data_16885 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 16885 _Entry.Title ; Solution Structure of UBM1 of murine Polymerase iota in Complex with Ubiquitin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2010-04-20 _Entry.Accession_date 2010-04-20 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.9.13 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Daniel Burschowsky . . . 16885 2 Fabian Rudolf . . . 16885 3 Gwenael Rabut . . . 16885 4 Torsten Herrmann . . . 16885 5 Matthias Peter . . . 16885 6 Gerhard Wider . . . 16885 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 . 'not applicable' 'not applicable' . 16885 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'polymerase iota' . 16885 TLS . 16885 ubiquitin . 16885 'ubiquitin-binding motif' . 16885 UBM . 16885 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 16885 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 423 16885 '15N chemical shifts' 131 16885 '1H chemical shifts' 909 16885 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 2011-01-18 2010-04-20 update BMRB 'update entry citation' 16885 1 . . 2010-10-14 2010-04-20 original author 'original release' 16885 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 16880 'Solution Structure of UBM2' 16885 PDB 2KWU . 16885 PDB 2KWV 'BMRB Entry Tracking System' 16885 stop_ save_ ############### # Citations # ############### save_UBM_Paper _Citation.Sf_category citations _Citation.Sf_framecode UBM_Paper _Citation.Entry_ID 16885 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 20929865 _Citation.Full_citation . _Citation.Title 'Structural Analysis of the Conserved Ubiquitin-binding Motifs (UBMs) of the Translesion Polymerase iota in Complex with Ubiquitin.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 286 _Citation.Journal_issue 2 _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 1364 _Citation.Page_last 1373 _Citation.Year 2011 _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 . . . 16885 1 2 Fabian Rudolf . . . 16885 1 3 Gwenael Rabut . . . 16885 1 4 Torsten Herrmann . . . 16885 1 5 Peter Matthias . . . 16885 1 6 Gerhard Wider . . . 16885 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID TLS 16885 1 UBM 16885 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 16885 _Assembly.ID 1 _Assembly.Name 'UBM1-Ubiquitin 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 . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 UBM1 1 $DNA_polymerase_iota_UBM1 A . yes native no no . . . 16885 1 2 Ubiquitin 2 $Ubiquitin B . yes native no no . . . 16885 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_DNA_polymerase_iota_UBM1 _Entity.Sf_category entity _Entity.Sf_framecode DNA_polymerase_iota_UBM1 _Entity.Entry_ID 16885 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name DNA_polymerase_iota_UBM1 _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 ; GSDTSDLPLQALPEGVDQEV FKQLPADIQEEILSGKSREN LKGKGSLS ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details 'Residues 485-486 represent non-native cloning artifacts. Residues 487-490 and 527-532 represent flexible flanking regions that are not shown in the Structure.' _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 48 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment 'DNA polymerase iota C-terminal ubiquitin-binding motif' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 5125.6 _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 PDB 2KWV . "Solution Structure Of Ubm1 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 100.00 48 100.00 100.00 1.67e-23 . . . . 16885 1 2 no DBJ BAC25154 . "unnamed protein product [Mus musculus]" . . . . . 93.75 254 100.00 100.00 3.27e-20 . . . . 16885 1 3 no DBJ BAE26322 . "unnamed protein product [Mus musculus]" . . . . . 95.83 717 97.83 97.83 4.93e-19 . . . . 16885 1 4 no DBJ BAE32662 . "unnamed protein product [Mus musculus]" . . . . . 95.83 549 97.83 97.83 1.36e-19 . . . . 16885 1 5 no GB AAD50424 . "DNA polymerase iota [Mus musculus]" . . . . . 95.83 717 100.00 100.00 4.46e-20 . . . . 16885 1 6 no GB AAH82278 . "Poli protein [Mus musculus]" . . . . . 95.83 674 100.00 100.00 4.64e-20 . . . . 16885 1 7 no GB AAS75834 . "DNA polymerase iota [Mus musculus]" . . . . . 95.83 717 97.83 97.83 2.03e-19 . . . . 16885 1 8 no GB AAS75835 . "DNA polymerase iota [Mus musculus]" . . . . . 95.83 717 97.83 97.83 4.98e-19 . . . . 16885 1 9 no GB AEQ34091 . "DNA polymerase iota [Mus musculus]" . . . . . 95.83 737 97.83 97.83 2.06e-19 . . . . 16885 1 10 no REF NP_001129562 . "DNA polymerase iota isoform 1 [Mus musculus]" . . . . . 95.83 674 100.00 100.00 4.64e-20 . . . . 16885 1 11 no REF NP_001276444 . "DNA polymerase iota isoform 3 [Mus musculus]" . . . . . 95.83 549 100.00 100.00 2.98e-20 . . . . 16885 1 12 no REF NP_001276445 . "DNA polymerase iota isoform 4 [Mus musculus]" . . . . . 95.83 651 100.00 100.00 3.79e-20 . . . . 16885 1 13 no REF NP_036102 . "DNA polymerase iota isoform 2 [Mus musculus]" . . . . . 95.83 737 100.00 100.00 4.76e-20 . . . . 16885 1 14 no REF XP_006526008 . "PREDICTED: DNA polymerase iota isoform X3 [Mus musculus]" . . . . . 95.83 736 100.00 100.00 4.75e-20 . . . . 16885 1 15 no SP Q6R3M4 . "RecName: Full=DNA polymerase iota; AltName: Full=Rad30 homolog B" . . . . . 95.83 717 97.83 97.83 2.03e-19 . . . . 16885 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 1 485 GLY . 16885 1 2 486 SER . 16885 1 3 487 ASP . 16885 1 4 488 THR . 16885 1 5 489 SER . 16885 1 6 490 ASP . 16885 1 7 491 LEU . 16885 1 8 492 PRO . 16885 1 9 493 LEU . 16885 1 10 494 GLN . 16885 1 11 495 ALA . 16885 1 12 496 LEU . 16885 1 13 497 PRO . 16885 1 14 498 GLU . 16885 1 15 499 GLY . 16885 1 16 500 VAL . 16885 1 17 501 ASP . 16885 1 18 502 GLN . 16885 1 19 503 GLU . 16885 1 20 504 VAL . 16885 1 21 505 PHE . 16885 1 22 506 LYS . 16885 1 23 507 GLN . 16885 1 24 508 LEU . 16885 1 25 509 PRO . 16885 1 26 510 ALA . 16885 1 27 511 ASP . 16885 1 28 512 ILE . 16885 1 29 513 GLN . 16885 1 30 514 GLU . 16885 1 31 515 GLU . 16885 1 32 516 ILE . 16885 1 33 517 LEU . 16885 1 34 518 SER . 16885 1 35 519 GLY . 16885 1 36 520 LYS . 16885 1 37 521 SER . 16885 1 38 522 ARG . 16885 1 39 523 GLU . 16885 1 40 524 ASN . 16885 1 41 525 LEU . 16885 1 42 526 LYS . 16885 1 43 527 GLY . 16885 1 44 528 LYS . 16885 1 45 529 GLY . 16885 1 46 530 SER . 16885 1 47 531 LEU . 16885 1 48 532 SER . 16885 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 16885 1 . SER 2 2 16885 1 . ASP 3 3 16885 1 . THR 4 4 16885 1 . SER 5 5 16885 1 . ASP 6 6 16885 1 . LEU 7 7 16885 1 . PRO 8 8 16885 1 . LEU 9 9 16885 1 . GLN 10 10 16885 1 . ALA 11 11 16885 1 . LEU 12 12 16885 1 . PRO 13 13 16885 1 . GLU 14 14 16885 1 . GLY 15 15 16885 1 . VAL 16 16 16885 1 . ASP 17 17 16885 1 . GLN 18 18 16885 1 . GLU 19 19 16885 1 . VAL 20 20 16885 1 . PHE 21 21 16885 1 . LYS 22 22 16885 1 . GLN 23 23 16885 1 . LEU 24 24 16885 1 . PRO 25 25 16885 1 . ALA 26 26 16885 1 . ASP 27 27 16885 1 . ILE 28 28 16885 1 . GLN 29 29 16885 1 . GLU 30 30 16885 1 . GLU 31 31 16885 1 . ILE 32 32 16885 1 . LEU 33 33 16885 1 . SER 34 34 16885 1 . GLY 35 35 16885 1 . LYS 36 36 16885 1 . SER 37 37 16885 1 . ARG 38 38 16885 1 . GLU 39 39 16885 1 . ASN 40 40 16885 1 . LEU 41 41 16885 1 . LYS 42 42 16885 1 . GLY 43 43 16885 1 . LYS 44 44 16885 1 . GLY 45 45 16885 1 . SER 46 46 16885 1 . LEU 47 47 16885 1 . SER 48 48 16885 1 stop_ save_ save_Ubiquitin _Entity.Sf_category entity _Entity.Sf_framecode Ubiquitin _Entity.Entry_ID 16885 _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 man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 8576.914 _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 . . . . 16885 2 2 no BMRB 11547 . ubiquitin . . . . . 100.00 76 98.68 98.68 2.41e-45 . . . . 16885 2 3 no BMRB 15047 . denatured_ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 4 no BMRB 15410 . Ubi . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 5 no BMRB 15689 . UBB . . . . . 98.68 103 98.67 100.00 4.23e-44 . . . . 16885 2 6 no BMRB 15866 . ubiquitin . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 16885 2 7 no BMRB 15907 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 8 no BMRB 16228 . ubiquitin . . . . . 100.00 76 97.37 98.68 1.18e-44 . . . . 16885 2 9 no BMRB 16582 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 10 no BMRB 16626 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 11 no BMRB 16763 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 12 no BMRB 16880 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 13 no BMRB 16895 . UBB+1 . . . . . 98.68 103 98.67 100.00 4.23e-44 . . . . 16885 2 14 no BMRB 17059 . ubiquitin . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 16885 2 15 no BMRB 17181 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 16 no BMRB 17239 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 17 no BMRB 17333 . UB . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 18 no BMRB 17439 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 19 no BMRB 17769 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 20 no BMRB 17919 . entity . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 21 no BMRB 18582 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 22 no BMRB 18583 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 23 no BMRB 18584 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 24 no BMRB 18610 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 25 no BMRB 18611 . Ubiquitin_A_state . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 26 no BMRB 18737 . UBIQUITIN . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 27 no BMRB 19394 . ubiquitin . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 16885 2 28 no BMRB 19399 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 29 no BMRB 19406 . entity . . . . . 100.00 152 100.00 100.00 4.37e-45 . . . . 16885 2 30 no BMRB 19412 . entity . . . . . 100.00 152 100.00 100.00 4.37e-45 . . . . 16885 2 31 no BMRB 19447 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 32 no BMRB 25070 . Ubiquitin . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 16885 2 33 no BMRB 25230 . Ubiquitin . . . . . 100.00 78 100.00 100.00 3.66e-46 . . . . 16885 2 34 no BMRB 4245 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 35 no BMRB 4375 . Ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 36 no BMRB 4983 . Ubiquitin . . . . . 98.68 76 97.33 100.00 3.66e-44 . . . . 16885 2 37 no BMRB 5101 . uq1_51 . . . . . 67.11 53 100.00 100.00 2.13e-26 . . . . 16885 2 38 no BMRB 5387 . ubq . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 39 no BMRB 6457 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 40 no BMRB 6466 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 41 no BMRB 6470 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 42 no BMRB 6488 . Ub . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 43 no BMRB 68 . ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 44 no BMRB 7111 . human_ubiquitin . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 47 no PDB 1D3Z . "Ubiquitin Nmr Structure" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 48 no PDB 1F9J . "Structure Of A New Crystal Form Of Tetraubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 49 no PDB 1FXT . "Structure Of A Conjugating Enzyme-Ubiquitin Thiolester Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 50 no PDB 1G6J . "Structure Of Recombinant Human Ubiquitin In Aot Reverse Micelles" . . . . . 98.68 76 100.00 100.00 5.16e-45 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 53 no PDB 1OGW . "Synthetic Ubiquitin With Fluoro-Leu At 50 And 67" . . . . . 100.00 76 97.37 97.37 1.80e-44 . . . . 16885 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 . . . . 16885 2 55 no PDB 1Q5W . "Ubiquitin Recognition By Npl4 Zinc-Fingers" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 56 no PDB 1S1Q . "Tsg101(Uev) Domain In Complex With Ubiquitin" . . . . . 98.68 76 100.00 100.00 5.16e-45 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 59 no PDB 1UBQ . "Structure Of Ubiquitin Refined At 1.8 Angstroms Resolution" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 60 no PDB 1UZX . "A Complex Of The Vps23 Uev With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 66 no PDB 1XD3 . "Crystal Structure Of Uchl3-Ubvme Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 16885 2 67 no PDB 1XQQ . "Simultaneous Determination Of Protein Structure And Dynamics" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 68 no PDB 1YD8 . "Complex Of Human Gga3 Gat Domain And Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 69 no PDB 1YIW . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin" . . . . . 100.00 76 98.68 100.00 1.94e-45 . . . . 16885 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 . . . . 16885 2 71 no PDB 1YX5 . "Solution Structure Of S5a Uim-1UBIQUITIN COMPLEX" . . . . . 100.00 98 100.00 100.00 1.57e-46 . . . . 16885 2 72 no PDB 1YX6 . "Solution Structure Of S5a Uim-2UBIQUITIN COMPLEX" . . . . . 100.00 98 100.00 100.00 1.57e-46 . . . . 16885 2 73 no PDB 1ZGU . "Solution Structure Of The Human Mms2-Ubiquitin Complex" . . . . . 100.00 76 98.68 100.00 1.06e-45 . . . . 16885 2 74 no PDB 2AYO . "Structure Of Usp14 Bound To Ubquitin Aldehyde" . . . . . 98.68 76 100.00 100.00 2.99e-45 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 78 no PDB 2D3G . "Double Sided Ubiquitin Binding Of Hrs-Uim" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 87 no PDB 2FUH . "Solution Structure Of The Ubch5cUB NON-Covalent Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 2 89 no PDB 2GMI . Mms2UBC13~UBIQUITIN . