020 . 1 . . . . 41 W HE3 . 17239 1 435 . 1 1 38 38 TRP HH2 H 1 6.962 0.020 . 1 . . . . 41 W HH2 . 17239 1 436 . 1 1 38 38 TRP HZ2 H 1 7.424 0.020 . 1 . . . . 41 W HZ2 . 17239 1 437 . 1 1 38 38 TRP HZ3 H 1 7.176 0.020 . 1 . . . . 41 W HZ3 . 17239 1 438 . 1 1 38 38 TRP CA C 13 59.690 0.300 . 1 . . . . 41 W CA . 17239 1 439 . 1 1 38 38 TRP CB C 13 24.542 0.300 . 1 . . . . 41 W CB . 17239 1 440 . 1 1 38 38 TRP CD1 C 13 127.354 0.300 . 1 . . . . 41 W CD1 . 17239 1 441 . 1 1 38 38 TRP CE3 C 13 119.632 0.300 . 1 . . . . 41 W CE3 . 17239 1 442 . 1 1 38 38 TRP CH2 C 13 123.638 0.300 . 1 . . . . 41 W CH2 . 17239 1 443 . 1 1 38 38 TRP CZ2 C 13 114.822 0.300 . 1 . . . . 41 W CZ2 . 17239 1 444 . 1 1 38 38 TRP CZ3 C 13 122.821 0.300 . 1 . . . . 41 W CZ3 . 17239 1 445 . 1 1 38 38 TRP N N 15 109.687 0.300 . 1 . . . . 41 W N . 17239 1 446 . 1 1 38 38 TRP NE1 N 15 128.713 0.300 . 1 . . . . 41 W NE1 . 17239 1 447 . 1 1 39 39 ASN H H 1 7.552 0.020 . 1 . . . . 42 N HN . 17239 1 448 . 1 1 39 39 ASN HA H 1 4.911 0.020 . 1 . . . . 42 N HA . 17239 1 449 . 1 1 39 39 ASN HB2 H 1 3.109 0.020 . 2 . . . . 42 N HB2 . 17239 1 450 . 1 1 39 39 ASN HB3 H 1 2.580 0.020 . 2 . . . . 42 N HB3 . 17239 1 451 . 1 1 39 39 ASN HD21 H 1 7.562 0.020 . 2 . . . . 42 N HD21 . 17239 1 452 . 1 1 39 39 ASN HD22 H 1 6.751 0.020 . 2 . . . . 42 N HD22 . 17239 1 453 . 1 1 39 39 ASN CA C 13 52.390 0.300 . 1 . . . . 42 N CA . 17239 1 454 . 1 1 39 39 ASN CB C 13 39.190 0.300 . 1 . . . . 42 N CB . 17239 1 455 . 1 1 39 39 ASN N N 15 118.197 0.300 . 1 . . . . 42 N N . 17239 1 456 . 1 1 39 39 ASN ND2 N 15 114.023 0.300 . 1 . . . . 42 N ND2 . 17239 1 457 . 1 1 40 40 ILE H H 1 8.962 0.020 . 1 . . . . 43 I HN . 17239 1 458 . 1 1 40 40 ILE HA H 1 3.876 0.020 . 1 . . . . 43 I HA . 17239 1 459 . 1 1 40 40 ILE HB H 1 1.940 0.020 . 1 . . . . 43 I HB . 17239 1 460 . 1 1 40 40 ILE HD11 H 1 1.126 0.020 . 1 . . . . 43 I QD1 . 17239 1 461 . 1 1 40 40 ILE HD12 H 1 1.126 0.020 . 1 . . . . 43 I QD1 . 17239 1 462 . 1 1 40 40 ILE HD13 H 1 1.126 0.020 . 1 . . . . 43 I QD1 . 17239 1 463 . 1 1 40 40 ILE HG12 H 1 1.769 0.020 . 1 . . . . 43 I HG12 . 17239 1 464 . 1 1 40 40 ILE HG13 H 1 1.390 0.020 . 1 . . . . 43 I HG13 . 17239 1 465 . 1 1 40 40 ILE HG21 H 1 1.094 0.020 . 