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 90 no PDB 2HD5 . "Usp2 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 2 92 no PDB 2IBI . "Covalent Ubiquitin-Usp2 Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 16885 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 . . . . 16885 2 94 no PDB 2JF5 . "Crystal Structure Of Lys63-Linked Di-Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 97 no PDB 2JZZ . "Solid-State Nmr Structure Of Microcrystalline Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 98 no PDB 2K25 . "Automated Nmr Structure Of The Ubb By Fapsy" . . . . . 98.68 103 98.67 100.00 4.23e-44 . . . . 16885 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 . . . . 16885 2 100 no PDB 2K6D . "Cin85 Sh3-C Domain In Complex With Ubiquitin" . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 106 no PDB 2KJH . "Nmr Based Structural Model Of The Ubch8-Ubiquitin Complex" . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 16885 2 107 no PDB 2KLG . "Pere Nmr Structure Of Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 119 no PDB 2LVO . "Structure Of The Gp78cue Domain Bound To Monubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 124 no PDB 2MBH . "Nmr Structure Of Eklf(22-40)/ubiquitin Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 131 no PDB 2MRE . "Nmr Structure Of The Rad18-ubz/ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 16885 2 132 no PDB 2MUR . "Solution Structure Of The Human Faap20 Ubz-ubiquitin Complex" . . . . . 100.00 78 100.00 100.00 3.66e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 140 no PDB 2RR9 . "The Solution Structure Of The K63-Ub2:tuims Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 141 no PDB 2RSU . "Alternative Structure Of Ubiquitin" . . . . . 100.00 76 98.68 98.68 2.41e-45 . . . . 16885 2 142 no PDB 2RU6 . "The Pure Alternative State Of Ubiquitin" . . . . . 100.00 76 98.68 98.68 2.41e-45 . . . . 16885 2 143 no PDB 2W9N . "Crystal Structure Of Linear Di-Ubiquitin" . . . . . 98.68 152 100.00 100.00 3.82e-44 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 148 no PDB 2XBB . "Nedd4 Hect:ub Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 149 no PDB 2XEW . "Crystal Structure Of K11-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 150 no PDB 2XK5 . "Crystal Structure Of K6-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 151 no PDB 2Y5B . "Structure Of Usp21 In Complex With Linear Diubiquitin-Aldehyde" . . . . . 98.68 152 100.00 100.00 2.82e-44 . . . . 16885 2 152 no PDB 2Z59 . "Complex Structures Of Mouse Rpn13 (22-130aa) And Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 153 no PDB 2ZCB . "Crystal Structure Of Ubiquitin P37aP38A" . . . . . 100.00 76 97.37 97.37 2.34e-44 . . . . 16885 2 154 no PDB 2ZCC . "Ubiquitin Crystallized Under High Pressure" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 159 no PDB 3A33 . "Ubch5b~ubiquitin Conjugate" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 163 no PDB 3ALB . "Cyclic Lys48-Linked Tetraubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 2 165 no PDB 3AXC . "Crystal Structure Of Linear Diubiquitin" . . . . . 100.00 154 100.00 100.00 4.07e-45 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 172 no PDB 3EEC . "X-Ray Structure Of Human Ubiquitin Cd(Ii) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 173 no PDB 3EFU . "X-Ray Structure Of Human Ubiquitin-Hg(Ii) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 174 no PDB 3EHV . "X-Ray Structure Of Human Ubiquitin Zn(Ii) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 175 no PDB 3H1U . "Structure Of Ubiquitin In Complex With Cd Ions" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 176 no PDB 3H7P . "Crystal Structure Of K63-Linked Di-Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 179 no PDB 3I3T . "Crystal Structure Of Covalent Ubiquitin-usp21 Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 16885 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 . . . . 16885 2 181 no PDB 3IHP . "Covalent Ubiquitin-Usp5 Complex" . . . . . 98.68 75 100.00 100.00 2.91e-45 . . . . 16885 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 . . . . 16885 2 183 no PDB 3JVZ . E2~ubiquitin-Hect . . . . . 100.00 81 100.00 100.00 5.23e-46 . . . . 16885 2 184 no PDB 3JW0 . E2~ubiquitin-Hect . . . . . 100.00 81 100.00 100.00 5.23e-46 . . . . 16885 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 . . . . 16885 2 186 no PDB 3K9P . "The Crystal Structure Of E2-25k And Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 190 no PDB 3M3J . "A New Crystal Form Of Lys48-Linked Diubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 193 no PDB 3N30 . "Crystal Structure Of Cubic Zn3-Hub (Human Ubiquitin) Adduct" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 196 no PDB 3NOB . "Structure Of K11-linked Di-ubiquitin" . . . . . 100.00 78 100.00 100.00 3.66e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 200 no PDB 3OJ3 . "Crystal Structure Of The A20 Znf4 And Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 4.53e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 203 no PDB 3PHD . "Crystal Structure Of Human Hdac6 In Complex With Ubiquitin" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 210 no PDB 3RUL . "New Strategy To Analyze Structures Of Glycopeptide-Target Complexes" . . . . . 98.68 79 100.00 100.00 2.70e-45 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 214 no PDB 3UGB . "Ubch5c~ubiquitin Conjugate" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 221 no PDB 3ZLZ . "Lys6-linked Tri-ubiquitin" . . . . . 100.00 76 98.68 100.00 1.06e-45 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 230 no PDB 4AP4 . "Rnf4 - Ubch5a - Ubiquitin Heterotrimeric Complex" . . . . . 100.00 80 100.00 100.00 4.66e-46 . . . . 16885 2 231 no PDB 4AUQ . "Structure Of Birc7-Ubch5b-Ub Complex." . . . . . 100.00 81 100.00 100.00 5.23e-46 . . . . 16885 2 232 no PDB 4BBN . "Nedd4 Hect-ub:ub Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 238 no PDB 4DDG . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 239 no PDB 4DDI . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 2 241 no PDB 4DHZ . "The Structure Of HCEOTUB1-Ubiquitin Aldehyde-Ubc13~ub" . . . . . 98.68 76 100.00 100.00 2.71e-45 . . . . 16885 2 242 no PDB 4FJV . "Crystal Structure Of Human Otubain2 And Ubiquitin Complex" . . . . . 100.00 86 100.00 100.00 6.71e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 247 no PDB 4JIO . "Bro1 V Domain And Ubiquitin" . . . . . 100.00 76 98.68 98.68 3.30e-45 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 253 no PDB 4KSK . "Gumby/fam105b In Complex With Ubiquitin" . . . . . 100.00 80 100.00 100.00 4.66e-46 . . . . 16885 2 254 no PDB 4KSL . "Gumby/fam105b In Complex With Linear Di-ubiquitin" . . . . . 100.00 156 100.00 100.00 4.31e-45 . . . . 16885 2 255 no PDB 4KZX . "Rabbit 40s Ribosomal Subunit In Complex With Eif1." . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 259 no PDB 4LDT . "The Structure Of H/ceotub1-ubiquitin Aldehyde-ubch5b~ub" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 260 no PDB 4LJO . "Structure Of An Active Ligase (hoip)/ubiquitin Transfer Complex" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 263 no PDB 4MDK . "Cdc34-ubiquitin-cc0651 Complex" . . . . . 100.00 80 100.00 100.00 4.66e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 267 no PDB 4NQK . "Structure Of An Ubiquitin Complex" . . . . . 100.00 79 100.00 100.00 8.16e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 270 no PDB 4PIG . "Crystal Structure Of The Ubiquitin K11s Mutant" . . . . . 100.00 76 98.68 98.68 1.92e-45 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 288 no PDB 4WZP . "Ser65 Phosphorylated Ubiquitin, Major Conformation" . . . . . 100.00 76 98.68 98.68 3.16e-45 . . . . 16885 2 289 no DBJ BAA03983 . "polyubiquitin [Rattus norvegicus]" . . . . . 100.00 305 100.00 100.00 2.21e-43 . . . . 16885 2 290 no DBJ BAA09860 . "polyubiquitin [Homo sapiens]" . . . . . 100.00 611 98.68 98.68 1.04e-40 . . . . 16885 2 291 no DBJ BAA11842 . "ubiquitin [Cavia porcellus]" . . . . . 100.00 311 100.00 100.00 2.40e-43 . . . . 16885 2 292 no DBJ BAA11843 . "ubiquitin extention protein [Cavia porcellus]" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 16885 2 293 no DBJ BAA23486 . "polyubiquitin [Homo sapiens]" . . . . . 100.00 609 98.68 98.68 5.60e-41 . . . . 16885 2 294 no EMBL CAA25706 . "unnamed protein product [Saccharomyces cerevisiae]" . . . . . 50.00 191 100.00 100.00 2.98e-16 . . . . 16885 2 295 no EMBL CAA26488 . "unnamed protein product [Gallus gallus]" . . . . . 100.00 157 98.68 98.68 2.66e-44 . . . . 16885 2 296 no EMBL CAA28495 . "ubiquitin [Homo sapiens]" . . . . . 100.00 229 100.00 100.00 3.53e-44 . . . . 16885 2 297 no EMBL CAA30183 . "unnamed protein product [Dictyostelium discoideum]" . . . . . 100.00 128 97.37 97.37 5.38e-44 . . . . 16885 2 298 no EMBL CAA30815 . "unnamed protein product [Cricetulus sp.]" . . . . . 93.42 223 100.00 100.00 3.70e-40 . . . . 16885 2 299 no GB AAA02769 . "polyprotein [Bovine viral diarrhea virus 1-Osloss]" . . . . . 98.68 3975 97.33 100.00 1.83e-39 . . . . 16885 2 300 no GB AAA28154 . "polyubiquitin [Caenorhabditis elegans]" . . . . . 100.00 838 97.37 98.68 7.19e-40 . . . . 16885 2 301 no GB AAA28997 . "ubiquitin [Drosophila melanogaster]" . . . . . 100.00 231 100.00 100.00 3.30e-44 . . . . 16885 2 302 no GB AAA28998 . "ubiquitin-hybrid protein precursor [Drosophila melanogaster]" . . . . . 100.00 156 100.00 100.00 9.66e-46 . . . . 16885 2 303 no GB AAA28999 . "ubiquitin, partial [Drosophila melanogaster]" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 304 no PIR I50437 . "polyubiquitin 4 - chicken [Gallus gallus]" . . . . . 100.00 305 100.00 100.00 2.21e-43 . . . . 16885 2 305 no PIR I51568 . "polyubiquitin - African clawed frog (fragment)" . . . . . 100.00 167 100.00 100.00 6.83e-45 . . . . 16885 2 306 no PIR I65237 . "ubiquitin / ribosomal protein L40, cytosolic [validated] - rat" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 16885 2 307 no PIR JN0790 . "ubiquitin/ribosomal protein CEP52 fusion protein - Leishmania major" . . . . . 100.00 128 97.37 98.68 2.33e-45 . . . . 16885 2 308 no PIR S13928 . "ubiquitin precursor - chicken [Gallus gallus]" . . . . . 100.00 229 100.00 100.00 3.64e-44 . . . . 16885 2 309 no PRF 0412265A . ubiquitin . . . . . 98.68 75 98.67 98.67 1.22e-44 . . . . 16885 2 310 no PRF 1101405A . "ubiquitin precursor" . . . . . 50.00 191 100.00 100.00 2.95e-16 . . . . 16885 2 311 no PRF 1212243A . "ubiquitin S1" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 2 312 no PRF 1212243B . "ubiquitin S5" . . . . . 92.11 77 98.57 98.57 7.61e-41 . . . . 16885 2 313 no PRF 1212243C . "ubiquitin S3" . . . . . 100.00 76 100.00 100.00 4.45e-46 . . . . 16885 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 . . . . 16885 2 315 no REF NP_001006688 . "ubiquitin C [Xenopus (Silurana) tropicalis]" . . . . . 100.00 609 100.00 100.00 9.87e-42 . . . . 16885 2 316 no REF NP_001009117 . "polyubiquitin-B [Pan troglodytes]" . . . . . 100.00 229 100.00 100.00 3.53e-44 . . . . 16885 2 317 no REF NP_001009202 . "polyubiquitin-B [Ovis aries]" . . . . . 100.00 305 98.68 100.00 3.89e-43 . . . . 16885 2 318 no REF NP_001009286 . "ubiquitin-60S ribosomal protein L40 [Ovis aries]" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 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 . . . . 16885 2 324 no TPD FAA00319 . "TPA: polyubiquitin [Cryptococcus neoformans var. neoformans B-3501A]" . . . . . 100.00 456 97.37 98.68 7.53e-41 . . . . 16885 2 325 no TPG DAA18802 . "TPA: polyubiquitin [Bos taurus]" . . . . . 100.00 305 100.00 100.00 2.33e-43 . . . . 16885 2 326 no TPG DAA20663 . "TPA: ubiquitin C [Bos taurus]" . . . . . 98.68 314 98.67 100.00 8.85e-42 . . . . 16885 2 327 no TPG DAA20672 . "TPA: ubiquitin B-like [Bos taurus]" . . . . . 100.00 77 98.68 98.68 3.32e-45 . . . . 16885 2 328 no TPG DAA24675 . "TPA: 40S ribosomal protein S27a [Bos taurus]" . . . . . 100.00 156 100.00 100.00 5.21e-46 . . . . 16885 2 329 no TPG DAA28295 . "TPA: ubiquitin and ribosomal protein L40 [Bos taurus]" . . . . . 100.00 128 100.00 100.00 3.09e-46 . . . . 16885 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 . 16885 2 2 . GLN . 16885 2 3 . ILE . 16885 2 4 . PHE . 16885 2 5 . VAL . 16885 2 6 . LYS . 16885 2 7 . THR . 16885 2 8 . LEU . 16885 2 9 . THR . 16885 2 10 . GLY . 16885 2 11 . LYS . 16885 2 12 . THR . 16885 2 13 . ILE . 16885 2 14 . THR . 16885 2 15 . LEU . 16885 2 16 . GLU . 16885 2 17 . VAL . 16885 2 18 . GLU . 16885 2 19 . PRO . 16885 2 20 . SER . 16885 2 21 . ASP . 16885 2 22 . THR . 16885 2 23 . ILE . 16885 2 24 . GLU . 16885 2 25 . ASN . 16885 2 26 . VAL . 16885 2 27 . LYS . 16885 2 28 . ALA . 16885 2 29 . LYS . 16885 2 30 . ILE . 16885 2 31 . GLN . 16885 2 32 . ASP . 16885 2 33 . LYS . 16885 2 34 . GLU . 16885 2 35 . GLY . 16885 2 36 . ILE . 16885 2 37 . PRO . 16885 2 38 . PRO . 16885 2 39 . ASP . 16885 2 40 . GLN . 16885 2 41 . GLN . 16885 2 42 . ARG . 16885 2 43 . LEU . 16885 2 44 . ILE . 16885 2 45 . PHE . 16885 2 46 . ALA . 16885 2 47 . GLY . 16885 2 48 . LYS . 16885 2 49 . GLN . 16885 2 50 . LEU . 16885 2 51 . GLU . 16885 2 52 . ASP . 16885 2 53 . GLY . 16885 2 54 . ARG . 16885 2 55 . THR . 16885 2 56 . LEU . 16885 2 57 . SER . 16885 2 58 . ASP . 16885 2 59 . TYR . 16885 2 60 . ASN . 16885 2 61 . ILE . 16885 2 62 . GLN . 16885 2 63 . LYS . 