1 . . . . 43 I QG2 . 17239 1 466 . 1 1 40 40 ILE HG22 H 1 1.094 0.020 . 1 . . . . 43 I QG2 . 17239 1 467 . 1 1 40 40 ILE HG23 H 1 1.094 0.020 . 1 . . . . 43 I QG2 . 17239 1 468 . 1 1 40 40 ILE CA C 13 65.196 0.300 . 1 . . . . 43 I CA . 17239 1 469 . 1 1 40 40 ILE CB C 13 38.565 0.300 . 1 . . . . 43 I CB . 17239 1 470 . 1 1 40 40 ILE CD1 C 13 14.494 0.300 . 1 . . . . 43 I CD1 . 17239 1 471 . 1 1 40 40 ILE CG1 C 13 30.193 0.300 . 1 . . . . 43 I CG1 . 17239 1 472 . 1 1 40 40 ILE CG2 C 13 17.230 0.300 . 1 . . . . 43 I CG2 . 17239 1 473 . 1 1 40 40 ILE N N 15 126.806 0.300 . 1 . . . . 43 I N . 17239 1 474 . 1 1 41 41 ASN H H 1 8.205 0.020 . 1 . . . . 44 N HN . 17239 1 475 . 1 1 41 41 ASN HA H 1 4.375 0.020 . 1 . . . . 44 N HA . 17239 1 476 . 1 1 41 41 ASN HB2 H 1 2.863 0.020 . 2 . . . . 44 N QB . 17239 1 477 . 1 1 41 41 ASN HB3 H 1 2.863 0.020 . 2 . . . . 44 N QB . 17239 1 478 . 1 1 41 41 ASN HD21 H 1 7.470 0.020 . 2 . . . . 44 N HD21 . 17239 1 479 . 1 1 41 41 ASN HD22 H 1 7.388 0.020 . 2 . . . . 44 N HD22 . 17239 1 480 . 1 1 41 41 ASN CA C 13 58.002 0.300 . 1 . . . . 44 N CA . 17239 1 481 . 1 1 41 41 ASN CB C 13 39.510 0.300 . 1 . . . . 44 N CB . 17239 1 482 . 1 1 41 41 ASN N N 15 120.092 0.300 . 1 . . . . 44 N N . 17239 1 483 . 1 1 41 41 ASN ND2 N 15 113.079 0.300 . 1 . . . . 44 N ND2 . 17239 1 484 . 1 1 42 42 TYR H H 1 8.507 0.020 . 1 . . . . 45 Y HN . 17239 1 485 . 1 1 42 42 TYR HA H 1 4.430 0.020 . 1 . . . . 45 Y HA . 17239 1 486 . 1 1 42 42 TYR HB2 H 1 3.424 0.020 . 2 . . . . 45 Y HB2 . 17239 1 487 . 1 1 42 42 TYR HB3 H 1 3.275 0.020 . 2 . . . . 45 Y HB3 . 17239 1 488 . 1 1 42 42 TYR HD1 H 1 7.201 0.020 . 3 . . . . 45 Y QD . 17239 1 489 . 1 1 42 42 TYR HD2 H 1 7.201 0.020 . 3 . . . . 45 Y QD . 17239 1 490 . 1 1 42 42 TYR HE1 H 1 6.894 0.020 . 3 . . . . 45 Y QE . 17239 1 491 . 1 1 42 42 TYR HE2 H 1 6.894 0.020 . 3 . . . . 45 Y QE . 17239 1 492 . 1 1 42 42 TYR CA C 13 59.549 0.300 . 1 . . . . 45 Y CA . 17239 1 493 . 1 1 42 42 TYR CB C 13 36.700 0.300 . 1 . . . . 45 Y CB . 17239 1 494 . 1 1 42 42 TYR CD1 C 13 131.813 0.300 . 3 . . . . 45 Y CD1 . 17239 1 495 . 1 1 42 42 TYR CE1 C 13 118.494 0.300 . 3 . . . . 45 Y CE1 . 17239 1 496 . 1 1 42 42 TYR N N 15 120.589 0.300 . 1 . . . . 45 Y N . 