16885 2 64 . GLU . 16885 2 65 . SER . 16885 2 66 . THR . 16885 2 67 . LEU . 16885 2 68 . HIS . 16885 2 69 . LEU . 16885 2 70 . VAL . 16885 2 71 . LEU . 16885 2 72 . ARG . 16885 2 73 . LEU . 16885 2 74 . ARG . 16885 2 75 . GLY . 16885 2 76 . GLY . 16885 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 16885 2 . GLN 2 2 16885 2 . ILE 3 3 16885 2 . PHE 4 4 16885 2 . VAL 5 5 16885 2 . LYS 6 6 16885 2 . THR 7 7 16885 2 . LEU 8 8 16885 2 . THR 9 9 16885 2 . GLY 10 10 16885 2 . LYS 11 11 16885 2 . THR 12 12 16885 2 . ILE 13 13 16885 2 . THR 14 14 16885 2 . LEU 15 15 16885 2 . GLU 16 16 16885 2 . VAL 17 17 16885 2 . GLU 18 18 16885 2 . PRO 19 19 16885 2 . SER 20 20 16885 2 . ASP 21 21 16885 2 . THR 22 22 16885 2 . ILE 23 23 16885 2 . GLU 24 24 16885 2 . ASN 25 25 16885 2 . VAL 26 26 16885 2 . LYS 27 27 16885 2 . ALA 28 28 16885 2 . LYS 29 29 16885 2 . ILE 30 30 16885 2 . GLN 31 31 16885 2 . ASP 32 32 16885 2 . LYS 33 33 16885 2 . GLU 34 34 16885 2 . GLY 35 35 16885 2 . ILE 36 36 16885 2 . PRO 37 37 16885 2 . PRO 38 38 16885 2 . ASP 39 39 16885 2 . GLN 40 40 16885 2 . GLN 41 41 16885 2 . ARG 42 42 16885 2 . LEU 43 43 16885 2 . ILE 44 44 16885 2 . PHE 45 45 16885 2 . ALA 46 46 16885 2 . GLY 47 47 16885 2 . LYS 48 48 16885 2 . GLN 49 49 16885 2 . LEU 50 50 16885 2 . GLU 51 51 16885 2 . ASP 52 52 16885 2 . GLY 53 53 16885 2 . ARG 54 54 16885 2 . THR 55 55 16885 2 . LEU 56 56 16885 2 . SER 57 57 16885 2 . ASP 58 58 16885 2 . TYR 59 59 16885 2 . ASN 60 60 16885 2 . ILE 61 61 16885 2 . GLN 62 62 16885 2 . LYS 63 63 16885 2 . GLU 64 64 16885 2 . SER 65 65 16885 2 . THR 66 66 16885 2 . LEU 67 67 16885 2 . HIS 68 68 16885 2 . LEU 69 69 16885 2 . VAL 70 70 16885 2 . LEU 71 71 16885 2 . ARG 72 72 16885 2 . LEU 73 73 16885 2 . ARG 74 74 16885 2 . GLY 75 75 16885 2 . GLY 76 76 16885 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 16885 _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 $DNA_polymerase_iota_UBM1 . 10013 organism . 'Mus musculus' 'House mouse' . . Eukaryota Metazoa Mus musculus . . . . . . . . . . . . . . . . . . . . . 16885 1 2 2 $Ubiquitin . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 16885 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 16885 _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 $DNA_polymerase_iota_UBM1 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21 Star DE3' . . . . . . . . . . . . . . . pGEX-4T-2 . . . . . . 16885 1 2 2 $Ubiquitin . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21 Star DE3' . . . . . . . . . . . . . . . pET-19b . . . . . . 16885 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15NUBM1+ub _Sample.Sf_category sample _Sample.Sf_framecode 15NUBM1+ub _Sample.Entry_ID 16885 _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 'DNA polymerase iota UBM1' '[U-99% 15N]' . . 1 $DNA_polymerase_iota_UBM1 . . . 1 2 mM . . . . 16885 1 2 Ubiquitin 'natural abundance' . . 2 $Ubiquitin . . . 4 8 mM . . . . 16885 1 3 'sodium phosphate' 'natural abundance' . . . . . . 25 . . mM . . . . 16885 1 4 'sodium chloride' 'natural abundance' . . . . . . 25 . . mM . . . . 16885 1 5 'potassium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 16885 1 6 CHAPS 'natural abundance' . . . . . . 2 . . mM . . . . 16885 1 7 PMSF 'natural abundance' . . . . . . 0.15 . . mM . . . . 16885 1 8 'sodium azide' 'natural abundance' . . . . . . 0.2 . . '% w/v' . . . . 16885 1 9 H2O 'natural abundance' . . . . . . 95 . . % . . . . 16885 1 10 H2O 'natural abundance' . . . . . . 5 . . % . . . . 16885 1 stop_ save_ save_13C15NUBM1+ub _Sample.Sf_category sample _Sample.Sf_framecode 13C15NUBM1+ub _Sample.Entry_ID 16885 _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 'DNA polymerase iota UBM1' '[U-95% 13C; U-99% 15N]' . . 1 $DNA_polymerase_iota_UBM1 . . . 1 2 mM . . . . 16885 2 2 Ubiquitin 'natural abundance' . . 2 $Ubiquitin . . . 4 8 mM . . . . 16885 2 3 'sodium phosphate' 'natural abundance' . . . . . . 25 . . mM . . . . 16885 2 4 'sodium chloride' 'natural abundance' . . . . . . 25 . . mM . . . . 16885 2 5 'potassium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 16885 2 6 CHAPS 'natural abundance' . . . . . . 2 . . mM . . . . 16885 2 7 PMSF 'natural abundance' . . . . . . 0.15 . . mM . . . . 16885 2 8 'sodium azide' 'natural abundance' . . . . . . 0.2 . . '% w/v' . . . . 16885 2 9 H2O 'natural abundance' . . . . . . 95 . . % . . . . 16885 2 10 H2O 'natural abundance' . . . . . . 5 . . % . . . . 16885 2 stop_ save_ save_15NUbi+ubm1 _Sample.Sf_category sample _Sample.Sf_framecode 15NUbi+ubm1 _Sample.Entry_ID 16885 _Sample.ID 3 _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 'DNA polymerase iota UBM1' 'natural abundance' . . 1 $DNA_polymerase_iota_UBM1 . . . 1 2 mM . . . . 16885 3 2 Ubiquitin '[U-99% 15N]' . . 2 $Ubiquitin . . . 4 8 mM . . . . 16885 3 3 'sodium phosphate' 'natural abundance' . . . . . . 25 . . mM . . . . 16885 3 4 'sodium chloride' 'natural abundance' . . . . . . 25 . . mM . . . . 16885 3 5 'potassium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 16885 3 6 CHAPS 'natural abundance' . . . . . . 2 . . mM . . . . 16885 3 7 PMSF 'natural abundance' . . . . . . 0.15 . . mM . . . . 16885 3 8 'sodium azide' 'natural abundance' . . . . . . 0.2 . . '% w/v' . . . . 16885 3 9 H2O 'natural abundance' . . . . . . 95 . . % . . . . 16885 3 10 H2O 'natural abundance' . . . . . . 5 . . % . . . . 16885 3 stop_ save_ save_13C15NUbi+ubm1 _Sample.Sf_category sample _Sample.Sf_framecode 13C15NUbi+ubm1 _Sample.Entry_ID 16885 _Sample.ID 4 _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 'DNA polymerase iota UBM1' 'natural abundance' . . 1 $DNA_polymerase_iota_UBM1 . . . 1 2 mM . . . . 16885 4 2 Ubiquitin '[U-95% 13C; U-99% 15N]' . . 2 $Ubiquitin . . . 4 8 mM . . . . 16885 4 3 'sodium phosphate' 'natural abundance' . . . . . . 25 . . mM . . . . 16885 4 4 'sodium chloride' 'natural abundance' . . . . . . 25 . . mM . . . . 16885 4 5 'potassium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 16885 4 6 CHAPS 'natural abundance' . . . . . . 2 . . mM . . . . 16885 4 7 PMSF 'natural abundance' . . . . . . 0.15 . . mM . . . . 16885 4 8 'sodium azide' 'natural abundance' . . . . . . 0.2 . . '% w/v' . . . . 16885 4 9 H2O 'natural abundance' . . . . . . 95 . . % . . . . 16885 4 10 H2O 'natural abundance' . . . . . . 5 . . % . . . . 16885 4 stop_ save_ save_labUbi-overUBM1 _Sample.Sf_category sample _Sample.Sf_framecode labUbi-overUBM1 _Sample.Entry_ID 16885 _Sample.ID 5 _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 'DNA polymerase iota UBM1' 'natural abundance' . . 1 $DNA_polymerase_iota_UBM1 . . . 1 2 mM . . . . 16885 5 2 Ubiquitin '[U-95% 13C; U-99% 15N]' . . 2 $Ubiquitin . . . 4 8 mM . . . . 16885 5 3 'sodium phosphate' 'natural abundance' . . . . . . 25 . . mM . . . . 16885 5 4 'sodium chloride' 'natural abundance' . . . . . . 25 . . mM . . . . 16885 5 5 'potassium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 16885 5 6 CHAPS 'natural abundance' . . . . . . 2 . . mM . . . . 16885 5 7 PMSF 'natural abundance' . . . . . . 0.15 . . mM . . . . 16885 5 8 'sodium azide' 'natural abundance' . . . . . . 0.2 . . '% w/v' . . . . 16885 5 9 H2O 'natural abundance' . . . . . . 95 . . % . . . . 16885 5 10 H2O 'natural abundance' . . . . . . 5 . . % . . . . 16885 5 stop_ save_ ####################### # Sample conditions # ####################### save_Sample_conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Sample_conditions _Sample_condition_list.Entry_ID 16885 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.189 . M 16885 1 pH 6.0 . pH 16885 1 pressure 1 . atm 16885 1 temperature 288 . K 16885 1 stop_ save_ ############################ # Computer software used # ############################ save_AMBER _Software.Sf_category software _Software.Sf_framecode AMBER _Software.Entry_ID 16885 _Software.ID 1 _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' . . 16885 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 16885 1 stop_ save_ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 16885 _Software.ID 2 _Software.Name TOPSPIN _Software.Version 2.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 16885 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 16885 2 processing 16885 2 stop_ save_ save_Molmol _Software.Sf_category software _Software.Sf_framecode Molmol _Software.Entry_ID 16885 _Software.ID 3 _Software.Name Molmol _Software.Version 2k.2 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Koradi, Billeter and Wuthrich' . . 16885 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'geometry optimization' 16885 3 stop_ save_ save_UNIO'08 _Software.Sf_category software _Software.Sf_framecode UNIO'08 _Software.Entry_ID 16885 _Software.ID 4 _Software.Name UNIO _Software.Version 1.0.4 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'T. Herrmann' . . 16885 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 16885 4 'peak picking' 16885 4 'structure solution' 16885 4 stop_ save_ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 16885 _Software.ID 5 _Software.Name DYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Braun and Wuthrich' . . 16885 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 16885 5 stop_ save_ save_CARA _Software.Sf_category software _Software.Sf_framecode CARA _Software.Entry_ID 16885 _Software.ID 6 _Software.Name CARA _Software.Version 1.8.4 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'R. Keller' . . 16885 6 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 16885 6 'data analysis' 16885 6 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 16885 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 16885 _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 16885 _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 16885 _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 . 600 . . . 16885 1 2 spectrometer_2 Bruker Avance . 750 . . . 16885 1 3 spectrometer_3 Bruker Avance . 900 . . . 16885 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 16885 _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 HNCACB' no . . . . . . . . . . 2 $13C15NUBM1+ub isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 2 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $15NUBM1+ub isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 3 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $15NUBM1+ub isotropic . . 1 $Sample_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16885 1 4 '3D 1H-13C NOESY' no . . . . . . . . . . 2 $13C15NUBM1+ub isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 5 '3D HCCH-COSY' no . . . . . . . . . . 2 $13C15NUBM1+ub isotropic . . 1 $Sample_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16885 1 6 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $15NUBM1+ub isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 7 '2D 1H-13C HSQC' no . . . . . . . . . . 2 $13C15NUBM1+ub isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 8 '3D HNCACB' no . . . . . . . . . . 4 $13C15NUbi+ubm1 isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 9 '3D 1H-15N NOESY' no . . . . . . . . . . 3 $15NUbi+ubm1 isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 10 '3D 1H-15N TOCSY' no . . . . . . . . . . 3 $15NUbi+ubm1 isotropic . . 1 $Sample_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16885 1 11 '3D 1H-13C NOESY' no . . . . . . . . . . 4 $13C15NUbi+ubm1 isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 12 '3D HCCH-COSY' no . . . . . . . . . . 4 $13C15NUbi+ubm1 isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 13 '2D 1H-15N HSQC' no . . . . . . . . . . 3 $15NUbi+ubm1 isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 14 '2D 1H-13C HSQC' no . . . . . . . . . . 4 $13C15NUbi+ubm1 isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 15 '3D 1H-13C-filtered-13C-edited NOESY' no . . . . . . . . . . 2 $13C15NUBM1+ub isotropic . . 1 $Sample_conditions . . . 3 $spectrometer_3 . . . . . . . . . . . . . . . . 16885 1 16 '3D 1H-13C-filtered-13C-edited NOESY' no . . . . . . . . . . 4 $13C15NUbi+ubm1 isotropic . . 1 $Sample_conditions . . . 3 $spectrometer_3 . . . . . . . . . . . . . . . . 16885 1 17 '3D 1H-13C-filtered-13C-edited NOESY' no . . . . . . . . . . 5 $labUbi-overUBM1 isotropic . . 1 $Sample_conditions . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 16885 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 16885 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 16885 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 16885 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 16885 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_UBM1_shift_list _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode UBM1_shift_list _Assigned_chem_shift_list.Entry_ID 16885 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Sample_conditions _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '3D HNCACB' . . . 16885 1 2 '3D 1H-15N NOESY' . . . 16885 1 3 '3D 1H-15N TOCSY' . . . 16885 1 4 '3D 1H-13C NOESY' . . . 16885 1 5 '3D HCCH-COSY' . . . 16885 1 6 '2D 1H-15N HSQC' . . . 16885 1 7 '2D 1H-13C HSQC' . . . 16885 1 8 '3D HNCACB' . . . 16885 1 9 '3D 1H-15N NOESY' . . . 16885 1 10 '3D 1H-15N TOCSY' . . . 16885 1 11 '3D 1H-13C NOESY' . . . 16885 1 12 '3D HCCH-COSY' . . . 16885 1 13 '2D 1H-15N HSQC' . . . 16885 1 14 '2D 1H-13C HSQC' . . . 16885 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 3.915 0.020 . 2 . . . . 485 GLY HA1 . 16885 1 2 . 1 1 1 1 GLY HA3 H 1 3.931 0.020 . 2 . . . . 485 GLY HA2 . 16885 1 3 . 1 1 1 1 GLY CA C 13 43.403 0.300 . 1 . . . . 485 GLY CA . 16885 1 4 . 1 1 2 2 SER H H 1 8.809 0.020 . 1 . . . . 486 SER HN . 16885 1 5 . 1 1 2 2 SER HA H 1 4.532 0.020 . 1 . . . . 486 SER HA . 16885 1 6 . 1 1 2 2 SER HB2 H 1 3.906 0.020 . 2 . . . . 486 SER QB . 16885 1 7 . 1 1 2 2 SER HB3 H 1 3.906 0.020 . 2 . . . . 486 SER QB . 16885 1 8 . 1 1 2 2 SER CA C 13 58.447 0.300 . 1 . . . . 486 SER CA . 16885 1 9 . 1 1 2 2 SER CB C 13 63.801 0.300 . 1 . . . . 486 SER CB . 16885 1 10 . 1 1 2 2 SER N N 15 113.768 0.300 . 1 . . . . 486 SER N . 16885 1 11 . 1 1 3 3 ASP H H 1 8.686 0.020 . 1 . . . . 487 ASP HN . 16885 1 12 . 1 1 3 3 ASP HA H 1 4.699 0.020 . 1 . . . . 487 ASP HA . 16885 1 13 . 1 1 3 3 ASP HB2 H 1 2.699 0.020 . 2 . . . . 487 ASP HB2 . 16885 1 14 . 1 1 3 3 ASP HB3 H 1 2.759 0.020 . 2 . . . . 487 ASP HB3 . 16885 1 15 . 1 1 3 3 ASP CA C 13 54.455 0.300 . 1 . . . . 487 ASP CA . 16885 1 16 . 1 1 3 3 ASP CB C 13 41.052 0.300 . 1 . . . . 487 ASP CB . 16885 1 17 . 1 1 3 3 ASP N N 15 120.187 0.300 . 1 . . . . 487 ASP N . 16885 1 18 . 1 1 4 4 THR H H 1 8.204 0.020 . 1 . . . . 488 THR HN . 16885 1 19 . 1 1 4 4 THR HA H 1 4.391 0.020 . 1 . . . . 488 THR HA . 16885 1 20 . 1 1 4 4 THR HB H 1 4.331 0.020 . 1 . . . . 488 THR HB . 16885 1 21 . 1 1 4 4 THR HG21 H 1 1.210 0.020 . 1 . . . . 488 THR QG2 . 16885 1 22 . 1 1 4 4 THR HG22 H 1 1.210 0.020 . 1 . . . . 488 THR QG2 . 16885 1 23 . 1 1 4 4 THR HG23 H 1 1.210 0.020 . 1 . . . . 488 THR QG2 . 16885 1 24 . 1 1 4 4 THR CA C 13 61.810 0.300 . 1 . . . . 488 THR CA . 16885 1 25 . 1 1 4 4 THR CB C 13 69.578 0.300 . 1 . . . . 488 THR CB . 16885 1 26 . 1 1 4 4 THR CG2 C 13 21.576 0.300 . 1 . . . . 488 THR CG2 . 16885 1 27 . 1 1 4 4 THR N N 15 111.886 0.300 . 1 . . . . 488 THR N . 16885 1 28 . 1 1 5 5 SER H H 1 8.401 0.020 . 1 . . . . 489 SER HN . 16885 1 29 . 1 1 5 5 SER HA H 1 4.434 0.020 . 1 . . . . 489 SER HA . 16885 1 30 . 1 1 5 5 SER HB2 H 1 3.877 0.020 . 2 . . . . 489 SER HB2 . 16885 1 31 . 1 1 5 5 SER HB3 H 1 3.905 0.020 . 2 . . . . 489 SER HB3 . 16885 1 32 . 1 1 5 5 SER CA C 13 58.784 0.300 . 1 . . . . 489 SER CA . 16885 1 33 . 1 1 5 5 SER CB C 13 63.780 0.300 . 1 . . . . 489 SER CB . 16885 1 34 . 1 1 5 5 SER N N 15 115.891 0.300 . 1 . . . . 489 SER N . 16885 1 35 . 1 1 6 6 ASP H H 1 8.386 0.020 . 1 . . . . 490 ASP HN . 16885 1 36 . 1 1 6 6 ASP HA H 1 4.637 0.020 . 1 . . . . 490 ASP HA . 16885 1 37 . 1 1 6 6 ASP HB2 H 1 2.585 0.020 . 2 . . . . 490 ASP HB2 . 16885 1 38 . 1 1 6 6 ASP HB3 H 1 2.697 0.020 . 2 . . . . 490 ASP HB3 . 16885 1 39 . 1 1 6 6 ASP CA C 13 54.224 0.300 . 1 . . . . 490 ASP CA . 16885 1 40 . 1 1 6 6 ASP CB C 13 40.977 0.300 . 1 . . . . 490 ASP CB . 16885 1 41 . 1 1 6 6 ASP N N 15 120.145 0.300 . 1 . . . . 490 ASP N . 16885 1 42 . 1 1 7 7 LEU H H 1 8.117 0.020 . 1 . . . . 491 LEU HN . 16885 1 43 . 1 1 7 7 LEU HA H 1 4.574 0.020 . 1 . . . . 491 LEU HA . 16885 1 44 . 1 1 7 7 LEU HB2 H 1 1.515 0.020 . 2 . . . . 491 LEU HB2 . 16885 1 45 . 1 1 7 7 LEU HB3 H 1 1.624 0.020 . 2 . . . . 491 LEU HB3 . 16885 1 46 . 1 1 7 7 LEU HD11 H 1 0.909 0.020 . 2 . . . . 491 LEU QD1 . 16885 1 47 . 1 1 7 7 LEU HD12 H 1 0.909 0.020 . 2 . . . . 491 LEU QD1 . 16885 1 48 . 1 1 7 7 LEU HD13 H 1 0.909 0.020 . 2 . . . . 491 LEU QD1 . 16885 1 49 . 1 1 7 7 LEU HD21 H 1 0.942 0.020 . 2 . . . . 491 LEU QD2 . 16885 1 50 . 1 1 7 7 LEU HD22 H 1 0.942 0.020 . 2 . . . . 491 LEU QD2 . 16885 1 51 . 1 1 7 7 LEU HD23 H 1 0.942 0.020 . 2 . . . . 491 LEU QD2 . 16885 1 52 . 1 1 7 7 LEU HG H 1 1.672 0.020 . 1 . . . . 491 LEU HG . 16885 1 53 . 1 1 7 7 LEU CA C 13 53.305 0.300 . 1 . . . . 491 LEU CA . 16885 1 54 . 1 1 7 7 LEU CB C 13 41.689 0.300 . 1 . . . . 491 LEU CB . 16885 1 55 . 1 1 7 7 LEU CD1 C 13 23.463 0.300 . 2 . . . . 491 LEU CD1 . 16885 1 56 . 1 1 7 7 LEU CD2 C 13 25.280 0.300 . 2 . . . . 491 LEU CD2 . 16885 1 57 . 1 1 7 7 LEU CG C 13 27.015 0.300 . 1 . . . . 491 LEU CG . 16885 1 58 . 1 1 7 7 LEU N N 15 121.099 0.300 . 1 . . . . 491 LEU N . 16885 1 59 . 1 1 8 8 PRO HA H 1 4.446 0.020 . 1 . . . . 492 PRO HA . 16885 1 60 . 1 1 8 8 PRO HB2 H 1 1.899 0.020 . 2 . . . . 492 PRO HB2 . 16885 1 61 . 1 1 8 8 PRO HB3 H 1 2.264 0.020 . 2 . . . . 492 PRO HB3 . 16885 1 62 . 1 1 8 8 PRO HD2 H 1 3.603 0.020 . 2 . . . . 492 PRO HD2 . 16885 1 63 . 1 1 8 8 PRO HD3 H 1 3.830 0.020 . 2 . . . . 492 PRO HD3 . 16885 1 64 . 1 1 8 8 PRO HG2 H 1 2.018 0.020 . 2 . . . . 492 PRO QG . 16885 1 65 . 1 1 8 8 PRO HG3 H 1 2.018 0.020 . 2 . . . . 492 PRO QG . 16885 1 66 . 1 1 8 8 PRO CA C 13 62.876 0.300 . 1 . . . . 492 PRO CA . 16885 1 67 . 1 1 8 8 PRO CB C 13 31.768 0.300 . 1 . . . . 492 PRO CB . 16885 1 68 . 1 1 8 8 PRO CD C 13 50.480 0.300 . 1 . . . . 492 PRO CD . 16885 1 69 . 1 1 8 8 PRO CG C 13 27.475 0.300 . 1 . . . . 492 PRO CG . 16885 1 70 . 1 1 9 9 LEU H H 1 8.337 0.020 . 1 . . . . 493 LEU HN . 16885 1 71 . 1 1 9 9 LEU HA H 1 4.198 0.020 . 1 . . . . 493 LEU HA . 16885 1 72 . 1 1 9 9 LEU HB2 H 1 1.540 0.020 . 2 . . . . 493 LEU HB2 . 16885 1 73 . 1 1 9 9 LEU HB3 H 1 1.634 0.020 . 2 . . . . 493 LEU HB3 . 16885 1 74 . 1 1 9 9 LEU HD11 H 1 0.875 0.020 . 2 . . . . 493 LEU QD1 . 16885 1 75 . 1 1 9 9 LEU HD12 H 1 0.875 0.020 . 2 . . . . 493 LEU QD1 . 16885 1 76 . 1 1 9 9 LEU HD13 H 1 0.875 0.020 . 2 . . . . 493 LEU QD1 . 16885 1 77 . 1 1 9 9 LEU HD21 H 1 0.939 0.020 . 2 . . . . 493 LEU QD2 . 16885 1 78 . 1 1 9 9 LEU HD22 H 1 0.939 0.020 . 2 . . . . 493 LEU QD2 . 16885 1 79 . 1 1 9 9 LEU HD23 H 1 0.939 0.020 . 2 . . . . 493 LEU QD2 . 16885 1 80 . 1 1 9 9 LEU HG H 1 1.663 0.020 . 1 . . . . 493 LEU HG . 16885 1 81 . 1 1 9 9 LEU CA C 13 55.513 0.300 . 1 . . . . 493 LEU CA . 16885 1 82 . 1 1 9 9 LEU CB C 13 42.070 0.300 . 1 . . . . 493 LEU CB . 16885 1 83 . 1 1 9 9 LEU CD1 C 13 23.712 0.300 . 2 . . . . 493 LEU CD1 . 16885 1 84 . 1 1 9 9 LEU CD2 C 13 25.009 0.300 . 2 . . . . 493 LEU CD2 . 16885 1 85 . 1 1 9 9 LEU CG C 13 26.973 0.300 . 1 . . . . 493 LEU CG . 16885 1 86 . 1 1 9 9 LEU N N 15 119.929 0.300 . 1 . . . . 493 LEU N . 16885 1 87 . 1 1 10 10 GLN H H 1 8.351 0.020 . 1 . . . . 494 GLN HN . 16885 1 88 . 1 1 10 10 GLN HA H 1 4.250 0.020 . 1 . . . . 494 GLN HA . 16885 1 89 . 1 1 10 10 GLN HB2 H 1 1.959 0.020 . 2 . . . . 494 GLN HB2 . 16885 1 90 . 1 1 10 10 GLN HB3 H 1 2.036 0.020 . 2 . . . . 494 GLN HB3 . 16885 1 91 . 1 1 10 10 GLN HE21 H 1 6.963 0.020 . 2 . . . . 494 GLN HE21 . 16885 1 92 . 1 1 10 10 GLN HE22 H 1 7.635 0.020 . 2 . . . . 494 GLN HE22 . 16885 1 93 . 1 1 10 10 GLN HG2 H 1 2.320 0.020 . 2 . . . . 494 GLN QG . 16885 1 94 . 1 1 10 10 GLN HG3 H 1 2.320 0.020 . 2 . . . . 494 GLN QG . 16885 1 95 . 1 1 10 10 GLN CA C 13 55.754 0.300 . 1 . . . . 494 GLN CA . 16885 1 96 . 1 1 10 10 GLN CB C 13 29.478 0.300 . 1 . . . . 494 GLN CB . 16885 1 97 . 1 1 10 10 GLN CG C 13 33.847 0.300 . 1 . . . . 494 GLN CG . 16885 1 98 . 1 1 10 10 GLN N N 15 118.477 0.300 . 1 . . . . 494 GLN N . 16885 1 99 . 1 1 10 10 GLN NE2 N 15 110.598 0.300 . 1 . . . . 494 GLN NE2 . 16885 1 100 . 1 1 11 11 ALA H H 1 8.188 0.020 . 1 . . . . 495 ALA HN . 16885 1 101 . 1 1 11 11 ALA HA H 1 4.264 0.020 . 1 . . . . 495 ALA HA . 16885 1 102 . 1 1 11 11 ALA HB1 H 1 1.316 0.020 . 1 . . . . 495 ALA QB . 16885 1 103 . 1 1 11 11 ALA HB2 H 1 1.316 0.020 . 1 . . . . 495 ALA QB . 16885 1 104 . 1 1 11 11 ALA HB3 H 1 1.316 0.020 . 1 . . . . 495 ALA QB . 16885 1 105 . 1 1 11 11 ALA CA C 13 51.934 0.300 . 1 . . . . 495 ALA CA . 16885 1 106 . 1 1 11 11 ALA CB C 13 19.309 0.300 . 1 . . . . 495 ALA CB . 16885 1 107 . 1 1 11 11 ALA N N 15 122.523 0.300 . 1 . . . . 495 ALA N . 16885 1 108 . 1 1 12 12 LEU H H 1 8.028 0.020 . 1 . . . . 496 LEU HN . 16885 1 109 . 1 1 12 12 LEU HA H 1 4.279 0.020 . 1 . . . . 496 LEU HA . 16885 1 110 . 1 1 12 12 LEU HB2 H 1 1.103 0.020 . 2 . . . . 496 LEU HB2 . 16885 1 111 . 1 1 12 12 LEU HB3 H 1 1.484 0.020 . 2 . . . . 496 LEU HB3 . 16885 1 112 . 1 1 12 12 LEU HD11 H 1 0.128 0.020 . 2 . . . . 496 LEU QD1 . 16885 1 113 . 1 1 12 12 LEU HD12 H 1 0.128 0.020 . 2 . . . . 496 LEU QD1 . 16885 1 114 . 1 1 12 12 LEU HD13 H 1 0.128 0.020 . 2 . . . . 496 LEU QD1 . 16885 1 115 . 1 1 12 12 LEU HD21 H 1 0.425 0.020 . 2 . . . . 496 LEU QD2 . 16885 1 116 . 1 1 12 12 LEU HD22 H 1 0.425 0.020 . 2 . . . . 496 LEU QD2 . 16885 1 117 . 1 1 12 12 LEU HD23 H 1 0.425 0.020 . 2 . . . . 496 LEU QD2 . 16885 1 118 . 1 1 12 12 LEU HG H 1 1.376 0.020 . 1 . . . . 496 LEU HG . 16885 1 119 . 1 1 12 12 LEU CA C 13 52.491 0.300 . 1 . . . . 496 LEU CA . 16885 1 120 . 1 1 12 12 LEU CB C 13 41.709 0.300 . 1 . . . . 496 LEU CB . 16885 1 121 . 1 1 12 12 LEU CD1 C 13 22.883 0.300 . 2 . . . . 496 LEU CD1 . 16885 1 122 . 1 1 12 12 LEU CD2 C 13 25.067 0.300 . 2 . . . . 496 LEU CD2 . 16885 1 123 . 1 1 12 12 LEU CG C 13 26.497 0.300 . 1 . . . . 496 LEU CG . 16885 1 124 . 1 1 12 12 LEU N N 15 119.385 0.300 . 1 . . . . 496 LEU N . 16885 1 125 . 1 1 13 13 PRO HA H 1 4.360 0.020 . 1 . . . . 497 PRO HA . 16885 1 126 . 1 1 13 13 PRO HB2 H 1 1.759 0.020 . 2 . . . . 497 PRO HB2 . 16885 1 127 . 1 1 13 13 PRO HB3 H 1 2.331 0.020 . 2 . . . . 497 PRO HB3 . 16885 1 128 . 1 1 13 13 PRO HD2 H 1 3.050 0.020 . 2 . . . . 497 PRO HD2 . 16885 1 129 . 1 1 13 13 PRO HD3 H 1 3.694 0.020 . 2 . . . . 497 PRO HD3 . 16885 1 130 . 1 1 13 13 PRO HG2 H 1 1.926 0.020 . 2 . . . . 497 PRO HG2 . 16885 1 131 . 1 1 13 13 PRO HG3 H 1 1.967 0.020 . 2 . . . . 497 PRO HG3 . 16885 1 132 . 1 1 13 13 PRO CA C 13 62.509 0.300 . 1 . . . . 497 PRO CA . 16885 1 133 . 1 1 13 13 PRO CB C 13 31.922 0.300 . 1 . . . . 497 PRO CB . 16885 1 134 . 1 1 13 13 PRO CD C 13 50.337 0.300 . 1 . . . . 497 PRO CD . 16885 1 135 . 1 1 13 13 PRO CG C 13 27.651 0.300 . 1 . . . . 497 PRO CG . 16885 1 136 . 1 1 14 14 GLU H H 1 8.585 0.020 . 1 . . . . 498 GLU HN . 16885 1 137 . 1 1 14 14 GLU HA H 1 4.022 0.020 . 1 . . . . 498 GLU HA . 16885 1 138 . 1 1 14 14 GLU HB2 H 1 1.965 0.020 . 2 . . . . 498 GLU QB . 16885 1 139 . 1 1 14 14 GLU HB3 H 1 1.965 0.020 . 2 . . . . 498 GLU QB . 16885 1 140 . 1 1 14 14 GLU HG2 H 1 2.280 0.020 . 2 . . . . 498 GLU HG2 . 16885 1 141 . 1 1 14 14 GLU HG3 H 1 2.310 0.020 . 2 . . . . 498 GLU HG3 . 16885 1 142 . 1 1 14 14 GLU CA C 13 57.813 0.300 . 1 . . . . 498 GLU CA . 16885 1 143 . 1 1 14 14 GLU CB C 13 29.678 0.300 . 1 . . . . 498 GLU CB . 16885 1 144 . 1 1 14 14 GLU CG C 13 36.086 0.300 . 1 . . . . 498 GLU CG . 16885 1 145 . 1 1 14 14 GLU N N 15 120.123 0.300 . 1 . . . . 498 GLU N . 16885 1 146 . 1 1 15 15 GLY H H 1 8.741 0.020 . 1 . . . . 499 GLY HN . 16885 1 147 . 1 1 15 15 GLY HA2 H 1 3.706 0.020 . 2 . . . . 499 GLY HA1 . 16885 1 148 . 1 1 15 15 GLY HA3 H 1 4.115 0.020 . 2 . . . . 499 GLY HA2 . 16885 1 149 . 1 1 15 15 GLY CA C 13 45.242 0.300 . 1 . . . . 499 GLY CA . 16885 1 150 . 1 1 15 15 GLY N N 15 109.183 0.300 . 1 . . . . 499 GLY N . 16885 1 151 . 1 1 16 16 VAL H H 1 7.260 0.020 . 1 . . . . 500 VAL HN . 16885 1 152 . 1 1 16 16 VAL HA H 1 3.909 0.020 . 1 . . . . 500 VAL HA . 16885 1 153 . 1 1 16 16 VAL HB H 1 1.923 0.020 . 1 . . . . 500 VAL HB . 16885 1 154 . 1 1 16 16 VAL HG11 H 1 0.806 0.020 . 2 . . . . 500 VAL QG1 . 16885 1 155 . 1 1 16 16 VAL HG12 H 1 0.806 0.020 . 2 . . . . 500 VAL QG1 . 16885 1 156 . 1 1 16 16 VAL HG13 H 1 0.806 0.020 . 2 . . . . 500 VAL QG1 . 16885 1 157 . 1 1 16 16 VAL HG21 H 1 0.868 0.020 . 2 . . . . 500 VAL QG2 . 16885 1 158 . 1 1 16 16 VAL HG22 H 1 0.868 0.020 . 2 . . . . 500 VAL QG2 . 16885 1 159 . 1 1 16 16 VAL HG23 H 1 0.868 0.020 . 2 . . . . 500 VAL QG2 . 16885 1 160 . 1 1 16 16 VAL CA C 13 62.173 0.300 . 1 . . . . 500 VAL CA . 16885 1 161 . 1 1 16 16 VAL CB C 13 32.336 0.300 . 1 . . . . 500 VAL CB . 16885 1 162 . 1 1 16 16 VAL CG1 C 13 22.777 0.300 . 2 . . . . 500 VAL CG1 . 16885 1 163 . 1 1 16 16 VAL CG2 C 13 21.947 0.300 . 2 . . . . 500 VAL CG2 . 16885 1 164 . 1 1 16 16 VAL N N 15 116.463 0.300 . 1 . . . . 500 VAL N . 16885 1 165 . 1 1 17 17 ASP H H 1 8.791 0.020 . 1 . . . . 501 ASP HN . 16885 1 166 . 1 1 17 17 ASP HA H 1 4.548 0.020 . 1 . . . . 501 ASP HA . 16885 1 167 . 1 1 17 17 ASP HB2 H 1 2.332 0.020 . 2 . . . . 501 ASP HB2 . 16885 1 168 . 1 1 17 17 ASP HB3 H 1 2.702 0.020 . 2 . . . . 501 ASP HB3 . 16885 1 169 . 1 1 17 17 ASP CA C 13 54.014 0.300 . 1 . . . . 501 ASP CA . 16885 1 170 . 1 1 17 17 ASP CB C 13 42.129 0.300 . 1 . . . . 501 ASP CB . 16885 1 171 . 1 1 17 17 ASP N N 15 125.810 0.300 . 1 . . . . 501 ASP N . 16885 1 172 . 1 1 18 18 GLN H H 1 9.096 0.020 . 1 . . . . 502 GLN HN . 16885 1 173 . 1 1 18 18 GLN HA H 1 3.840 0.020 . 1 . . . . 502 GLN HA . 16885 1 174 . 1 1 18 18 GLN HB2 H 1 2.119 0.020 . 2 . . . . 502 GLN QB . 16885 1 175 . 1 1 18 18 GLN HB3 H 1 2.119 0.020 . 2 . . . . 502 GLN QB . 16885 1 176 . 1 1 18 18 GLN HE21 H 1 6.884 0.020 . 2 . . . . 502 GLN HE21 . 16885 1 177 . 1 1 18 18 GLN HE22 H 1 7.636 0.020 . 2 . . . . 502 GLN HE22 . 16885 1 178 . 1 1 18 18 GLN HG2 H 1 2.384 0.020 . 2 . . . . 502 GLN HG2 . 16885 1 179 . 1 1 18 18 GLN HG3 H 1 2.448 0.020 . 2 . . . . 502 GLN HG3 . 16885 1 180 . 1 1 18 18 GLN CA C 13 59.324 0.300 . 1 . . . . 502 GLN CA . 16885 1 181 . 1 1 18 18 GLN CB C 13 28.519 0.300 . 1 . . . . 502 GLN CB . 16885 1 182 . 1 1 18 18 GLN CG C 13 33.849 0.300 . 1 . . . . 502 GLN CG . 16885 1 183 . 1 1 18 18 GLN N N 15 125.654 0.300 . 1 . . . . 502 GLN N . 16885 1 184 . 1 1 18 18 GLN NE2 N 15 109.488 0.300 . 1 . . . . 502 GLN NE2 . 16885 1 185 . 1 1 19 19 GLU H H 1 8.253 0.020 . 1 . . . . 503 GLU HN . 16885 1 186 . 1 1 19 19 GLU HA H 1 4.054 0.020 . 1 . . . . 503 GLU HA . 16885 1 187 . 1 1 19 19 GLU HB2 H 1 2.131 0.020 . 2 . . . . 503 GLU QB . 16885 1 188 . 1 1 19 19 GLU HB3 H 1 2.131 0.020 . 2 . . . . 503 GLU QB . 16885 1 189 . 1 1 19 19 GLU HG2 H 1 2.252 0.020 . 2 . . . . 503 GLU HG2 . 16885 1 190 . 1 1 19 19 GLU HG3 H 1 2.371 0.020 . 