17239 1 497 . 1 1 43 43 ALA H H 1 8.889 0.020 . 1 . . . . 46 A HN . 17239 1 498 . 1 1 43 43 ALA HA H 1 4.433 0.020 . 1 . . . . 46 A HA . 17239 1 499 . 1 1 43 43 ALA HB1 H 1 1.456 0.020 . 1 . . . . 46 A QB . 17239 1 500 . 1 1 43 43 ALA HB2 H 1 1.456 0.020 . 1 . . . . 46 A QB . 17239 1 501 . 1 1 43 43 ALA HB3 H 1 1.456 0.020 . 1 . . . . 46 A QB . 17239 1 502 . 1 1 43 43 ALA CA C 13 55.443 0.300 . 1 . . . . 46 A CA . 17239 1 503 . 1 1 43 43 ALA CB C 13 19.653 0.300 . 1 . . . . 46 A CB . 17239 1 504 . 1 1 43 43 ALA N N 15 121.494 0.300 . 1 . . . . 46 A N . 17239 1 505 . 1 1 44 44 LEU H H 1 8.853 0.020 . 1 . . . . 47 L HN . 17239 1 506 . 1 1 44 44 LEU HA H 1 3.939 0.020 . 1 . . . . 47 L HA . 17239 1 507 . 1 1 44 44 LEU HB2 H 1 2.083 0.020 . 2 . . . . 47 L HB2 . 17239 1 508 . 1 1 44 44 LEU HB3 H 1 1.161 0.020 . 2 . . . . 47 L HB3 . 17239 1 509 . 1 1 44 44 LEU HD11 H 1 0.829 0.020 . 2 . . . . 47 L QD1 . 17239 1 510 . 1 1 44 44 LEU HD12 H 1 0.829 0.020 . 2 . . . . 47 L QD1 . 17239 1 511 . 1 1 44 44 LEU HD13 H 1 0.829 0.020 . 2 . . . . 47 L QD1 . 17239 1 512 . 1 1 44 44 LEU HD21 H 1 0.117 0.020 . 2 . . . . 47 L QD2 . 17239 1 513 . 1 1 44 44 LEU HD22 H 1 0.117 0.020 . 2 . . . . 47 L QD2 . 17239 1 514 . 1 1 44 44 LEU HD23 H 1 0.117 0.020 . 2 . . . . 47 L QD2 . 17239 1 515 . 1 1 44 44 LEU HG H 1 1.834 0.020 . 1 . . . . 47 L HG . 17239 1 516 . 1 1 44 44 LEU CA C 13 57.733 0.300 . 1 . . . . 47 L CA . 17239 1 517 . 1 1 44 44 LEU CB C 13 43.441 0.300 . 1 . . . . 47 L CB . 17239 1 518 . 1 1 44 44 LEU CD1 C 13 28.776 0.300 . 2 . . . . 47 L CD1 . 17239 1 519 . 1 1 44 44 LEU CD2 C 13 24.886 0.300 . 2 . . . . 47 L CD2 . 17239 1 520 . 1 1 44 44 LEU CG C 13 27.115 0.300 . 1 . . . . 47 L CG . 17239 1 521 . 1 1 44 44 LEU N N 15 118.364 0.300 . 1 . . . . 47 L N . 17239 1 522 . 1 1 45 45 ASN H H 1 7.798 0.020 . 1 . . . . 48 N HN . 17239 1 523 . 1 1 45 45 ASN HA H 1 4.238 0.020 . 1 . . . . 48 N HA . 17239 1 524 . 1 1 45 45 ASN HB2 H 1 2.846 0.020 . 2 . . . . 48 N HB2 . 17239 1 525 . 1 1 45 45 ASN HB3 H 1 2.760 0.020 . 2 . . . . 48 N HB3 . 17239 1 526 . 1 1 45 45 ASN HD21 H 1 7.594 0.020 . 2 . . . . 48 N HD21 . 17239 1 527 . 1 1 45 45 ASN HD22 H 1 7.250 0.020 . 2 . . . . 48 N HD22 . 17239 1 528 . 1 1 45 45 ASN CA C 13 57.953 0.300 . 1 . . . . 48 N CA . 17239 1 529 . 1 1 45 45 ASN CB C 13 39.636 0.300 . 1 . . . . 48 N CB . 17239 1 530 . 1 1 45 45 ASN N N 15 116.978 0.300 . 1 . . . . 48 N N . 17239 1 531 . 1 1 45 45 ASN ND2 N 15 115.904 0.300 . 1 . . . . 48 N ND2 . 17239 1 532 . 1 1 46 46 ASP H H 1 7.842 0.020 . 1 . . . . 49 D HN . 17239 1 533 . 1 1 46 46 ASP HA H 1 4.420 0.020 . 1 . . . . 49 D HA . 17239 1 534 . 1 1 46 46 ASP HB2 H 1 3.283 0.020 . 2 . . . . 49 D HB2 . 17239 1 535 . 1 1 46 46 ASP HB3 H 1 3.080 0.020 . 2 . . . . 49 D HB3 . 17239 1 536 . 1 1 46 46 ASP CA C 13 56.923 0.300 . 1 . . . . 49 D CA . 17239 1 537 . 1 1 46 46 ASP CB C 13 41.864 0.300 . 1 . . . . 49 D CB . 17239 1 538 . 1 1 46 46 ASP N N 15 117.903 0.300 . 1 . . . . 49 D N . 17239 1 539 . 1 1 47 47 TYR H H 1 8.162 0.020 . 1 . . . . 50 Y HN . 17239 1 540 . 1 1 47 47 TYR HA H 1 3.351 0.020 . 1 . . . . 50 Y HA . 17239 1 541 . 1 1 47 47 TYR HB2 H 1 2.669 0.020 . 2 . . . . 50 Y HB2 . 17239 1 542 . 1 1 47 47 TYR HB3 H 1 2.231 0.020 . 2 . . . . 50 Y HB3 . 17239 1 543 . 1 1 47 47 TYR HD1 H 1 5.467 0.020 . 3 . . . . 50 Y QD . 17239 1 544 . 1 1 47 47 TYR HD2 H 1 5.467 0.020 . 3 . . . . 50 Y QD . 17239 1 545 . 1 1 47 47 TYR HE1 H 1 6.284 0.020 . 3 . . . . 50 Y QE . 17239 1 546 . 1 1 47 47 TYR HE2 H 1 6.284 0.020 . 3 . . . . 50 Y QE . 17239 1 547 . 1 1 47 47 TYR CA C 13 61.791 0.300 . 1 . . . . 50 Y CA . 17239 1 548 . 1 1 47 47 TYR CB C 13 39.035 0.300 . 1 . . . . 50 Y CB . 17239 1 549 . 1 1 47 47 TYR CD1 C 13 132.756 0.300 . 3 . . . . 50 Y CD1 . 17239 1 550 . 1 1 47 47 TYR CE1 C 13 117.310 0.300 . 3 . . . . 50 Y CE1 . 17239 1 551 . 1 1 47 47 TYR N N 15 117.896 0.300 . 1 . . . . 50 Y N . 17239 1 552 . 1 1 48 48 TYR H H 1 8.337 0.020 . 1 . . . . 51 Y HN . 17239 1 553 . 1 1 48 48 TYR HA H 1 4.149 0.020 . 1 . . . . 51 Y HA . 17239 1 554 . 1 1 48 48 TYR HB2 H 1 3.208 0.020 . 2 . . . . 51 Y HB2 . 17239 1 555 . 1 1 48 48 TYR HB3 H 1 2.473 0.020 . 2 . . . . 51 Y HB3 . 17239 1 556 . 1 1 48 48 TYR HD1 H 1 7.155 0.020 . 3 . . . . 51 Y QD . 17239 1 557 . 1 1 48 48 TYR HD2 H 1 7.155 0.020 . 3 . . . . 51 Y QD . 17239 1 558 . 1 1 48 48 TYR HE1 H 1 6.620 0.020 . 3 . . . . 51 Y QE . 17239 1 559 . 1 1 48 48 TYR HE2 H 1 6.620 0.020 . 3 . . . . 51 Y QE . 17239 1 560 . 