2 . . . . 503 GLU HG3 . 16885 1 191 . 1 1 19 19 GLU CA C 13 58.798 0.300 . 1 . . . . 503 GLU CA . 16885 1 192 . 1 1 19 19 GLU CB C 13 28.881 0.300 . 1 . . . . 503 GLU CB . 16885 1 193 . 1 1 19 19 GLU CG C 13 36.348 0.300 . 1 . . . . 503 GLU CG . 16885 1 194 . 1 1 19 19 GLU N N 15 116.428 0.300 . 1 . . . . 503 GLU N . 16885 1 195 . 1 1 20 20 VAL H H 1 7.851 0.020 . 1 . . . . 504 VAL HN . 16885 1 196 . 1 1 20 20 VAL HA H 1 3.283 0.020 . 1 . . . . 504 VAL HA . 16885 1 197 . 1 1 20 20 VAL HB H 1 2.160 0.020 . 1 . . . . 504 VAL HB . 16885 1 198 . 1 1 20 20 VAL HG11 H 1 0.701 0.020 . 2 . . . . 504 VAL QG1 . 16885 1 199 . 1 1 20 20 VAL HG12 H 1 0.701 0.020 . 2 . . . . 504 VAL QG1 . 16885 1 200 . 1 1 20 20 VAL HG13 H 1 0.701 0.020 . 2 . . . . 504 VAL QG1 . 16885 1 201 . 1 1 20 20 VAL HG21 H 1 1.057 0.020 . 2 . . . . 504 VAL QG2 . 16885 1 202 . 1 1 20 20 VAL HG22 H 1 1.057 0.020 . 2 . . . . 504 VAL QG2 . 16885 1 203 . 1 1 20 20 VAL HG23 H 1 1.057 0.020 . 2 . . . . 504 VAL QG2 . 16885 1 204 . 1 1 20 20 VAL CA C 13 66.212 0.300 . 1 . . . . 504 VAL CA . 16885 1 205 . 1 1 20 20 VAL CB C 13 31.857 0.300 . 1 . . . . 504 VAL CB . 16885 1 206 . 1 1 20 20 VAL CG1 C 13 20.675 0.300 . 2 . . . . 504 VAL CG1 . 16885 1 207 . 1 1 20 20 VAL CG2 C 13 22.175 0.300 . 2 . . . . 504 VAL CG2 . 16885 1 208 . 1 1 20 20 VAL N N 15 118.218 0.300 . 1 . . . . 504 VAL N . 16885 1 209 . 1 1 21 21 PHE H H 1 8.299 0.020 . 1 . . . . 505 PHE HN . 16885 1 210 . 1 1 21 21 PHE HA H 1 3.689 0.020 . 1 . . . . 505 PHE HA . 16885 1 211 . 1 1 21 21 PHE HB2 H 1 2.897 0.020 . 2 . . . . 505 PHE HB2 . 16885 1 212 . 1 1 21 21 PHE HB3 H 1 3.083 0.020 . 2 . . . . 505 PHE HB3 . 16885 1 213 . 1 1 21 21 PHE HD1 H 1 6.994 0.020 . 3 . . . . 505 PHE QD . 16885 1 214 . 1 1 21 21 PHE HD2 H 1 6.994 0.020 . 3 . . . . 505 PHE QD . 16885 1 215 . 1 1 21 21 PHE HE1 H 1 7.307 0.020 . 3 . . . . 505 PHE QE . 16885 1 216 . 1 1 21 21 PHE HE2 H 1 7.307 0.020 . 3 . . . . 505 PHE QE . 16885 1 217 . 1 1 21 21 PHE HZ H 1 7.218 0.020 . 1 . . . . 505 PHE HZ . 16885 1 218 . 1 1 21 21 PHE CA C 13 62.072 0.300 . 1 . . . . 505 PHE CA . 16885 1 219 . 1 1 21 21 PHE CB C 13 40.131 0.300 . 1 . . . . 505 PHE CB . 16885 1 220 . 1 1 21 21 PHE CD1 C 13 131.515 0.300 . 3 . . . . 505 PHE CD1 . 16885 1 221 . 1 1 21 21 PHE CE1 C 13 131.476 0.300 . 3 . . . . 505 PHE CE1 . 16885 1 222 . 1 1 21 21 PHE CZ C 13 129.878 0.300 . 1 . . . . 505 PHE CZ . 16885 1 223 . 1 1 21 21 PHE N N 15 115.860 0.300 . 1 . . . . 505 PHE N . 16885 1 224 . 1 1 22 22 LYS H H 1 7.666 0.020 . 1 . . . . 506 LYS HN . 16885 1 225 . 1 1 22 22 LYS HA H 1 3.807 0.020 . 1 . . . . 506 LYS HA . 16885 1 226 . 1 1 22 22 LYS HB2 H 1 1.918 0.020 . 2 . . . . 506 LYS HB2 . 16885 1 227 . 1 1 22 22 LYS HB3 H 1 1.936 0.020 . 2 . . . . 506 LYS HB3 . 16885 1 228 . 1 1 22 22 LYS HD2 H 1 1.719 0.020 . 2 . . . . 506 LYS HD2 . 16885 1 229 . 1 1 22 22 LYS HD3 H 1 1.749 0.020 . 2 . . . . 506 LYS HD3 . 16885 1 230 . 1 1 22 22 LYS HE2 H 1 2.971 0.020 . 2 . . . . 506 LYS QE . 16885 1 231 . 1 1 22 22 LYS HE3 H 1 2.971 0.020 . 2 . . . . 506 LYS QE . 16885 1 232 . 1 1 22 22 LYS HG2 H 1 1.638 0.020 . 2 . . . . 506 LYS HG2 . 16885 1 233 . 1 1 22 22 LYS HG3 H 1 1.720 0.020 . 2 . . . . 506 LYS HG3 . 16885 1 234 . 1 1 22 22 LYS CA C 13 58.342 0.300 . 1 . . . . 506 LYS CA . 16885 1 235 . 1 1 22 22 LYS CB C 13 32.795 0.300 . 1 . . . . 506 LYS CB . 16885 1 236 . 1 1 22 22 LYS CD C 13 29.613 0.300 . 1 . . . . 506 LYS CD . 16885 1 237 . 1 1 22 22 LYS CE C 13 41.996 0.300 . 1 . . . . 506 LYS CE . 16885 1 238 . 1 1 22 22 LYS CG C 13 25.465 0.300 . 1 . . . . 506 LYS CG . 16885 1 239 . 1 1 22 22 LYS N N 15 111.612 0.300 . 1 . . . . 506 LYS N . 16885 1 240 . 1 1 23 23 GLN H H 1 7.515 0.020 . 1 . . . . 507 GLN HN . 16885 1 241 . 1 1 23 23 GLN HA H 1 4.224 0.020 . 1 . . . . 507 GLN HA . 16885 1 242 . 1 1 23 23 GLN HB2 H 1 1.564 0.020 . 2 . . . . 507 GLN HB2 . 16885 1 243 . 1 1 23 23 GLN HB3 H 1 2.178 0.020 . 2 . . . . 507 GLN HB3 . 16885 1 244 . 1 1 23 23 GLN HE21 H 1 6.898 0.020 . 2 . . . . 507 GLN HE21 . 16885 1 245 . 1 1 23 23 GLN HE22 H 1 7.498 0.020 . 2 . . . . 507 GLN HE22 . 16885 1 246 . 1 1 23 23 GLN HG2 H 1 2.282 0.020 . 2 . . . . 507 GLN HG2 . 16885 1 247 . 1 1 23 23 GLN HG3 H 1 2.391 0.020 . 2 . . . . 507 GLN HG3 . 16885 1 248 . 1 1 23 23 GLN CA C 13 55.021 0.300 . 1 . . . . 507 GLN CA . 16885 1 249 . 1 1 23 23 GLN CB C 13 29.199 0.300 . 1 . . . . 507 GLN CB . 16885 1 250 . 1 1 23 23 GLN CG C 13 33.919 0.300 . 1 . . . . 507 GLN CG . 16885 1 251 . 1 1 23 23 GLN N N 15 113.708 0.300 . 1 . . . . 507 GLN N . 16885 1 252 . 1 1 23 23 GLN NE2 N 15 110.799 0.300 . 1 . . . . 507 GLN NE2 . 16885 1 253 . 1 1 24 24 LEU H H 1 7.056 0.020 . 1 . . . . 508 LEU HN . 16885 1 254 . 1 1 24 24 LEU HA H 1 4.326 0.020 . 1 . . . . 508 LEU HA . 16885 1 255 . 1 1 24 24 LEU HB2 H 1 0.938 0.020 . 2 . . . . 508 LEU HB2 . 16885 1 256 . 1 1 24 24 LEU HB3 H 1 1.493 0.020 . 2 . . . . 508 LEU HB3 . 16885 1 257 . 1 1 24 24 LEU HD11 H 1 0.462 0.020 . 2 . . . . 508 LEU QD1 . 16885 1 258 . 1 1 24 24 LEU HD12 H 1 0.462 0.020 . 2 . . . . 508 LEU QD1 . 16885 1 259 . 1 1 24 24 LEU HD13 H 1 0.462 0.020 . 2 . . . . 508 LEU QD1 . 16885 1 260 . 1 1 24 24 LEU HD21 H 1 0.640 0.020 . 2 . . . . 508 LEU QD2 . 16885 1 261 . 1 1 24 24 LEU HD22 H 1 0.640 0.020 . 2 . . . . 508 LEU QD2 . 16885 1 262 . 1 1 24 24 LEU HD23 H 1 0.640 0.020 . 2 . . . . 508 LEU QD2 . 16885 1 263 . 1 1 24 24 LEU HG H 1 1.955 0.020 . 1 . . . . 508 LEU HG . 16885 1 264 . 1 1 24 24 LEU CA C 13 52.345 0.300 . 1 . . . . 508 LEU CA . 16885 1 265 . 1 1 24 24 LEU CB C 13 40.658 0.300 . 1 . . . . 508 LEU CB . 16885 1 266 . 1 1 24 24 LEU CD1 C 13 21.779 0.300 . 2 . . . . 508 LEU CD1 . 16885 1 267 . 1 1 24 24 LEU CD2 C 13 26.646 0.300 . 2 . . . . 508 LEU CD2 . 16885 1 268 . 1 1 24 24 LEU CG C 13 24.887 0.300 . 1 . . . . 508 LEU CG . 16885 1 269 . 1 1 24 24 LEU N N 15 117.311 0.300 . 1 . . . . 508 LEU N . 16885 1 270 . 1 1 25 25 PRO HA H 1 4.438 0.020 . 1 . . . . 509 PRO HA . 16885 1 271 . 1 1 25 25 PRO HB2 H 1 2.149 0.020 . 2 . . . . 509 PRO HB2 . 16885 1 272 . 1 1 25 25 PRO HB3 H 1 2.565 0.020 . 2 . . . . 509 PRO HB3 . 16885 1 273 . 1 1 25 25 PRO HD2 H 1 3.260 0.020 . 2 . . . . 509 PRO HD2 . 16885 1 274 . 1 1 25 25 PRO HD3 H 1 3.556 0.020 . 2 . . . . 509 PRO HD3 . 16885 1 275 . 1 1 25 25 PRO HG2 H 1 1.968 0.020 . 2 . . . . 509 PRO QG . 16885 1 276 . 1 1 25 25 PRO HG3 H 1 1.968 0.020 . 2 . . . . 509 PRO QG . 16885 1 277 . 1 1 25 25 PRO CA C 13 62.082 0.300 . 1 . . . . 509 PRO CA . 16885 1 278 . 1 1 25 25 PRO CB C 13 32.424 0.300 . 1 . . . . 509 PRO CB . 16885 1 279 . 1 1 25 25 PRO CD C 13 50.165 0.300 . 1 . . . . 509 PRO CD . 16885 1 280 . 1 1 25 25 PRO CG C 13 27.834 0.300 . 1 . . . . 509 PRO CG . 16885 1 281 . 1 1 26 26 ALA H H 1 8.883 0.020 . 1 . . . . 510 ALA HN . 16885 1 282 . 1 1 26 26 ALA HA H 1 4.018 0.020 . 1 . . . . 510 ALA HA . 16885 1 283 . 1 1 26 26 ALA HB1 H 1 1.462 0.020 . 1 . . . . 510 ALA QB . 16885 1 284 . 1 1 26 26 ALA HB2 H 1 1.462 0.020 . 1 . . . . 510 ALA QB . 16885 1 285 . 1 1 26 26 ALA HB3 H 1 1.462 0.020 . 1 . . . . 510 ALA QB . 16885 1 286 . 1 1 26 26 ALA CA C 13 55.372 0.300 . 1 . . . . 510 ALA CA . 16885 1 287 . 1 1 26 26 ALA CB C 13 18.603 0.300 . 1 . . . . 510 ALA CB . 16885 1 288 . 1 1 26 26 ALA N N 15 123.111 0.300 . 1 . . . . 510 ALA N . 16885 1 289 . 1 1 27 27 ASP H H 1 8.903 0.020 . 1 . . . . 511 ASP HN . 16885 1 290 . 1 1 27 27 ASP HA H 1 4.337 0.020 . 1 . . . . 511 ASP HA . 16885 1 291 . 1 1 27 27 ASP HB2 H 1 2.587 0.020 . 2 . . . . 511 ASP HB2 . 16885 1 292 . 1 1 27 27 ASP HB3 H 1 2.751 0.020 . 2 . . . . 511 ASP HB3 . 16885 1 293 . 1 1 27 27 ASP CA C 13 56.406 0.300 . 1 . . . . 511 ASP CA . 16885 1 294 . 1 1 27 27 ASP CB C 13 38.708 0.300 . 1 . . . . 511 ASP CB . 16885 1 295 . 1 1 27 27 ASP N N 15 112.752 0.300 . 1 . . . . 511 ASP N . 16885 1 296 . 1 1 28 28 ILE H H 1 7.198 0.020 . 1 . . . . 512 ILE HN . 16885 1 297 . 1 1 28 28 ILE HA H 1 3.805 0.020 . 1 . . . . 512 ILE HA . 16885 1 298 . 1 1 28 28 ILE HB H 1 1.670 0.020 . 1 . . . . 512 ILE HB . 16885 1 299 . 1 1 28 28 ILE HD11 H 1 0.699 0.020 . 1 . . . . 512 ILE QD1 . 16885 1 300 . 1 1 28 28 ILE HD12 H 1 0.699 0.020 . 1 . . . . 512 ILE QD1 . 16885 1 301 . 1 1 28 28 ILE HD13 H 1 0.699 0.020 . 1 . . . . 512 ILE QD1 . 16885 1 302 . 1 1 28 28 ILE HG12 H 1 1.042 0.020 . 2 . . . . 512 ILE HG12 . 16885 1 303 . 1 1 28 28 ILE HG13 H 1 1.613 0.020 . 2 . . . . 512 ILE HG13 . 16885 1 304 . 1 1 28 28 ILE HG21 H 1 0.900 0.020 . 1 . . . . 512 ILE QG2 . 16885 1 305 . 1 1 28 28 ILE HG22 H 1 0.900 0.020 . 1 . . . . 512 ILE QG2 . 16885 1 306 . 1 1 28 28 ILE HG23 H 1 0.900 0.020 . 1 . . . . 512 ILE QG2 . 16885 1 307 . 1 1 28 28 ILE CA C 13 63.944 0.300 . 1 . . . . 512 ILE CA . 16885 1 308 . 1 1 28 28 ILE CB C 13 37.257 0.300 . 1 . . . . 512 ILE CB . 16885 1 309 . 1 1 28 28 ILE CD1 C 13 12.319 0.300 . 1 . . . . 512 ILE CD1 . 16885 1 310 . 1 1 28 28 ILE CG1 C 13 28.603 0.300 . 1 . . . . 512 ILE CG1 . 16885 1 311 . 1 1 28 28 ILE CG2 C 13 18.575 0.300 . 1 . . . . 512 ILE CG2 . 16885 1 312 . 1 1 28 28 ILE N N 15 120.535 0.300 . 1 . . . . 512 ILE N . 16885 1 313 . 1 1 29 29 GLN H H 1 8.139 0.020 . 1 . . . . 513 GLN HN . 16885 1 314 . 1 1 29 29 GLN HA H 1 3.632 0.020 . 1 . . . . 513 GLN HA . 16885 1 315 . 1 1 29 29 GLN HB2 H 1 1.747 0.020 . 2 . . . . 513 GLN HB2 . 16885 1 316 . 1 1 29 29 GLN HB3 H 1 2.196 0.020 . 2 . . . . 513 GLN HB3 . 16885 1 317 . 1 1 29 29 GLN HE21 H 1 6.472 0.020 . 2 . . . . 513 GLN HE21 . 16885 1 318 . 1 1 29 29 GLN HE22 H 1 6.911 0.020 . 2 . . . . 513 GLN HE22 . 16885 1 319 . 1 1 29 29 GLN HG2 H 1 0.703 0.020 . 2 . . . . 513 GLN HG2 . 16885 1 320 . 1 1 29 29 GLN HG3 H 1 1.934 0.020 . 2 . . . . 513 GLN HG3 . 16885 1 321 . 1 1 29 29 GLN CA C 13 59.959 0.300 . 1 . . . . 513 GLN CA . 16885 1 322 . 1 1 29 29 GLN CB C 13 27.872 0.300 . 1 . . . . 513 GLN CB . 16885 1 323 . 1 1 29 29 GLN CG C 13 33.336 0.300 . 1 . . . . 513 GLN CG . 16885 1 324 . 1 1 29 29 GLN N N 15 116.944 0.300 . 1 . . . . 513 GLN N . 16885 1 325 . 1 1 29 29 GLN NE2 N 15 109.696 0.300 . 1 . . . . 513 GLN NE2 . 16885 1 326 . 1 1 30 30 GLU H H 1 8.002 0.020 . 1 . . . . 514 GLU HN . 16885 1 327 . 1 1 30 30 GLU HA H 1 4.050 0.020 . 1 . . . . 514 GLU HA . 16885 1 328 . 1 1 30 30 GLU HB2 H 1 2.093 0.020 . 2 . . . . 514 GLU HB2 . 16885 1 329 . 1 1 30 30 GLU HB3 H 1 2.120 0.020 . 2 . . . . 514 GLU HB3 . 16885 1 330 . 1 1 30 30 GLU HG2 H 1 2.311 0.020 . 2 . . . . 514 GLU HG2 . 16885 1 331 . 1 1 30 30 GLU HG3 H 1 2.401 0.020 . 2 . . . . 514 GLU HG3 . 16885 1 332 . 1 1 30 30 GLU CA C 13 59.264 0.300 . 1 . . . . 514 GLU CA . 16885 1 333 . 1 1 30 30 GLU CB C 13 29.228 0.300 . 1 . . . . 514 GLU CB . 16885 1 334 . 1 1 30 30 GLU CG C 13 35.954 0.300 . 1 . . . . 514 GLU CG . 16885 1 335 . 1 1 30 30 GLU N N 15 114.113 0.300 . 1 . . . . 514 GLU N . 16885 1 336 . 1 1 31 31 GLU H H 1 7.646 0.020 . 1 . . . . 515 GLU HN . 16885 1 337 . 1 1 31 31 GLU HA H 1 4.011 0.020 . 1 . . . . 515 GLU HA . 16885 1 338 . 1 1 31 31 GLU HB2 H 1 2.154 0.020 . 2 . . . . 515 GLU HB2 . 16885 1 339 . 1 1 31 31 GLU HB3 H 1 2.406 0.020 . 2 . . . . 515 GLU HB3 . 16885 1 340 . 1 1 31 31 GLU HG2 H 1 2.156 0.020 . 2 . . . . 515 GLU HG2 . 16885 1 341 . 1 1 31 31 GLU HG3 H 1 2.562 0.020 . 2 . . . . 515 GLU HG3 . 16885 1 342 . 1 1 31 31 GLU CA C 13 59.423 0.300 . 1 . . . . 515 GLU CA . 16885 1 343 . 1 1 31 31 GLU CB C 13 30.196 0.300 . 1 . . . . 515 GLU CB . 16885 1 344 . 1 1 31 31 GLU CG C 13 35.997 0.300 . 1 . . . . 515 GLU CG . 16885 1 345 . 1 1 31 31 GLU N N 15 119.382 0.300 . 1 . . . . 515 GLU N . 16885 1 346 . 1 1 32 32 ILE H H 1 8.173 0.020 . 1 . . . . 516 ILE HN . 16885 1 347 . 1 1 32 32 ILE HA H 1 3.816 0.020 . 1 . . . . 516 ILE HA . 16885 1 348 . 1 1 32 32 ILE HB H 1 2.224 0.020 . 1 . . . . 516 ILE HB . 16885 1 349 . 1 1 32 32 ILE HD11 H 1 0.903 0.020 . 1 . . . . 516 ILE QD1 . 16885 1 350 . 1 1 32 32 ILE HD12 H 1 0.903 0.020 . 1 . . . . 516 ILE QD1 . 16885 1 351 . 1 1 32 32 ILE HD13 H 1 0.903 0.020 . 1 . . . . 516 ILE QD1 . 16885 1 352 . 1 1 32 32 ILE HG12 H 1 1.255 0.020 . 2 . . . . 516 ILE HG12 . 16885 1 353 . 1 1 32 32 ILE HG13 H 1 1.865 0.020 . 2 . . . . 516 ILE HG13 . 16885 1 354 . 1 1 32 32 ILE HG21 H 1 0.957 0.020 . 1 . . . . 516 ILE QG2 . 16885 1 355 . 1 1 32 32 ILE HG22 H 1 0.957 0.020 . 1 . . . . 516 ILE QG2 . 16885 1 356 . 1 1 32 32 ILE HG23 H 1 0.957 0.020 . 1 . . . . 516 ILE QG2 . 16885 1 357 . 1 1 32 32 ILE CA C 13 64.241 0.300 . 1 . . . . 516 ILE CA . 16885 1 358 . 1 1 32 32 ILE CB C 13 38.442 0.300 . 1 . . . . 516 ILE CB . 16885 1 359 . 1 1 32 32 ILE CD1 C 13 15.623 0.300 . 1 . . . . 516 ILE CD1 . 16885 1 360 . 1 1 32 32 ILE CG1 C 13 28.897 0.300 . 1 . . . . 516 ILE CG1 . 16885 1 361 . 1 1 32 32 ILE CG2 C 13 17.454 0.300 . 1 . . . . 516 ILE CG2 . 16885 1 362 . 1 1 32 32 ILE N N 15 117.774 0.300 . 1 . . . . 516 ILE N . 16885 1 363 . 1 1 33 33 LEU H H 1 8.383 0.020 . 1 . . . . 517 LEU HN . 16885 1 364 . 1 1 33 33 LEU HA H 1 4.090 0.020 . 1 . . . . 517 LEU HA . 16885 1 365 . 1 1 33 33 LEU HB2 H 1 1.563 0.020 . 2 . . . . 517 LEU HB2 . 16885 1 366 . 1 1 33 33 LEU HB3 H 1 1.930 0.020 . 2 . . . . 517 LEU HB3 . 16885 1 367 . 1 1 33 33 LEU HD11 H 1 0.735 0.020 . 2 . . . . 517 LEU QD1 . 16885 1 368 . 1 1 33 33 LEU HD12 H 1 0.735 0.020 . 2 . . . . 517 LEU QD1 . 16885 1 369 . 1 1 33 33 LEU HD13 H 1 0.735 0.020 . 2 . . . . 517 LEU QD1 . 16885 1 370 . 1 1 33 33 LEU HD21 H 1 0.970 0.020 . 2 . . . . 517 LEU QD2 . 16885 1 371 . 1 1 33 33 LEU HD22 H 1 0.970 0.020 . 2 . . . . 517 LEU QD2 . 16885 1 372 . 1 1 33 33 LEU HD23 H 1 0.970 0.020 . 2 . . . . 517 LEU QD2 . 16885 1 373 . 1 1 33 33 LEU HG H 1 1.984 0.020 . 1 . . . . 517 LEU HG . 16885 1 374 . 1 1 33 33 LEU CA C 13 57.271 0.300 . 1 . . . . 517 LEU CA . 16885 1 375 . 1 1 33 33 LEU CB C 13 41.842 0.300 . 1 . . . . 517 LEU CB . 16885 1 376 . 1 1 33 33 LEU CD1 C 13 22.657 0.300 . 2 . . . . 517 LEU CD1 . 16885 1 377 . 1 1 33 33 LEU CD2 C 13 25.590 0.300 . 2 . . . . 517 LEU CD2 . 16885 1 378 . 1 1 33 33 LEU CG C 13 26.813 0.300 . 1 . . . . 517 LEU CG . 16885 1 379 . 1 1 33 33 LEU N N 15 116.633 0.300 . 1 . . . . 517 LEU N . 16885 1 380 . 1 1 34 34 SER H H 1 8.190 0.020 . 1 . . . . 518 SER HN . 16885 1 381 . 1 1 34 34 SER HA H 1 4.448 0.020 . 1 . . . . 518 SER HA . 16885 1 382 . 1 1 34 34 SER HB2 H 1 4.043 0.020 . 2 . . . . 518 SER QB . 16885 1 383 . 1 1 34 34 SER HB3 H 1 4.043 0.020 . 2 . . . . 518 SER QB . 16885 1 384 . 1 1 34 34 SER CA C 13 59.639 0.300 . 1 . . . . 518 SER CA . 16885 1 385 . 1 1 34 34 SER CB C 13 64.100 0.300 . 1 . . . . 518 SER CB . 16885 1 386 . 1 1 34 34 SER N N 15 110.734 0.300 . 1 . . . . 518 SER N . 16885 1 387 . 1 1 35 35 GLY H H 1 8.007 0.020 . 1 . . . . 519 GLY HN . 16885 1 388 . 1 1 35 35 GLY HA2 H 1 3.965 0.020 . 2 . . . . 519 GLY HA1 . 16885 1 389 . 1 1 35 35 GLY HA3 H 1 4.083 0.020 . 2 . . . . 519 GLY HA2 . 16885 1 390 . 1 1 35 35 GLY CA C 13 46.182 0.300 . 1 . . . . 519 GLY CA . 16885 1 391 . 1 1 35 35 GLY N N 15 108.167 0.300 . 1 . . . . 519 GLY N . 16885 1 392 . 1 1 36 36 LYS H H 1 8.083 0.020 . 1 . . . . 520 LYS HN . 16885 1 393 . 1 1 36 36 LYS HA H 1 4.366 0.020 . 1 . . . . 520 LYS HA . 16885 1 394 . 1 1 36 36 LYS HB2 H 1 1.718 0.020 . 2 . . . . 520 LYS HB2 . 16885 1 395 . 1 1 36 36 LYS HB3 H 1 1.891 0.020 . 2 . . . . 520 LYS HB3 . 16885 1 396 . 1 1 36 36 LYS HD2 H 1 1.650 0.020 . 2 . . . . 520 LYS HD2 . 16885 1 397 . 1 1 36 36 LYS HD3 H 1 1.675 0.020 . 2 . . . . 520 LYS HD3 . 16885 1 398 . 1 1 36 36 LYS HE2 H 1 2.980 0.020 . 2 . . . . 520 LYS QE . 16885 1 399 . 1 1 36 36 LYS HE3 H 1 2.980 0.020 . 2 . . . . 520 LYS QE . 16885 1 400 . 1 1 36 36 LYS HG2 H 1 1.416 0.020 . 2 . . . . 520 LYS HG2 . 16885 1 401 . 1 1 36 36 LYS HG3 H 1 1.448 0.020 . 2 . . . . 520 LYS HG3 . 16885 1 402 . 1 1 36 36 LYS CA C 13 56.428 0.300 . 1 . . . . 520 LYS CA . 16885 1 403 . 1 1 36 36 LYS CB C 13 33.415 0.300 . 1 . . . . 520 LYS CB . 16885 1 404 . 1 1 36 36 LYS CD C 13 29.051 0.300 . 1 . . . . 520 LYS CD . 16885 1 405 . 1 1 36 36 LYS CE C 13 42.147 0.300 . 1 . . . . 520 LYS CE . 16885 1 406 . 1 1 36 36 LYS CG C 13 24.823 0.300 . 1 . . . . 520 LYS CG . 16885 1 407 . 1 1 36 36 LYS N N 15 117.662 0.300 . 1 . . . . 520 LYS N . 16885 1 408 . 1 1 37 37 SER H H 1 8.204 0.020 . 1 . . . . 521 SER HN . 16885 1 409 . 1 1 37 37 SER HA H 1 4.398 0.020 . 1 . . . . 521 SER HA . 16885 1 410 . 1 1 37 37 SER HB2 H 1 3.873 0.020 . 2 . . . . 521 SER HB2 . 16885 1 411 . 1 1 37 37 SER HB3 H 1 3.905 0.020 . 2 . . . . 521 SER HB3 . 16885 1 412 . 1 1 37 37 SER CA C 13 58.795 0.300 . 1 . . . . 521 SER CA . 16885 1 413 . 1 1 37 37 SER CB C 13 63.585 0.300 . 1 . . . . 521 SER CB . 16885 1 414 . 1 1 37 37 SER N N 15 113.150 0.300 . 1 . . . . 521 SER N . 16885 1 415 . 1 1 38 38 ARG H H 1 8.526 0.020 . 1 . . . . 522 ARG HN . 16885 1 416 . 1 1 38 38 ARG HA H 1 4.285 0.020 . 1 . . . . 522 ARG HA . 16885 1 417 . 1 1 38 38 ARG HB2 H 1 1.796 0.020 . 2 . . . . 522 ARG HB2 . 16885 1 418 . 1 1 38 38 ARG HB3 H 1 1.901 0.020 . 2 . . . . 522 ARG HB3 . 16885 1 419 . 1 1 38 38 ARG HD2 H 1 3.227 0.020 . 2 . . . . 522 ARG QD . 16885 1 420 . 1 1 38 38 ARG HD3 H 1 3.227 0.020 . 2 . . . . 522 ARG QD . 16885 1 421 . 1 1 38 38 ARG HE H 1 7.357 0.020 . 1 . . . . 522 ARG HE . 16885 1 422 . 1 1 38 38 ARG HG2 H 1 1.653 0.020 . 2 . . . . 522 ARG HG2 . 16885 1 423 . 1 1 38 38 ARG HG3 H 1 1.697 0.020 . 2 . . . . 522 ARG HG3 . 16885 1 424 . 1 1 38 38 ARG CA C 13 56.688 0.300 . 1 . . . . 522 ARG CA . 16885 1 425 . 1 1 38 38 ARG CB C 13 30.708 0.300 . 1 . . . . 522 ARG CB . 16885 1 426 . 1 1 38 38 ARG CD C 13 43.436 0.300 . 1 . . . . 522 ARG CD . 16885 1 427 . 1 1 38 38 ARG CG C 13 27.364 0.300 . 1 . . . . 522 ARG CG . 16885 1 428 . 1 1 38 38 ARG N N 15 121.095 0.300 . 1 . . . . 522 ARG N . 16885 1 429 . 1 1 38 38 ARG NE N 15 82.229 0.300 . 1 . . . . 522 ARG NE . 16885 1 430 . 1 1 39 39 GLU H H 1 8.763 0.020 . 1 . . . . 523 GLU HN . 16885 1 431 . 1 1 39 39 GLU HA H 1 4.138 0.020 . 1 . . . . 523 GLU HA . 16885 1 432 . 1 1 39 39 GLU HB2 H 1 1.940 0.020 . 2 . . . . 523 GLU HB2 . 16885 1 433 . 1 1 39 39 GLU HB3 H 1 1.978 0.020 . 2 . . . . 523 GLU HB3 . 16885 1 434 . 1 1 39 39 GLU HG2 H 1 2.314 0.020 . 2 . . . . 523 GLU QG . 16885 1 435 . 1 1 39 39 GLU HG3 H 1 2.314 0.020 . 2 . . . . 523 GLU QG . 16885 1 436 . 1 1 39 39 GLU CA C 13 57.519 0.300 . 1 . . . . 523 GLU CA . 16885 1 437 . 1 1 39 39 GLU CB C 13 30.014 0.300 . 1 . . . . 523 GLU CB . 16885 1 438 . 1 1 39 39 GLU CG C 13 36.597 0.300 . 1 . . . . 523 GLU CG . 16885 1 439 . 1 1 39 39 GLU N N 15 118.990 0.300 . 1 . . . . 523 GLU N . 16885 1 440 . 1 1 40 40 ASN H H 1 8.426 0.020 . 1 . . . . 524 ASN HN . 16885 1 441 . 1 1 40 40 ASN HA H 1 4.688 0.020 . 1 . . . . 524 ASN HA . 16885 1 442 . 1 1 40 40 ASN HB2 H 1 2.763 0.020 . 2 . . . . 524 ASN HB2 . 16885 1 443 . 1 1 40 40 ASN HB3 H 1 2.878 0.020 . 2 . . . . 524 ASN HB3 . 16885 1 444 . 1 1 40 40 ASN HD21 H 1 6.964 0.020 . 2 . . . . 524 ASN HD21 . 16885 1 445 . 1 1 40 40 ASN HD22 H 1 7.674 0.020 . 2 . . . . 524 ASN HD22 . 16885 1 446 . 1 1 40 40 ASN CA C 13 53.308 0.300 . 1 . . . . 524 ASN CA . 16885 1 447 . 1 1 40 40 ASN CB C 13 38.573 0.300 . 1 . . . . 524 ASN CB . 16885 1 448 . 1 1 40 40 ASN N N 15 116.728 0.300 . 1 . . . . 524 ASN N . 16885 1 449 . 1 1 40 40 ASN ND2 N 15 110.552 0.300 . 1 . . . . 524 ASN ND2 . 16885 1 450 . 1 1 41 41 LEU H H 1 8.227 0.020 . 1 . . . . 525 LEU HN . 16885 1 451 . 1 1 41 41 LEU HA H 1 4.304 0.020 . 1 . . . . 525 LEU HA . 16885 1 452 . 1 1 41 41 LEU HB2 H 1 1.609 0.020 . 2 . . . . 525 LEU HB2 . 16885 1 453 . 1 1 41 41 LEU HB3 H 1 1.683 0.020 . 2 . . . . 525 LEU HB3 . 16885 1 454 . 1 1 41 41 LEU HD11 H 1 0.814 0.020 . 2 . . . . 525 LEU QD1 . 16885 1 455 . 1 1 41 41 LEU HD12 H 1 0.814 0.020 . 2 . . . . 525 LEU QD1 . 16885 1 456 . 1 1 41 41 LEU HD13 H 1 0.814 0.020 . 2 . . . . 525 LEU QD1 . 16885 1 457 . 1 1 41 41 LEU HD21 H 1 0.908 0.020 . 2 . . . . 525 LEU QD2 . 16885 1 458 . 1 1 41 41 LEU HD22 H 1 0.908 0.020 . 2 . . . . 525 LEU QD2 . 16885 1 459 . 1 1 41 41 LEU HD23 H 1 0.908 0.020 . 2 . . . . 525 LEU QD2 . 16885 1 460 . 1 1 41 41 LEU HG H 1 1.619 0.020 . 1 . . . . 525 LEU HG . 16885 1 461 . 1 1 41 41 LEU CA C 13 55.332 0.300 . 1 . . . . 525 LEU CA . 16885 1 462 . 1 1 41 41 LEU CB C 13 42.094 0.300 . 1 . . . . 525 LEU CB . 16885 1 463 . 1 1 41 41 LEU CD1 C 13 23.156 0.300 . 2 . . . . 525 LEU CD1 . 16885 1 464 . 1 1 41 41 LEU CD2 C 13 25.218 0.300 . 2 . . . . 525 LEU CD2 . 16885 1 465 . 1 1 41 41 LEU CG C 13 26.803 0.300 . 1 . . . . 525 LEU CG . 16885 1 466 . 1 1 41 41 LEU N N 15 120.630 0.300 . 1 . . . . 525 LEU N . 16885 1 467 . 1 1 42 42 LYS H H 1 8.207 0.020 . 1 . . . . 526 LYS HN . 16885 1 468 . 1 1 42 42 LYS HA H 1 4.284 0.020 . 1 . . . . 526 LYS HA . 16885 1 469 . 1 1 42 42 LYS HB2 H 1 1.812 0.020 . 2 . . . . 526 LYS HB2 . 16885 1 470 . 1 1 42 42 LYS HB3 H 1 1.875 0.020 . 2 . . . . 526 LYS HB3 . 16885 1 471 . 1 1 42 42 LYS HD2 H 1 1.693 0.020 . 2 . . . . 526 LYS QD . 16885 1 472 . 1 1 42 42 LYS HD3 H 1 1.693 0.020 . 2 . . . . 526 LYS QD . 16885 1 473 . 1 1 42 42 LYS HE2 H 1 2.999 0.020 . 2 . . . . 526 LYS QE . 16885 1 474 . 1 1 42 42 LYS HE3 H 1 2.999 0.020 . 2 . . . . 526 LYS QE . 16885 1 475 . 1 1 42 42 LYS HG2 H 1 1.421 0.020 . 2 . . . . 526 LYS HG2 . 16885 1 476 . 1 1 42 42 LYS HG3 H 1 1.480 0.020 . 2 . . . . 526 LYS HG3 . 16885 1 477 . 1 1 42 42 LYS CA C 13 56.667 0.300 . 1 . . . . 526 LYS CA . 16885 1 478 . 1 1 42 42 LYS CB C 13 32.809 0.300 . 1 . . . . 526 LYS CB . 16885 1 479 . 1 1 42 42 LYS CD C 13 29.091 0.300 . 1 . . . . 526 LYS CD . 16885 1 480 . 1 1 42 42 LYS CE C 13 42.138 0.300 . 1 . . . . 526 LYS CE . 16885 1 481 . 1 1 42 42 LYS CG C 13 24.802 0.300 . 1 . . . . 526 LYS CG . 16885 1 482 . 1 1 42 42 LYS N N 15 118.607 0.300 . 1 . . . . 526 LYS N . 16885 1 483 . 1 1 43 43 GLY H H 1 8.383 0.020 . 1 . . . . 527 GLY HN . 16885 1 484 . 1 1 43 43 GLY HA2 H 1 3.968 0.020 . 2 . . . . 527 GLY QA . 16885 1 485 . 1 1 43 43 GLY HA3 H 1 3.968 0.020 . 2 . . . . 527 GLY QA . 16885 1 486 . 1 1 43 43 GLY CA C 13 45.278 0.300 . 1 . . . . 527 GLY CA . 16885 1 487 . 1 1 43 43 GLY N N 15 107.468 0.300 . 1 . . . . 527 GLY N . 16885 1 488 . 1 1 44 44 LYS H H 1 8.320 0.020 . 1 . . . . 528 LYS HN . 16885 1 489 . 1 1 44 44 LYS HA H 1 4.333 0.020 . 1 . . . . 528 LYS HA . 16885 1 490 . 1 1 44 44 LYS HB2 H 1 1.793 0.020 . 2 . . . . 528 LYS HB2 . 16885 1 491 . 1 1 44 44 LYS HB3 H 1 1.891 0.020 . 2 . . . . 528 LYS HB3 . 16885 1 492 . 1 1 44 44 LYS HD2 H 1 1.699 0.020 . 2 . . . . 528 LYS QD . 16885 1 493 . 1 1 44 44 LYS HD3 H 1 1.699 0.020 . 2 . . . . 528 LYS QD . 16885 1 494 . 1 1 44 44 LYS HE2 H 1 3.007 0.020 . 2 . . . . 528 LYS QE . 16885 1 495 . 1 1 44 44 LYS HE3 H 1 3.007 0.020 . 2 . . . . 528 LYS QE . 16885 1 496 . 1 1 44 44 LYS HG2 H 1 1.430 0.020 . 2 . . . . 528 LYS HG2 . 16885 1 497 . 1 1 44 44 LYS HG3 H 1 1.480 0.020 . 2 . . . . 528 LYS HG3 . 16885 1 498 . 1 1 44 44 LYS CA C 13 56.500 0.300 . 1 . . . . 528 LYS CA . 16885 1 499 . 1 1 44 44 LYS CB C 13 32.944 0.300 . 1 . . . . 528 LYS CB . 16885 1 500 . 1 1 44 44 LYS CD C 13 29.089 0.300 . 1 . . . . 528 LYS CD . 16885 1 501 . 1 1 44 44 LYS CE C 13 42.192 0.300 . 1 . . . . 528 LYS CE . 16885 1 502 . 1 1 44 44 LYS CG C 13 24.730 0.300 . 1 . . . . 528 LYS CG . 16885 1 503 . 1 1 44 44 LYS N N 15 118.800 0.300 . 1 . . . . 528 LYS N . 16885 1 504 . 1 1 45 45 GLY H H 1 8.586 0.020 . 1 . . . . 529 GLY HN . 16885 1 505 . 1 1 45 45 GLY HA2 H 1 3.992 0.020 . 2 . . . . 529 GLY QA . 16885 1 506 . 1 1 45 45 GLY HA3 H 1 3.992 0.020 . 2 . . . . 529 GLY QA . 16885 1 507 . 1 1 45 45 GLY CA C 13 45.296 0.300 . 1 . . . . 529 GLY CA . 16885 1 508 . 1 1 45 45 GLY N N 15 108.073 0.300 . 1 . . . . 529 GLY N . 16885 1 509 . 1 1 46 46 SER H H 1 8.264 0.020 . 1 . . . . 530 SER HN . 16885 1 510 . 1 1 46 46 SER HA H 1 4.478 0.020 . 1 . . . . 530 SER HA . 16885 1 511 . 1 1 46 46 SER HB2 H 1 3.889 0.020 . 2 . . . . 530 SER QB . 16885 1 512 . 1 1 46 46 SER HB3 H 1 3.889 0.020 . 2 . . . . 530 SER QB . 16885 1 513 . 1 1 46 46 SER CA C 13 58.379 0.300 . 1 . . . . 530 SER CA . 16885 1 514 . 1 1 46 46 SER CB C 13 63.864 0.300 . 1 . . . . 530 SER CB . 16885 1 515 . 1 1 46 46 SER N N 15 113.546 0.300 . 1 . . . . 530 SER N . 16885 1 516 . 1 1 47 47 LEU H H 1 8.456 0.020 . 1 . . . . 531 LEU HN . 16885 1 517 . 1 1 47 47 LEU HA H 1 4.448 0.020 . 1 . . . . 531 LEU HA . 16885 1 518 . 1 1 47 47 LEU HB2 H 1 1.678 0.020 . 2 . . . . 531 LEU QB . 16885 1 519 . 1 1 47 47 LEU HB3 H 1 1.678 0.020 . 2 . . . . 531 LEU QB . 16885 1 520 . 1 1 47 47 LEU HD11 H 1 0.882 0.020 . 2 . . . . 531 LEU QD1 . 16885 1 521 . 1 1 47 47 LEU HD12 H 1 0.882 0.020 . 2 . . . . 531 LEU QD1 . 16885 1 522 . 1 1 47 47 LEU HD13 H 1 0.882 0.020 . 2 . . . . 531 LEU QD1 . 16885 1 523 . 1 1 47 47 LEU HD21 H 1 0.938 0.020 . 2 . . . . 531 LEU QD2 . 16885 1 524 . 1 1 47 47 LEU HD22 H 1 0.938 0.020 . 2 . . . . 531 LEU QD2 . 16885 1 525 . 1 1 47 47 LEU HD23 H 1 0.938 0.020 . 2 . . . . 531 LEU QD2 . 16885 1 526 . 1 1 47 47 LEU HG H 1 1.671 0.020 . 1 . . . . 531 LEU HG . 16885 1 527 . 1 1 47 47 LEU CA C 13 55.255 0.300 . 1 . . . . 531 LEU CA . 16885 1 528 . 1 1 47 47 LEU CB C 13 42.290 0.300 . 1 . . . . 531 LEU CB . 16885 1 529 . 1 1 47 47 LEU CD1 C 13 23.261 0.300 . 2 . . . . 531 LEU CD1 . 16885 1 530 . 1 1 47 47 LEU CD2 C 13 25.146 0.300 . 2 . . . . 531 LEU CD2 . 16885 1 531 . 1 1 47 47 LEU CG C 13 26.921 0.300 . 1 . . . . 531 LEU CG . 16885 1 532 . 1 1 47 47 LEU N N 15 122.135 0.300 . 1 . . . . 531 LEU N . 16885 1 533 . 1 1 48 48 SER H H 1 7.932 0.020 . 1 . . . . 532 SER HN . 16885 1 534 . 1 1 48 48 SER HA H 1 4.255 0.020 . 1 . . . . 532 SER HA . 16885 1 535 . 1 1 48 48 SER HB2 H 1 3.844 0.020 . 2 . . . . 532 SER QB . 16885 1 536 . 1 1 48 48 SER HB3 H 1 3.844 0.020 . 2 . . . . 532 SER QB . 16885 1 537 . 1 1 48 48 SER CA C 13 59.938 0.300 . 1 . . . . 532 SER CA . 16885 1 538 . 1 1 48 48 SER CB C 13 64.842 0.300 . 1 . . . . 532 SER CB . 16885 1 539 . 1 1 48 48 SER N N 15 119.382 0.300 . 1 . . . . 532 SER N . 16885 1 540 . 2 2 1 1 MET HA H 1 4.235 0.020 . 1 . . . . 1 MET HA . 16885 1 541 . 2 2 1 1 MET HB2 H 1 2.063 0.020 . 2 . . . . 1 MET HB2 . 16885 1 542 . 2 2 1 1 MET HB3 H 1 2.109 0.020 . 2 . . . . 1 MET HB3 . 16885 1 543 . 2 2 1 1 MET HE1 H 1 1.630 0.020 . 1 . . . . 1 MET QE . 16885 1 544 . 2 2 1 1 MET HE2 H 1 1.630 0.020 . 1 . . . . 1 MET QE . 16885 1 545 . 2 2 1 1 MET HE3 H 1 1.630 0.020 . 1 . . . . 1 MET QE . 16885 1 546 . 2 2 1 1 MET HG2 H 1 1.936 0.020 . 2 . . . . 1 MET HG2 . 16885 1 547 . 2 2 1 1 MET HG3 H 1 2.567 0.020 . 2 . . . . 1 MET HG3 . 16885 1 548 . 2 2 1 1 MET CA C 13 54.339 0.300 . 1 . . . . 1 MET CA . 16885 1 549 . 2 2 1 1 MET CB C 13 32.982 0.300 . 1 . . . . 1 MET CB . 16885 1 550 . 2 2 1 1 MET CE C 13 17.747 0.300 . 1 . . . . 1 MET CE . 16885 1 551 . 2 2 1 1 MET CG C 13 30.807 0.300 . 1 . . . . 1 MET CG . 16885 1 552 . 2 2 2 2 GLN H H 1 9.068 0.020 . 1 . . . . 2 GLN HN . 16885 1 553 . 2 2 2 2 GLN HA H 1 5.286 0.020 . 1 . . . . 2 GLN HA . 16885 1 554 . 2 2 2 2 GLN HB2 H 1 1.656 0.020 . 2 . . . . 2 GLN HB2 . 16885 1 555 . 2 2 2 2 GLN HB3 H 1 1.863 0.020 . 2 . . . . 2 GLN HB3 . 16885 1 556 . 2 2 2 2 GLN HE21 H 1 6.811 0.020 . 2 . . . . 2 GLN HE21 . 16885 1 557 . 2 2 2 2 GLN HE22 H 1 7.802 0.020 . 2 . . . . 2 GLN HE22 . 