1 1 48 48 TYR CA C 13 62.959 0.300 . 1 . . . . 51 Y CA . 17239 1 561 . 1 1 48 48 TYR CB C 13 37.212 0.300 . 1 . . . . 51 Y CB . 17239 1 562 . 1 1 48 48 TYR CD1 C 13 132.709 0.300 . 3 . . . . 51 Y CD1 . 17239 1 563 . 1 1 48 48 TYR CE1 C 13 117.600 0.300 . 3 . . . . 51 Y CE1 . 17239 1 564 . 1 1 48 48 TYR N N 15 114.456 0.300 . 1 . . . . 51 Y N . 17239 1 565 . 1 1 49 49 ASP H H 1 8.064 0.020 . 1 . . . . 52 D HN . 17239 1 566 . 1 1 49 49 ASP HA H 1 4.760 0.020 . 1 . . . . 52 D HA . 17239 1 567 . 1 1 49 49 ASP HB2 H 1 3.081 0.020 . 2 . . . . 52 D HB2 . 17239 1 568 . 1 1 49 49 ASP HB3 H 1 2.770 0.020 . 2 . . . . 52 D HB3 . 17239 1 569 . 1 1 49 49 ASP CA C 13 56.169 0.300 . 1 . . . . 52 D CA . 17239 1 570 . 1 1 49 49 ASP CB C 13 40.762 0.300 . 1 . . . . 52 D CB . 17239 1 571 . 1 1 49 49 ASP N N 15 120.100 0.300 . 1 . . . . 52 D N . 17239 1 572 . 1 1 50 50 LYS H H 1 7.783 0.020 . 1 . . . . 53 K HN . 17239 1 573 . 1 1 50 50 LYS HA H 1 4.329 0.020 . 1 . . . . 53 K HA . 17239 1 574 . 1 1 50 50 LYS HB2 H 1 1.980 0.020 . 2 . . . . 53 K HB2 . 17239 1 575 . 1 1 50 50 LYS HB3 H 1 1.826 0.020 . 2 . . . . 53 K HB3 . 17239 1 576 . 1 1 50 50 LYS HD2 H 1 1.664 0.020 . 2 . . . . 53 K QD . 17239 1 577 . 1 1 50 50 LYS HD3 H 1 1.664 0.020 . 2 . . . . 53 K QD . 17239 1 578 . 1 1 50 50 LYS HE2 H 1 2.977 0.020 . 2 . . . . 53 K QE . 17239 1 579 . 1 1 50 50 LYS HE3 H 1 2.977 0.020 . 2 . . . . 53 K QE . 17239 1 580 . 1 1 50 50 LYS HG2 H 1 1.545 0.020 . 2 . . . . 53 K HG2 . 17239 1 581 . 1 1 50 50 LYS HG3 H 1 1.502 0.020 . 2 . . . . 53 K HG3 . 17239 1 582 . 1 1 50 50 LYS CA C 13 56.855 0.300 . 1 . . . . 53 K CA . 17239 1 583 . 1 1 50 50 LYS CB C 13 33.644 0.300 . 1 . . . . 53 K CB . 17239 1 584 . 1 1 50 50 LYS CD C 13 28.535 0.300 . 1 . . . . 53 K CD . 17239 1 585 . 1 1 50 50 LYS CE C 13 42.447 0.300 . 1 . . . . 53 K CE . 17239 1 586 . 1 1 50 50 LYS CG C 13 24.979 0.300 . 1 . . . . 53 K CG . 17239 1 587 . 1 1 50 50 LYS N N 15 118.112 0.300 . 1 . . . . 53 K N . 17239 1 588 . 1 1 51 51 GLU H H 1 8.326 0.020 . 1 . . . . 54 E HN . 17239 1 589 . 1 1 51 51 GLU HA H 1 4.197 0.020 . 1 . . . . 54 E HA . 17239 1 590 . 1 1 51 51 GLU HB2 H 1 1.773 0.020 . 2 . . . . 54 E HB2 . 17239 1 591 . 1 1 51 51 GLU HB3 H 1 1.516 0.020 . 2 . . . . 