16885 1 558 . 2 2 2 2 GLN HG2 H 1 1.859 0.020 . 2 . . . . 2 GLN HG2 . 16885 1 559 . 2 2 2 2 GLN HG3 H 1 2.216 0.020 . 2 . . . . 2 GLN HG3 . 16885 1 560 . 2 2 2 2 GLN CA C 13 55.030 0.300 . 1 . . . . 2 GLN CA . 16885 1 561 . 2 2 2 2 GLN CB C 13 30.685 0.300 . 1 . . . . 2 GLN CB . 16885 1 562 . 2 2 2 2 GLN CG C 13 34.623 0.300 . 1 . . . . 2 GLN CG . 16885 1 563 . 2 2 2 2 GLN N N 15 120.938 0.300 . 1 . . . . 2 GLN N . 16885 1 564 . 2 2 2 2 GLN NE2 N 15 109.945 0.300 . 1 . . . . 2 GLN NE2 . 16885 1 565 . 2 2 3 3 ILE H H 1 8.325 0.020 . 1 . . . . 3 ILE HN . 16885 1 566 . 2 2 3 3 ILE HA H 1 4.157 0.020 . 1 . . . . 3 ILE HA . 16885 1 567 . 2 2 3 3 ILE HB H 1 1.757 0.020 . 1 . . . . 3 ILE HB . 16885 1 568 . 2 2 3 3 ILE HD11 H 1 0.585 0.020 . 1 . . . . 3 ILE QD1 . 16885 1 569 . 2 2 3 3 ILE HD12 H 1 0.585 0.020 . 1 . . . . 3 ILE QD1 . 16885 1 570 . 2 2 3 3 ILE HD13 H 1 0.585 0.020 . 1 . . . . 3 ILE QD1 . 16885 1 571 . 2 2 3 3 ILE HG12 H 1 0.816 0.020 . 2 . . . . 3 ILE HG12 . 16885 1 572 . 2 2 3 3 ILE HG13 H 1 1.035 0.020 . 2 . . . . 3 ILE HG13 . 16885 1 573 . 2 2 3 3 ILE HG21 H 1 0.619 0.020 . 1 . . . . 3 ILE QG2 . 16885 1 574 . 2 2 3 3 ILE HG22 H 1 0.619 0.020 . 1 . . . . 3 ILE QG2 . 16885 1 575 . 2 2 3 3 ILE HG23 H 1 0.619 0.020 . 1 . . . . 3 ILE QG2 . 16885 1 576 . 2 2 3 3 ILE CA C 13 59.642 0.300 . 1 . . . . 3 ILE CA . 16885 1 577 . 2 2 3 3 ILE CB C 13 42.117 0.300 . 1 . . . . 3 ILE CB . 16885 1 578 . 2 2 3 3 ILE CD1 C 13 14.154 0.300 . 1 . . . . 3 ILE CD1 . 16885 1 579 . 2 2 3 3 ILE CG1 C 13 24.792 0.300 . 1 . . . . 3 ILE CG1 . 16885 1 580 . 2 2 3 3 ILE CG2 C 13 17.743 0.300 . 1 . . . . 3 ILE CG2 . 16885 1 581 . 2 2 3 3 ILE N N 15 112.667 0.300 . 1 . . . . 3 ILE N . 16885 1 582 . 2 2 4 4 PHE H H 1 8.625 0.020 . 1 . . . . 4 PHE HN . 16885 1 583 . 2 2 4 4 PHE HA H 1 5.536 0.020 . 1 . . . . 4 PHE HA . 16885 1 584 . 2 2 4 4 PHE HB2 H 1 2.863 0.020 . 2 . . . . 4 PHE HB2 . 16885 1 585 . 2 2 4 4 PHE HB3 H 1 3.048 0.020 . 2 . . . . 4 PHE HB3 . 16885 1 586 . 2 2 4 4 PHE HD1 H 1 7.072 0.020 . 3 . . . . 4 PHE QD . 16885 1 587 . 2 2 4 4 PHE HD2 H 1 7.072 0.020 . 3 . . . . 4 PHE QD . 16885 1 588 . 2 2 4 4 PHE HE1 H 1 7.244 0.020 . 3 . . . . 4 PHE QE . 16885 1 589 . 2 2 4 4 PHE HE2 H 1 7.244 0.020 . 3 . . . . 4 PHE QE . 16885 1 590 . 2 2 4 4 PHE HZ H 1 7.245 0.020 . 1 . . . . 4 PHE HZ . 16885 1 591 . 2 2 4 4 PHE CA C 13 55.125 0.300 . 1 . . . . 4 PHE CA . 16885 1 592 . 2 2 4 4 PHE CB C 13 41.087 0.300 . 1 . . . . 4 PHE CB . 16885 1 593 . 2 2 4 4 PHE CD1 C 13 132.191 0.300 . 3 . . . . 4 PHE CD1 . 16885 1 594 . 2 2 4 4 PHE CE1 C 13 131.093 0.300 . 3 . . . . 4 PHE CE1 . 16885 1 595 . 2 2 4 4 PHE CZ C 13 129.629 0.300 . 1 . . . . 4 PHE CZ . 16885 1 596 . 2 2 4 4 PHE N N 15 115.966 0.300 . 1 . . . . 4 PHE N . 16885 1 597 . 2 2 5 5 VAL H H 1 9.434 0.020 . 1 . . . . 5 VAL HN . 16885 1 598 . 2 2 5 5 VAL HA H 1 4.802 0.020 . 1 . . . . 5 VAL HA . 16885 1 599 . 2 2 5 5 VAL HB H 1 1.922 0.020 . 1 . . . . 5 VAL HB . 16885 1 600 . 2 2 5 5 VAL HG11 H 1 0.687 0.020 . 2 . . . . 5 VAL QG1 . 16885 1 601 . 2 2 5 5 VAL HG12 H 1 0.687 0.020 . 2 . . . . 5 VAL QG1 . 16885 1 602 . 2 2 5 5 VAL HG13 H 1 0.687 0.020 . 2 . . . . 5 VAL QG1 . 16885 1 603 . 2 2 5 5 VAL HG21 H 1 0.732 0.020 . 2 . . . . 5 VAL QG2 . 16885 1 604 . 2 2 5 5 VAL HG22 H 1 0.732 0.020 . 2 . . . . 5 VAL QG2 . 16885 1 605 . 2 2 5 5 VAL HG23 H 1 0.732 0.020 . 2 . . . . 5 VAL QG2 . 16885 1 606 . 2 2 5 5 VAL CA C 13 60.314 0.300 . 1 . . . . 5 VAL CA . 16885 1 607 . 2 2 5 5 VAL CB C 13 33.879 0.300 . 1 . . . . 5 VAL CB . 16885 1 608 . 2 2 5 5 VAL CG1 C 13 22.681 0.300 . 2 . . . . 5 VAL CG1 . 16885 1 609 . 2 2 5 5 VAL CG2 C 13 20.811 0.300 . 2 . . . . 5 VAL CG2 . 16885 1 610 . 2 2 5 5 VAL N N 15 119.623 0.300 . 1 . . . . 5 VAL N . 16885 1 611 . 2 2 6 6 LYS H H 1 9.136 0.020 . 1 . . . . 6 LYS HN . 16885 1 612 . 2 2 6 6 LYS HA H 1 5.686 0.020 . 1 . . . . 6 LYS HA . 16885 1 613 . 2 2 6 6 LYS HB2 H 1 1.517 0.020 . 2 . . . . 6 LYS HB2 . 16885 1 614 . 2 2 6 6 LYS HB3 H 1 1.744 0.020 . 2 . . . . 6 LYS HB3 . 16885 1 615 . 2 2 6 6 LYS HD2 H 1 1.590 0.020 . 2 . . . . 6 LYS HD2 . 16885 1 616 . 2 2 6 6 LYS HD3 H 1 1.626 0.020 . 2 . . . . 6 LYS HD3 . 16885 1 617 . 2 2 6 6 LYS HE2 H 1 2.869 0.020 . 2 . . . . 6 LYS QE . 16885 1 618 . 2 2 6 6 LYS HE3 H 1 2.869 0.020 . 2 . . . . 6 LYS QE . 16885 1 619 . 2 2 6 6 LYS HG2 H 1 1.315 0.020 . 2 . . . . 6 LYS HG2 . 16885 1 620 . 2 2 6 6 LYS HG3 H 1 1.584 0.020 . 2 . . . . 6 LYS HG3 . 16885 1 621 . 2 2 6 6 LYS CA C 13 54.051 0.300 . 1 . . . . 6 LYS CA . 16885 1 622 . 2 2 6 6 LYS CB C 13 35.684 0.300 . 1 . . . . 6 LYS CB . 16885 1 623 . 2 2 6 6 LYS CD C 13 29.615 0.300 . 1 . . . . 6 LYS CD . 16885 1 624 . 2 2 6 6 LYS CE C 13 41.887 0.300 . 1 . . . . 6 LYS CE . 16885 1 625 . 2 2 6 6 LYS CG C 13 25.351 0.300 . 1 . . . . 6 LYS CG . 16885 1 626 . 2 2 6 6 LYS N N 15 125.643 0.300 . 1 . . . . 6 LYS N . 16885 1 627 . 2 2 7 7 THR H H 1 8.848 0.020 . 1 . . . . 7 THR HN . 16885 1 628 . 2 2 7 7 THR HA H 1 5.144 0.020 . 1 . . . . 7 THR HA . 16885 1 629 . 2 2 7 7 THR HB H 1 4.954 0.020 . 1 . . . . 7 THR HB . 16885 1 630 . 2 2 7 7 THR HG21 H 1 1.241 0.020 . 1 . . . . 7 THR QG2 . 16885 1 631 . 2 2 7 7 THR HG22 H 1 1.241 0.020 . 1 . . . . 7 THR QG2 . 16885 1 632 . 2 2 7 7 THR HG23 H 1 1.241 0.020 . 1 . . . . 7 THR QG2 . 16885 1 633 . 2 2 7 7 THR CA C 13 60.130 0.300 . 1 . . . . 7 THR CA . 16885 1 634 . 2 2 7 7 THR CB C 13 70.593 0.300 . 1 . . . . 7 THR CB . 16885 1 635 . 2 2 7 7 THR CG2 C 13 21.596 0.300 . 1 . . . . 7 THR CG2 . 16885 1 636 . 2 2 7 7 THR N N 15 112.104 0.300 . 1 . . . . 7 THR N . 16885 1 637 . 2 2 8 8 LEU H H 1 8.867 0.020 . 1 . . . . 8 LEU HN . 16885 1 638 . 2 2 8 8 LEU HA H 1 4.255 0.020 . 1 . . . . 8 LEU HA . 16885 1 639 . 2 2 8 8 LEU HB2 H 1 1.844 0.020 . 2 . . . . 8 LEU HB2 . 16885 1 640 . 2 2 8 8 LEU HB3 H 1 1.960 0.020 . 2 . . . . 8 LEU HB3 . 16885 1 641 . 2 2 8 8 LEU HD11 H 1 1.034 0.020 . 2 . . . . 8 LEU QD1 . 16885 1 642 . 2 2 8 8 LEU HD12 H 1 1.034 0.020 . 2 . . . . 8 LEU QD1 . 16885 1 643 . 2 2 8 8 LEU HD13 H 1 1.034 0.020 . 2 . . . . 8 LEU QD1 . 16885 1 644 . 2 2 8 8 LEU HD21 H 1 1.109 0.020 . 2 . . . . 8 LEU QD2 . 16885 1 645 . 2 2 8 8 LEU HD22 H 1 1.109 0.020 . 2 . . . . 8 LEU QD2 . 16885 1 646 . 2 2 8 8 LEU HD23 H 1 1.109 0.020 . 2 . . . . 8 LEU QD2 . 16885 1 647 . 2 2 8 8 LEU HG H 1 2.048 0.020 . 1 . . . . 8 LEU HG . 16885 1 648 . 2 2 8 8 LEU CA C 13 57.248 0.300 . 1 . . . . 8 LEU CA . 16885 1 649 . 2 2 8 8 LEU CB C 13 43.054 0.300 . 1 . . . . 8 LEU CB . 16885 1 650 . 2 2 8 8 LEU CD1 C 13 25.375 0.300 . 2 . . . . 8 LEU CD1 . 16885 1 651 . 2 2 8 8 LEU CD2 C 13 25.375 0.300 . 2 . . . . 8 LEU CD2 . 16885 1 652 . 2 2 8 8 LEU CG C 13 27.274 0.300 . 1 . . . . 8 LEU CG . 16885 1 653 . 2 2 8 8 LEU N N 15 116.648 0.300 . 1 . . . . 8 LEU N . 16885 1 654 . 2 2 9 9 THR H H 1 7.562 0.020 . 1 . . . . 9 THR HN . 16885 1 655 . 2 2 9 9 THR HA H 1 4.648 0.020 . 1 . . . . 9 THR HA . 16885 1 656 . 2 2 9 9 THR HB H 1 4.622 0.020 . 1 . . . . 9 THR HB . 16885 1 657 . 2 2 9 9 THR HG21 H 1 1.250 0.020 . 1 . . . . 9 THR QG2 . 16885 1 658 . 2 2 9 9 THR HG22 H 1 1.250 0.020 . 1 . . . . 9 THR QG2 . 16885 1 659 . 2 2 9 9 THR HG23 H 1 1.250 0.020 . 1 . . . . 9 THR QG2 . 16885 1 660 . 2 2 9 9 THR CA C 13 61.029 0.300 . 1 . . . . 9 THR CA . 16885 1 661 . 2 2 9 9 THR CB C 13 69.213 0.300 . 1 . . . . 9 THR CB . 16885 1 662 . 2 2 9 9 THR CG2 C 13 21.785 0.300 . 1 . . . . 9 THR CG2 . 16885 1 663 . 2 2 9 9 THR N N 15 100.712 0.300 . 1 . . . . 9 THR N . 16885 1 664 . 2 2 10 10 GLY H H 1 8.235 0.020 . 1 . . . . 10 GLY HN . 16885 1 665 . 2 2 10 10 GLY HA2 H 1 3.528 0.020 . 2 . . . . 10 GLY HA1 . 16885 1 666 . 2 2 10 10 GLY HA3 H 1 4.474 0.020 . 2 . . . . 10 GLY HA2 . 16885 1 667 . 2 2 10 10 GLY CA C 13 45.331 0.300 . 1 . . . . 10 GLY CA . 16885 1 668 . 2 2 10 10 GLY N N 15 107.365 0.300 . 1 . . . . 10 GLY N . 16885 1 669 . 2 2 11 11 LYS H H 1 7.383 0.020 . 1 . . . . 11 LYS HN . 16885 1 670 . 2 2 11 11 LYS HA H 1 4.287 0.020 . 1 . . . . 11 LYS HA . 16885 1 671 . 2 2 11 11 LYS HB2 H 1 1.722 0.020 . 2 . . . . 11 LYS HB2 . 16885 1 672 . 2 2 11 11 LYS HB3 H 1 1.898 0.020 . 2 . . . . 11 LYS HB3 . 16885 1 673 . 2 2 11 11 LYS HD2 H 1 1.602 0.020 . 2 . . . . 11 LYS HD2 . 16885 1 674 . 2 2 11 11 LYS HD3 H 1 1.673 0.020 . 2 . . . . 11 LYS HD3 . 16885 1 675 . 2 2 11 11 LYS HE2 H 1 2.921 0.020 . 2 . . . . 11 LYS QE . 16885 1 676 . 2 2 11 11 LYS HE3 H 1 2.921 0.020 . 2 . . . . 11 LYS QE . 16885 1 677 . 2 2 11 11 LYS HG2 H 1 1.219 0.020 . 2 . . . . 11 LYS HG2 . 16885 1 678 . 2 2 11 11 LYS HG3 H 1 1.468 0.020 . 2 . . . . 11 LYS HG3 . 16885 1 679 . 2 2 11 11 LYS CA C 13 56.731 0.300 . 1 . . . . 11 LYS CA . 16885 1 680 . 2 2 11 11 LYS CB C 13 33.024 0.300 . 1 . . . . 11 LYS CB . 16885 1 681 . 2 2 11 11 LYS CD C 13 29.596 0.300 . 1 . . . . 11 LYS CD . 16885 1 682 . 2 2 11 11 LYS CE C 13 41.960 0.300 . 1 . . . . 11 LYS CE . 16885 1 683 . 2 2 11 11 LYS CG C 13 25.270 0.300 . 1 . . . . 11 LYS CG . 16885 1 684 . 2 2 11 11 LYS N N 15 120.786 0.300 . 1 . . . . 11 LYS N . 16885 1 685 . 2 2 12 12 THR H H 1 8.726 0.020 . 1 . . . . 12 THR HN . 16885 1 686 . 2 2 12 12 THR HA H 1 5.059 0.020 . 1 . . . . 12 THR HA . 16885 1 687 . 2 2 12 12 THR HB H 1 3.963 0.020 . 1 . . . . 12 THR HB . 16885 1 688 . 2 2 12 12 THR HG21 H 1 1.106 0.020 . 1 . . . . 12 THR QG2 . 16885 1 689 . 2 2 12 12 THR HG22 H 1 1.106 0.020 . 1 . . . . 12 THR QG2 . 16885 1 690 . 2 2 12 12 THR HG23 H 1 1.106 0.020 . 1 . . . . 12 THR QG2 . 16885 1 691 . 2 2 12 12 THR CA C 13 62.540 0.300 . 1 . . . . 12 THR CA . 16885 1 692 . 2 2 12 12 THR CB C 13 69.832 0.300 . 1 . . . . 12 THR CB . 16885 1 693 . 2 2 12 12 THR CG2 C 13 21.824 0.300 . 1 . . . . 12 THR CG2 . 16885 1 694 . 2 2 12 12 THR N N 15 118.634 0.300 . 1 . . . . 12 THR N . 16885 1 695 . 2 2 13 13 ILE H H 1 9.820 0.020 . 1 . . . . 13 ILE HN . 16885 1 696 . 2 2 13 13 ILE HA H 1 4.449 0.020 . 1 . . . . 13 ILE HA . 16885 1 697 . 2 2 13 13 ILE HB H 1 1.869 0.020 . 1 . . . . 13 ILE HB . 16885 1 698 . 2 2 13 13 ILE HD11 H 1 0.706 0.020 . 1 . . . . 13 ILE QD1 . 16885 1 699 . 2 2 13 13 ILE HD12 H 1 0.706 0.020 . 1 . . . . 13 ILE QD1 . 16885 1 700 . 2 2 13 13 ILE HD13 H 1 0.706 0.020 . 1 . . . . 13 ILE QD1 . 16885 1 701 . 2 2 13 13 ILE HG12 H 1 1.063 0.020 . 2 . . . . 13 ILE HG12 . 16885 1 702 . 2 2 13 13 ILE HG13 H 1 1.468 0.020 . 2 . . . . 13 ILE HG13 . 16885 1 703 . 2 2 13 13 ILE HG21 H 1 0.878 0.020 . 1 . . . . 13 ILE QG2 . 16885 1 704 . 2 2 13 13 ILE HG22 H 1 0.878 0.020 . 1 . . . . 13 ILE QG2 . 16885 1 705 . 2 2 13 13 ILE HG23 H 1 0.878 0.020 . 1 . . . . 13 ILE QG2 . 16885 1 706 . 2 2 13 13 ILE CA C 13 60.122 0.300 . 1 . . . . 13 ILE CA . 16885 1 707 . 2 2 13 13 ILE CB C 13 40.998 0.300 . 1 . . . . 13 ILE CB . 16885 1 708 . 2 2 13 13 ILE CD1 C 13 14.562 0.300 . 1 . . . . 13 ILE CD1 . 16885 1 709 . 2 2 13 13 ILE CG1 C 13 27.032 0.300 . 1 . . . . 13 ILE CG1 . 16885 1 710 . 2 2 13 13 ILE CG2 C 13 17.575 0.300 . 1 . . . . 13 ILE CG2 . 16885 1 711 . 2 2 13 13 ILE N N 15 127.422 0.300 . 1 . . . . 13 ILE N . 16885 1 712 . 2 2 14 14 THR H H 1 8.869 0.020 . 1 . . . . 14 THR HN . 16885 1 713 . 2 2 14 14 THR HA H 1 4.947 0.020 . 1 . . . . 14 THR HA . 16885 1 714 . 2 2 14 14 THR HB H 1 4.046 0.020 . 1 . . . . 14 THR HB . 16885 1 715 . 2 2 14 14 THR HG21 H 1 1.152 0.020 . 1 . . . . 14 THR QG2 . 16885 1 716 . 2 2 14 14 THR HG22 H 1 1.152 0.020 . 1 . . . . 14 THR QG2 . 16885 1 717 . 2 2 14 14 THR HG23 H 1 1.152 0.020 . 1 . . . . 14 THR QG2 . 16885 1 718 . 2 2 14 14 THR CA C 13 62.186 0.300 . 1 . . . . 14 THR CA . 16885 1 719 . 2 2 14 14 THR CB C 13 69.487 0.300 . 1 . . . . 14 THR CB . 16885 1 720 . 2 2 14 14 THR CG2 C 13 21.696 0.300 . 1 . . . . 14 THR CG2 . 16885 1 721 . 2 2 14 14 THR N N 15 120.257 0.300 . 1 . . . . 14 THR N . 16885 1 722 . 2 2 15 15 LEU H H 1 8.697 0.020 . 1 . . . . 15 LEU HN . 16885 1 723 . 2 2 15 15 LEU HA H 1 4.790 0.020 . 1 . . . . 15 LEU HA . 16885 1 724 . 2 2 15 15 LEU HB2 H 1 1.217 0.020 . 2 . . . . 15 LEU HB2 . 16885 1 725 . 2 2 15 15 LEU HB3 H 1 1.349 0.020 . 2 . . . . 15 LEU HB3 . 16885 1 726 . 2 2 15 15 LEU HD11 H 1 0.707 0.020 . 2 . . . . 15 LEU QD1 . 16885 1 727 . 2 2 15 15 LEU HD12 H 1 0.707 0.020 . 2 . . . . 15 LEU QD1 . 16885 1 728 . 2 2 15 15 LEU HD13 H 1 0.707 0.020 . 2 . . . . 15 LEU QD1 . 16885 1 729 . 2 2 15 15 LEU HD21 H 1 0.761 0.020 . 2 . . . . 15 LEU QD2 . 16885 1 730 . 2 2 15 15 LEU HD22 H 1 0.761 0.020 . 2 . . . . 15 LEU QD2 . 16885 1 731 . 2 2 15 15 LEU HD23 H 1 0.761 0.020 . 2 . . . . 15 LEU QD2 . 16885 1 732 . 2 2 15 15 LEU HG H 1 1.412 0.020 . 1 . . . . 15 LEU HG . 16885 1 733 . 2 2 15 15 LEU CA C 13 52.697 0.300 . 1 . . . . 15 LEU CA . 16885 1 734 . 2 2 15 15 LEU CB C 13 47.196 0.300 . 1 . . . . 15 LEU CB . 16885 1 735 . 2 2 15 15 LEU CD1 C 13 27.171 0.300 . 2 . . . . 15 LEU CD1 . 16885 1 736 . 2 2 15 15 LEU CD2 C 13 24.008 0.300 . 2 . . . . 15 LEU CD2 . 16885 1 737 . 2 2 15 15 LEU CG C 13 26.676 0.300 . 1 . . . . 15 LEU CG . 16885 1 738 . 2 2 15 15 LEU N N 15 122.545 0.300 . 1 . . . . 15 LEU N . 16885 1 739 . 2 2 16 16 GLU H H 1 8.164 0.020 . 1 . . . . 16 GLU HN . 16885 1 740 . 2 2 16 16 GLU HA H 1 4.876 0.020 . 1 . . . . 16 GLU HA . 16885 1 741 . 2 2 16 16 GLU HB2 H 1 1.827 0.020 . 2 . . . . 16 GLU HB2 . 16885 1 742 . 2 2 16 16 GLU HB3 H 1 1.916 0.020 . 2 . . . . 16 GLU HB3 . 16885 1 743 . 2 2 16 16 GLU HG2 H 1 2.089 0.020 . 2 . . . . 16 GLU HG2 . 16885 1 744 . 2 2 16 16 GLU HG3 H 1 2.252 0.020 . 2 . . . . 16 GLU HG3 . 16885 1 745 . 2 2 16 16 GLU CA C 13 54.780 0.300 . 1 . . . . 16 GLU CA . 16885 1 746 . 2 2 16 16 GLU CB C 13 29.816 0.300 . 1 . . . . 16 GLU CB . 16885 1 747 . 2 2 16 16 GLU CG C 13 35.404 0.300 . 