54 E HB3 . 17239 1 592 . 1 1 51 51 GLU HG2 H 1 2.060 0.020 . 2 . . . . 54 E HG2 . 17239 1 593 . 1 1 51 51 GLU HG3 H 1 1.862 0.020 . 2 . . . . 54 E HG3 . 17239 1 594 . 1 1 51 51 GLU CA C 13 56.478 0.300 . 1 . . . . 54 E CA . 17239 1 595 . 1 1 51 51 GLU CB C 13 28.757 0.300 . 1 . . . . 54 E CB . 17239 1 596 . 1 1 51 51 GLU CG C 13 35.381 0.300 . 1 . . . . 54 E CG . 17239 1 597 . 1 1 51 51 GLU N N 15 120.406 0.300 . 1 . . . . 54 E N . 17239 1 598 . 1 1 52 52 ILE H H 1 7.980 0.020 . 1 . . . . 55 I HN . 17239 1 599 . 1 1 52 52 ILE HA H 1 4.169 0.020 . 1 . . . . 55 I HA . 17239 1 600 . 1 1 52 52 ILE HB H 1 1.954 0.020 . 1 . . . . 55 I HB . 17239 1 601 . 1 1 52 52 ILE HD11 H 1 0.877 0.020 . 1 . . . . 55 I QD1 . 17239 1 602 . 1 1 52 52 ILE HD12 H 1 0.877 0.020 . 1 . . . . 55 I QD1 . 17239 1 603 . 1 1 52 52 ILE HD13 H 1 0.877 0.020 . 1 . . . . 55 I QD1 . 17239 1 604 . 1 1 52 52 ILE HG12 H 1 1.475 0.020 . 1 . . . . 55 I HG12 . 17239 1 605 . 1 1 52 52 ILE HG13 H 1 1.213 0.020 . 1 . . . . 55 I HG13 . 17239 1 606 . 1 1 52 52 ILE HG21 H 1 0.941 0.020 . 1 . . . . 55 I QG2 . 17239 1 607 . 1 1 52 52 ILE HG22 H 1 0.941 0.020 . 1 . . . . 55 I QG2 . 17239 1 608 . 1 1 52 52 ILE HG23 H 1 0.941 0.020 . 1 . . . . 55 I QG2 . 17239 1 609 . 1 1 52 52 ILE CA C 13 61.410 0.300 . 1 . . . . 55 I CA . 17239 1 610 . 1 1 52 52 ILE CB C 13 38.611 0.300 . 1 . . . . 55 I CB . 17239 1 611 . 1 1 52 52 ILE CD1 C 13 13.038 0.300 . 1 . . . . 55 I CD1 . 17239 1 612 . 1 1 52 52 ILE CG1 C 13 27.391 0.300 . 1 . . . . 55 I CG1 . 17239 1 613 . 1 1 52 52 ILE CG2 C 13 17.622 0.300 . 1 . . . . 55 I CG2 . 17239 1 614 . 1 1 52 52 ILE N N 15 120.527 0.300 . 1 . . . . 55 I N . 17239 1 615 . 1 1 53 53 GLY H H 1 8.480 0.020 . 1 . . . . 56 G HN . 17239 1 616 . 1 1 53 53 GLY HA2 H 1 4.004 0.020 . 2 . . . . 56 G QA . 17239 1 617 . 1 1 53 53 GLY HA3 H 1 4.004 0.020 . 2 . . . . 56 G QA . 17239 1 618 . 1 1 53 53 GLY CA C 13 45.390 0.300 . 1 . . . . 56 G CA . 17239 1 619 . 1 1 53 53 GLY N N 15 111.645 0.300 . 1 . . . . 56 G N . 17239 1 620 . 1 1 54 54 THR H H 1 8.019 0.020 . 1 . . . . 57 T HN . 17239 1 621 . 1 1 54 54 THR HA H 1 4.342 0.020 . 1 . . . . 57 T HA . 17239 1 622 . 1 1 54 54 THR HB H 1 4.174 0.020 . 1 . . . . 57 T HB . 17239 1 623 . 1 1 54 54 THR HG21 H 1 1.131 0.020 . 1 . . . . 57 T QG2 . 17239 1 624 . 1 1 54 54 THR HG22 H 1 1.131 0.020 . 1 . . . . 57 T QG2 . 17239 1 625 . 1 1 54 54 THR HG23 H 1 1.131 0.020 . 1 . . . . 57 T QG2 . 17239 1 626 . 1 1 54 54 THR CA C 13 61.748 0.300 . 1 . . . . 57 T CA . 17239 1 627 . 1 1 54 54 THR CB C 13 69.991 0.300 . 1 . . . . 57 T CB . 17239 1 628 . 1 1 54 54 THR CG2 C 13 21.609 0.300 . 1 . . . . 57 T CG2 . 17239 1 629 . 1 1 54 54 THR N N 15 113.047 0.300 . 1 . . . . 57 T N . 17239 1 630 . 1 1 55 55 PHE H H 1 8.447 0.020 . 1 . . . . 58 F HN . 17239 1 631 . 1 1 55 55 PHE HA H 1 4.747 0.020 . 1 . . . . 58 F HA . 17239 1 632 . 1 1 55 55 PHE HB2 H 1 3.196 0.020 . 2 . . . . 58 F HB2 . 17239 1 633 . 1 1 55 55 PHE HB3 H 1 3.072 0.020 . 2 . . . . 58 F HB3 . 17239 1 634 . 1 1 55 55 PHE HD1 H 1 7.287 0.020 . 3 . . . . 58 F QD . 17239 1 635 . 1 1 55 55 PHE HD2 H 1 7.287 0.020 . 3 . . . . 58 F QD . 17239 1 636 . 1 1 55 55 PHE HE1 H 1 7.329 0.020 . 3 . . . . 58 F QE . 17239 1 637 . 1 1 55 55 PHE HE2 H 1 7.329 0.020 . 3 . . . . 58 F QE . 17239 1 638 . 1 1 55 55 PHE HZ H 1 7.243 0.020 . 1 . . . . 58 F HZ . 17239 1 639 . 1 1 55 55 PHE CA C 13 57.851 0.300 . 1 . . . . 58 F CA . 17239 1 640 . 1 1 55 55 PHE CB C 13 39.696 0.300 . 1 . . . . 58 F CB . 17239 1 641 . 1 1 55 55 PHE CD1 C 13 131.579 0.300 . 3 . . . . 58 F CD1 . 17239 1 642 . 1 1 55 55 PHE CE1 C 13 131.637 0.300 . 3 . . . . 58 F CE1 . 17239 1 643 . 1 1 55 55 PHE CZ C 13 129.752 0.300 . 1 . . . . 58 F CZ . 17239 1 644 . 1 1 55 55 PHE N N 15 122.414 0.300 . 1 . . . . 58 F N . 17239 1 645 . 1 1 56 56 THR H H 1 8.172 0.020 . 1 . . . . 59 T HN . 17239 1 646 . 1 1 56 56 THR HA H 1 4.357 0.020 . 1 . . . . 59 T HA . 17239 1 647 . 1 1 56 56 THR HB H 1 4.211 0.020 . 1 . . . . 59 T HB . 17239 1 648 . 1 1 56 56 THR HG21 H 1 1.180 0.020 . 1 . . . . 59 T QG2 . 17239 1 649 . 1 1 56 56 THR HG22 H 1 1.180 0.020 . 1 . . . . 59 T QG2 . 17239 1 650 . 1 1 56 56 THR HG23 H 1 1.180 0.020 . 1 . . . . 59 T QG2 . 17239 1 651 . 1 1 56 56 THR CA C 13 61.536 0.300 . 1 . . . . 59 T CA . 17239 1 652 . 1 1 56 56 THR CB C 13 69.937 0.300 . 1 . . . . 59 T CB . 17239 1 653 . 1 1 56 56 THR CG2 C 13 21.439 0.300 . 1 . . . . 59 T CG2 . 17239 1 654 . 1 1 56 56 THR N N 15 115.561 0.300 . 1 . . . . 59 T N . 17239 1 655 . 1 1 57 57 ASP H H 1 8.341 0.020 . 1 . . . . 60 D HN . 17239 1 656 . 1 1 57 57 ASP HA H 1 4.622 0.020 . 1 . . . . 60 D HA . 17239 1 657 . 1 1 57 57 ASP HB2 H 1 2.724 0.020 . 2 . . . . 60 D HB2 . 17239 1 658 . 1 1 57 57 ASP HB3 H 1 2.615 0.020 . 2 . . . . 60 D HB3 . 17239 1 659 . 1 1 57 57 ASP CA C 13 54.345 0.300 . 1 . . . . 60 D CA . 17239 1 660 . 1 1 57 57 ASP CB C 13 41.264 0.300 . 1 . . . . 60 D CB . 17239 1 661 . 1 1 57 57 ASP N N 15 122.410 0.300 . 1 . . . . 60 D N . 17239 1 662 . 1 1 58 58 GLU H H 1 8.365 0.020 . 1 . . . . 61 E HN . 17239 1 663 . 1 1 58 58 GLU HA H 1 4.329 0.020 . 1 . . . . 61 E HA . 17239 1 664 . 1 1 58 58 GLU HB2 H 1 2.075 0.020 . 2 . . . . 61 E HB2 . 17239 1 665 . 1 1 58 58 GLU HB3 H 1 1.929 0.020 . 2 . . . . 61 E HB3 . 17239 1 666 . 1 1 58 58 GLU HG2 H 1 2.308 0.020 . 2 . . . . 61 E HG2 . 17239 1 667 . 1 1 58 58 GLU HG3 H 1 2.250 0.020 . 2 . . . . 61 E HG3 . 17239 1 668 . 1 1 58 58 GLU CA C 13 56.590 0.300 . 1 . . . . 61 E CA . 17239 1 669 . 1 1 58 58 GLU CB C 13 30.465 0.300 . 1 . . . . 61 E CB . 17239 1 670 . 1 1 58 58 GLU CG C 13 36.213 0.300 . 1 . . . . 61 E CG . 17239 1 671 . 1 1 58 58 GLU N N 15 121.191 0.300 . 1 . . . . 61 E N . 17239 1 672 . 1 1 59 59 VAL H H 1 7.851 0.020 . 1 . . . . 62 V HN . 17239 1 673 . 1 1 59 59 VAL HA H 1 4.026 0.020 . 1 . . . . 62 V HA . 17239 1 674 . 1 1 59 59 VAL HB H 1 2.079 0.020 . 1 . . . . 62 V HB . 17239 1 675 . 1 1 59 59 VAL HG11 H 1 0.900 0.020 . 2 . . . . 62 V QG1 . 17239 1 676 . 1 1 59 59 VAL HG12 H 1 0.900 0.020 . 2 . . . . 62 V QG1 . 17239 1 677 . 1 1 59 59 VAL HG13 H 1 0.900 0.020 . 2 . . . . 62 V QG1 . 17239 1 678 . 1 1 59 59 VAL HG21 H 1 0.884 0.020 . 2 . . . . 62 V QG2 . 17239 1 679 . 1 1 59 59 VAL HG22 H 1 0.884 0.020 . 2 . . . . 62 V QG2 . 17239 1 680 . 1 1 59 59 VAL HG23 H 1 0.884 0.020 . 2 . . . . 62 V QG2 . 17239 1 681 . 1 1 59 59 VAL CA C 13 63.708 0.300 . 1 . . . . 62 V CA . 17239 1 682 . 1 1 59 59 VAL CB C 13 33.202 0.300 . 1 . . . . 62 V CB . 17239 1 683 . 1 1 59 59 VAL CG1 C 13 21.665 0.300 . 2 . . . . 62 V CG1 . 17239 1 684 . 1 1 59 59 VAL CG2 C 13 20.227 0.300 . 2 . . . . 62 V CG2 . 17239 1 685 . 1 1 59 59 VAL N N 15 124.888 0.300 . 1 . . . . 62 V N . 17239 1 stop_ save_