1 . . . . 16 GLU CG . 16885 1 748 . 2 2 16 16 GLU N N 15 120.123 0.300 . 1 . . . . 16 GLU N . 16885 1 749 . 2 2 17 17 VAL H H 1 9.014 0.020 . 1 . . . . 17 VAL HN . 16885 1 750 . 2 2 17 17 VAL HA H 1 4.687 0.020 . 1 . . . . 17 VAL HA . 16885 1 751 . 2 2 17 17 VAL HB H 1 2.337 0.020 . 1 . . . . 17 VAL HB . 16885 1 752 . 2 2 17 17 VAL HG11 H 1 0.417 0.020 . 2 . . . . 17 VAL QG1 . 16885 1 753 . 2 2 17 17 VAL HG12 H 1 0.417 0.020 . 2 . . . . 17 VAL QG1 . 16885 1 754 . 2 2 17 17 VAL HG13 H 1 0.417 0.020 . 2 . . . . 17 VAL QG1 . 16885 1 755 . 2 2 17 17 VAL HG21 H 1 0.706 0.020 . 2 . . . . 17 VAL QG2 . 16885 1 756 . 2 2 17 17 VAL HG22 H 1 0.706 0.020 . 2 . . . . 17 VAL QG2 . 16885 1 757 . 2 2 17 17 VAL HG23 H 1 0.706 0.020 . 2 . . . . 17 VAL QG2 . 16885 1 758 . 2 2 17 17 VAL CA C 13 58.392 0.300 . 1 . . . . 17 VAL CA . 16885 1 759 . 2 2 17 17 VAL CB C 13 36.402 0.300 . 1 . . . . 17 VAL CB . 16885 1 760 . 2 2 17 17 VAL CG1 C 13 19.624 0.300 . 2 . . . . 17 VAL CG1 . 16885 1 761 . 2 2 17 17 VAL CG2 C 13 22.072 0.300 . 2 . . . . 17 VAL CG2 . 16885 1 762 . 2 2 17 17 VAL N N 15 115.121 0.300 . 1 . . . . 17 VAL N . 16885 1 763 . 2 2 18 18 GLU H H 1 8.687 0.020 . 1 . . . . 18 GLU HN . 16885 1 764 . 2 2 18 18 GLU HA H 1 5.088 0.020 . 1 . . . . 18 GLU HA . 16885 1 765 . 2 2 18 18 GLU HB2 H 1 1.582 0.020 . 2 . . . . 18 GLU HB2 . 16885 1 766 . 2 2 18 18 GLU HB3 H 1 2.145 0.020 . 2 . . . . 18 GLU HB3 . 16885 1 767 . 2 2 18 18 GLU HG2 H 1 2.223 0.020 . 2 . . . . 18 GLU HG2 . 16885 1 768 . 2 2 18 18 GLU HG3 H 1 2.346 0.020 . 2 . . . . 18 GLU HG3 . 16885 1 769 . 2 2 18 18 GLU CA C 13 52.635 0.300 . 1 . . . . 18 GLU CA . 16885 1 770 . 2 2 18 18 GLU CB C 13 30.811 0.300 . 1 . . . . 18 GLU CB . 16885 1 771 . 2 2 18 18 GLU CG C 13 35.005 0.300 . 1 . . . . 18 GLU CG . 16885 1 772 . 2 2 18 18 GLU N N 15 116.728 0.300 . 1 . . . . 18 GLU N . 16885 1 773 . 2 2 19 19 PRO HA H 1 4.118 0.020 . 1 . . . . 19 PRO HA . 16885 1 774 . 2 2 19 19 PRO HB2 H 1 2.009 0.020 . 2 . . . . 19 PRO HB2 . 16885 1 775 . 2 2 19 19 PRO HB3 H 1 2.444 0.020 . 2 . . . . 19 PRO HB3 . 16885 1 776 . 2 2 19 19 PRO HD2 H 1 3.814 0.020 . 2 . . . . 19 PRO HD2 . 16885 1 777 . 2 2 19 19 PRO HD3 H 1 4.006 0.020 . 2 . . . . 19 PRO HD3 . 16885 1 778 . 2 2 19 19 PRO HG2 H 1 2.065 0.020 . 2 . . . . 19 PRO HG2 . 16885 1 779 . 2 2 19 19 PRO HG3 H 1 2.213 0.020 . 2 . . . . 19 PRO HG3 . 16885 1 780 . 2 2 19 19 PRO CA C 13 65.235 0.300 . 1 . . . . 19 PRO CA . 16885 1 781 . 2 2 19 19 PRO CB C 13 31.843 0.300 . 1 . . . . 19 PRO CB . 16885 1 782 . 2 2 19 19 PRO CD C 13 50.398 0.300 . 1 . . . . 19 PRO CD . 16885 1 783 . 2 2 19 19 PRO CG C 13 28.021 0.300 . 1 . . . . 19 PRO CG . 16885 1 784 . 2 2 20 20 SER H H 1 7.074 0.020 . 1 . . . . 20 SER HN . 16885 1 785 . 2 2 20 20 SER HA H 1 4.356 0.020 . 1 . . . . 20 SER HA . 16885 1 786 . 2 2 20 20 SER HB2 H 1 3.785 0.020 . 2 . . . . 20 SER HB2 . 16885 1 787 . 2 2 20 20 SER HB3 H 1 4.157 0.020 . 2 . . . . 20 SER HB3 . 16885 1 788 . 2 2 20 20 SER CA C 13 57.344 0.300 . 1 . . . . 20 SER CA . 16885 1 789 . 2 2 20 20 SER CB C 13 63.369 0.300 . 1 . . . . 20 SER CB . 16885 1 790 . 2 2 20 20 SER N N 15 100.949 0.300 . 1 . . . . 20 SER N . 16885 1 791 . 2 2 21 21 ASP H H 1 8.118 0.020 . 1 . . . . 21 ASP HN . 16885 1 792 . 2 2 21 21 ASP HA H 1 4.679 0.020 . 1 . . . . 21 ASP HA . 16885 1 793 . 2 2 21 21 ASP HB2 H 1 2.519 0.020 . 2 . . . . 21 ASP HB2 . 16885 1 794 . 2 2 21 21 ASP HB3 H 1 2.944 0.020 . 2 . . . . 21 ASP HB3 . 16885 1 795 . 2 2 21 21 ASP CA C 13 55.812 0.300 . 1 . . . . 21 ASP CA . 16885 1 796 . 2 2 21 21 ASP CB C 13 40.816 0.300 . 1 . . . . 21 ASP CB . 16885 1 797 . 2 2 21 21 ASP N N 15 121.704 0.300 . 1 . . . . 21 ASP N . 16885 1 798 . 2 2 22 22 THR H H 1 7.946 0.020 . 1 . . . . 22 THR HN . 16885 1 799 . 2 2 22 22 THR HA H 1 4.888 0.020 . 1 . . . . 22 THR HA . 16885 1 800 . 2 2 22 22 THR HB H 1 4.832 0.020 . 1 . . . . 22 THR HB . 16885 1 801 . 2 2 22 22 THR HG21 H 1 1.255 0.020 . 1 . . . . 22 THR QG2 . 16885 1 802 . 2 2 22 22 THR HG22 H 1 1.255 0.020 . 1 . . . . 22 THR QG2 . 16885 1 803 . 2 2 22 22 THR HG23 H 1 1.255 0.020 . 1 . . . . 22 THR QG2 . 16885 1 804 . 2 2 22 22 THR CA C 13 59.553 0.300 . 1 . . . . 22 THR CA . 16885 1 805 . 2 2 22 22 THR CB C 13 71.145 0.300 . 1 . . . . 22 THR CB . 16885 1 806 . 2 2 22 22 THR CG2 C 13 22.129 0.300 . 1 . . . . 22 THR CG2 . 16885 1 807 . 2 2 22 22 THR N N 15 106.661 0.300 . 1 . . . . 22 THR N . 16885 1 808 . 2 2 23 23 ILE H H 1 8.600 0.020 . 1 . . . . 23 ILE HN . 16885 1 809 . 2 2 23 23 ILE HA H 1 3.657 0.020 . 1 . . . . 23 ILE HA . 16885 1 810 . 2 2 23 23 ILE HB H 1 2.620 0.020 . 1 . . . . 23 ILE HB . 16885 1 811 . 2 2 23 23 ILE HD11 H 1 0.572 0.020 . 1 . . . . 23 ILE QD1 . 16885 1 812 . 2 2 23 23 ILE HD12 H 1 0.572 0.020 . 1 . . . . 23 ILE QD1 . 16885 1 813 . 2 2 23 23 ILE HD13 H 1 0.572 0.020 . 1 . . . . 23 ILE QD1 . 16885 1 814 . 2 2 23 23 ILE HG12 H 1 1.319 0.020 . 2 . . . . 23 ILE HG12 . 16885 1 815 . 2 2 23 23 ILE HG13 H 1 1.939 0.020 . 2 . . . . 23 ILE HG13 . 16885 1 816 . 2 2 23 23 ILE HG21 H 1 0.797 0.020 . 1 . . . . 23 ILE QG2 . 16885 1 817 . 2 2 23 23 ILE HG22 H 1 0.797 0.020 . 1 . . . . 23 ILE QG2 . 16885 1 818 . 2 2 23 23 ILE HG23 H 1 0.797 0.020 . 1 . . . . 23 ILE QG2 . 16885 1 819 . 2 2 23 23 ILE CA C 13 62.219 0.300 . 1 . . . . 23 ILE CA . 16885 1 820 . 2 2 23 23 ILE CB C 13 34.289 0.300 . 1 . . . . 23 ILE CB . 16885 1 821 . 2 2 23 23 ILE CD1 C 13 9.315 0.300 . 1 . . . . 23 ILE CD1 . 16885 1 822 . 2 2 23 23 ILE CG1 C 13 27.741 0.300 . 1 . . . . 23 ILE CG1 . 16885 1 823 . 2 2 23 23 ILE CG2 C 13 18.055 0.300 . 1 . . . . 23 ILE CG2 . 16885 1 824 . 2 2 23 23 ILE N N 15 119.334 0.300 . 1 . . . . 23 ILE N . 16885 1 825 . 2 2 24 24 GLU H H 1 9.841 0.020 . 1 . . . . 24 GLU HN . 16885 1 826 . 2 2 24 24 GLU HA H 1 3.875 0.020 . 1 . . . . 24 GLU HA . 16885 1 827 . 2 2 24 24 GLU HB2 H 1 2.038 0.020 . 2 . . . . 24 GLU QB . 16885 1 828 . 2 2 24 24 GLU HB3 H 1 2.038 0.020 . 2 . . . . 24 GLU QB . 16885 1 829 . 2 2 24 24 GLU HG2 H 1 2.302 0.020 . 2 . . . . 24 GLU HG2 . 16885 1 830 . 2 2 24 24 GLU HG3 H 1 2.343 0.020 . 2 . . . . 24 GLU HG3 . 16885 1 831 . 2 2 24 24 GLU CA C 13 60.403 0.300 . 1 . . . . 24 GLU CA . 16885 1 832 . 2 2 24 24 GLU CB C 13 28.928 0.300 . 1 . . . . 24 GLU CB . 16885 1 833 . 2 2 24 24 GLU CG C 13 35.879 0.300 . 1 . . . . 24 GLU CG . 16885 1 834 . 2 2 25 25 ASN H H 1 8.003 0.020 . 1 . . . . 25 ASN HN . 16885 1 835 . 2 2 25 25 ASN HA H 1 4.549 0.020 . 1 . . . . 25 ASN HA . 16885 1 836 . 2 2 25 25 ASN HB2 H 1 2.853 0.020 . 2 . . . . 25 ASN HB2 . 16885 1 837 . 2 2 25 25 ASN HB3 H 1 3.249 0.020 . 2 . . . . 25 ASN HB3 . 16885 1 838 . 2 2 25 25 ASN HD21 H 1 6.971 0.020 . 2 . . . . 25 ASN HD21 . 16885 1 839 . 2 2 25 25 ASN HD22 H 1 7.897 0.020 . 2 . . . . 25 ASN HD22 . 16885 1 840 . 2 2 25 25 ASN CA C 13 55.924 0.300 . 1 . . . . 25 ASN CA . 16885 1 841 . 2 2 25 25 ASN CB C 13 38.319 0.300 . 1 . . . . 25 ASN CB . 16885 1 842 . 2 2 25 25 ASN N N 15 118.742 0.300 . 1 . . . . 25 ASN N . 16885 1 843 . 2 2 25 25 ASN ND2 N 15 107.499 0.300 . 1 . . . . 25 ASN ND2 . 16885 1 844 . 2 2 26 26 VAL H H 1 8.221 0.020 . 1 . . . . 26 VAL HN . 16885 1 845 . 2 2 26 26 VAL HA H 1 3.390 0.020 . 1 . . . . 26 VAL HA . 16885 1 846 . 2 2 26 26 VAL HB H 1 2.330 0.020 . 1 . . . . 26 VAL HB . 16885 1 847 . 2 2 26 26 VAL HG11 H 1 0.699 0.020 . 2 . . . . 26 VAL QG1 . 16885 1 848 . 2 2 26 26 VAL HG12 H 1 0.699 0.020 . 2 . . . . 26 VAL QG1 . 16885 1 849 . 2 2 26 26 VAL HG13 H 1 0.699 0.020 . 2 . . . . 26 VAL QG1 . 16885 1 850 . 2 2 26 26 VAL HG21 H 1 0.987 0.020 . 2 . . . . 26 VAL QG2 . 16885 1 851 . 2 2 26 26 VAL HG22 H 1 0.987 0.020 . 2 . . . . 26 VAL QG2 . 16885 1 852 . 2 2 26 26 VAL HG23 H 1 0.987 0.020 . 2 . . . . 26 VAL QG2 . 16885 1 853 . 2 2 26 26 VAL CA C 13 67.663 0.300 . 1 . . . . 26 VAL CA . 16885 1 854 . 2 2 26 26 VAL CB C 13 30.661 0.300 . 1 . . . . 26 VAL CB . 16885 1 855 . 2 2 26 26 VAL CG1 C 13 21.634 0.300 . 2 . . . . 26 VAL CG1 . 16885 1 856 . 2 2 26 26 VAL CG2 C 13 23.569 0.300 . 2 . . . . 26 VAL CG2 . 16885 1 857 . 2 2 26 26 VAL N N 15 119.945 0.300 . 1 . . . . 26 VAL N . 16885 1 858 . 2 2 27 27 LYS H H 1 8.562 0.020 . 1 . . . . 27 LYS HN . 16885 1 859 . 2 2 27 27 LYS HA H 1 4.596 0.020 . 1 . . . . 27 LYS HA . 16885 1 860 . 2 2 27 27 LYS HB2 H 1 1.449 0.020 . 2 . . . . 27 LYS HB2 . 16885 1 861 . 2 2 27 27 LYS HB3 H 1 2.008 0.020 . 2 . . . . 27 LYS HB3 . 16885 1 862 . 2 2 27 27 LYS HD2 H 1 1.630 0.020 . 2 . . . . 27 LYS HD2 . 16885 1 863 . 2 2 27 27 LYS HD3 H 1 1.745 0.020 . 2 . . . . 27 LYS HD3 . 16885 1 864 . 2 2 27 27 LYS HE2 H 1 2.565 0.020 . 2 . . . . 27 LYS HE2 . 16885 1 865 . 2 2 27 27 LYS HE3 H 1 2.643 0.020 . 2 . . . . 27 LYS HE3 . 16885 1 866 . 2 2 27 27 LYS HG2 H 1 1.380 0.020 . 2 . . . . 27 LYS HG2 . 16885 1 867 . 2 2 27 27 LYS HG3 H 1 1.558 0.020 . 2 . . . . 27 LYS HG3 . 16885 1 868 . 2 2 27 27 LYS CA C 13 59.178 0.300 . 1 . . . . 27 LYS CA . 16885 1 869 . 2 2 27 27 LYS CB C 13 33.537 0.300 . 1 . . . . 27 LYS CB . 16885 1 870 . 2 2 27 27 LYS CD C 13 30.205 0.300 . 1 . . . . 27 LYS CD . 16885 1 871 . 2 2 27 27 LYS CE C 13 42.482 0.300 . 1 . . . . 27 LYS CE . 16885 1 872 . 2 2 27 27 LYS CG C 13 26.284 0.300 . 1 . . . . 27 LYS CG . 16885 1 873 . 2 2 27 27 LYS N N 15 116.853 0.300 . 1 . . . . 27 LYS N . 16885 1 874 . 2 2 28 28 ALA H H 1 8.021 0.020 . 1 . . . . 28 ALA HN . 16885 1 875 . 2 2 28 28 ALA HA H 1 4.157 0.020 . 1 . . . . 28 ALA HA . 16885 1 876 . 2 2 28 28 ALA HB1 H 1 1.636 0.020 . 1 . . . . 28 ALA QB . 16885 1 877 . 2 2 28 28 ALA HB2 H 1 1.636 0.020 . 1 . . . . 28 ALA QB . 16885 1 878 . 2 2 28 28 ALA HB3 H 1 1.636 0.020 . 1 . . . . 28 ALA QB . 16885 1 879 . 2 2 28 28 ALA CA C 13 55.268 0.300 . 1 . . . . 28 ALA CA . 16885 1 880 . 2 2 28 28 ALA CB C 13 17.673 0.300 . 1 . . . . 28 ALA CB . 16885 1 881 . 2 2 28 28 ALA N N 15 121.175 0.300 . 1 . . . . 28 ALA N . 16885 1 882 . 2 2 29 29 LYS H H 1 7.980 0.020 . 1 . . . . 29 LYS HN . 16885 1 883 . 2 2 29 29 LYS HA H 1 4.205 0.020 . 1 . . . . 29 LYS HA . 16885 1 884 . 2 2 29 29 LYS HB2 H 1 1.959 0.020 . 2 . . . . 29 LYS HB2 . 16885 1 885 . 2 2 29 29 LYS HB3 H 1 2.155 0.020 . 2 . . . . 29 LYS HB3 . 16885 1 886 . 2 2 29 29 LYS HD2 H 1 1.445 0.020 . 2 . . . . 29 LYS HD2 . 16885 1 887 . 2 2 29 29 LYS HD3 H 1 1.807 0.020 . 2 . . . . 29 LYS HD3 . 16885 1 888 . 2 2 29 29 LYS HE2 H 1 2.972 0.020 . 2 . . . . 29 LYS HE2 . 16885 1 889 . 2 2 29 29 LYS HE3 H 1 3.202 0.020 . 2 . . . . 29 LYS HE3 . 16885 1 890 . 2 2 29 29 LYS HG2 H 1 1.609 0.020 . 2 . . . . 29 LYS HG2 . 16885 1 891 . 2 2 29 29 LYS HG3 H 1 1.792 0.020 . 2 . . . . 29 LYS HG3 . 16885 1 892 . 2 2 29 29 LYS CA C 13 59.753 0.300 . 1 . . . . 29 LYS CA . 16885 1 893 . 2 2 29 29 LYS CB C 13 33.263 0.300 . 1 . . . . 29 LYS CB . 16885 1 894 . 2 2 29 29 LYS CD C 13 30.279 0.300 . 1 . . . . 29 LYS CD . 16885 1 895 . 2 2 29 29 LYS CE C 13 42.404 0.300 . 1 . . . . 29 LYS CE . 16885 1 896 . 2 2 29 29 LYS CG C 13 26.482 0.300 . 1 . . . . 29 LYS CG . 16885 1 897 . 2 2 29 29 LYS N N 15 118.321 0.300 . 1 . . . . 29 LYS N . 16885 1 898 . 2 2 30 30 ILE H H 1 8.353 0.020 . 1 . . . . 30 ILE HN . 16885 1 899 . 2 2 30 30 ILE HA H 1 3.519 0.020 . 1 . . . . 30 ILE HA . 16885 1 900 . 2 2 30 30 ILE HB H 1 2.373 0.020 . 1 . . . . 30 ILE HB . 16885 1 901 . 2 2 30 30 ILE HD11 H 1 0.905 0.020 . 1 . . . . 30 ILE QD1 . 16885 1 902 . 2 2 30 30 ILE HD12 H 1 0.905 0.020 . 1 . . . . 30 ILE QD1 . 16885 1 903 . 2 2 30 30 ILE HD13 H 1 0.905 0.020 . 1 . . . . 30 ILE QD1 . 16885 1 904 . 2 2 30 30 ILE HG12 H 1 0.690 0.020 . 2 . . . . 30 ILE HG12 . 16885 1 905 . 2 2 30 30 ILE HG13 H 1 2.023 0.020 . 2 . . . . 30 ILE HG13 . 16885 1 906 . 2 2 30 30 ILE HG21 H 1 0.700 0.020 . 1 . . . . 30 ILE QG2 . 16885 1 907 . 2 2 30 30 ILE HG22 H 1 0.700 0.020 . 1 . . . . 30 ILE QG2 . 16885 1 908 . 2 2 30 30 ILE HG23 H 1 0.700 0.020 . 1 . . . . 30 ILE QG2 . 16885 1 909 . 2 2 30 30 ILE CA C 13 66.056 0.300 . 1 . . . . 30 ILE CA . 16885 1 910 . 2 2 30 30 ILE CB C 13 36.720 0.300 . 1 . . . . 30 ILE CB . 16885 1 911 . 2 2 30 30 ILE CD1 C 13 15.066 0.300 . 1 . . . . 30 ILE CD1 . 16885 1 912 . 2 2 30 30 ILE CG1 C 13 31.289 0.300 . 1 . . . . 30 ILE CG1 . 16885 1 913 . 2 2 30 30 ILE CG2 C 13 17.010 0.300 . 1 . . . . 30 ILE CG2 . 16885 1 914 . 2 2 30 30 ILE N N 15 119.416 0.300 . 1 . . . . 30 ILE N . 16885 1 915 . 2 2 31 31 GLN H H 1 8.546 0.020 . 1 . . . . 31 GLN HN . 16885 1 916 . 2 2 31 31 GLN HA H 1 3.840 0.020 . 1 . . . . 31 GLN HA . 16885 1 917 . 2 2 31 31 GLN HB2 H 1 2.005 0.020 . 2 . . . . 31 GLN HB2 . 16885 1 918 . 2 2 31 31 GLN HB3 H 1 2.527 0.020 . 2 . . . . 31 GLN HB3 . 16885 1 919 . 2 2 31 31 GLN HE21 H 1 6.900 0.020 . 2 . . . . 31 GLN HE21 . 16885 1 920 . 2 2 31 31 GLN HE22 H 1 7.760 0.020 . 2 . . . . 31 GLN HE22 . 16885 1 921 . 2 2 31 31 GLN HG2 H 1 1.920 0.020 . 2 . . . . 31 GLN HG2 . 16885 1 922 . 2 2 31 31 GLN HG3 H 1 2.280 0.020 . 2 . . . . 31 GLN HG3 . 16885 1 923 . 2 2 31 31 GLN CA C 13 60.066 0.300 . 1 . . . . 31 GLN CA . 16885 1 924 . 2 2 31 31 GLN CB C 13 27.633 0.300 . 1 . . . . 31 GLN CB . 16885 1 925 . 2 2 31 31 GLN CG C 13 33.782 0.300 . 1 . . . . 31 GLN CG . 16885 1 926 . 2 2 31 31 GLN N N 15 121.410 0.300 . 1 . . . . 31 GLN N . 16885 1 927 . 2 2 31 31 GLN NE2 N 15 108.148 0.300 . 1 . . . . 31 GLN NE2 . 16885 1 928 . 2 2 32 32 ASP H H 1 8.159 0.020 . 1 . . . . 32 ASP HN . 16885 1 929 . 2 2 32 32 ASP HA H 1 4.327 0.020 . 1 . . . . 32 ASP HA . 16885 1 930 . 2 2 32 32 ASP HB2 H 1 2.755 0.020 . 2 . . . . 32 ASP HB2 . 16885 1 931 . 2 2 32 32 ASP HB3 H 1 2.848 0.020 . 2 . . . . 32 ASP HB3 . 16885 1 932 . 2 2 32 32 ASP CA C 13 57.397 0.300 . 1 . . . . 32 ASP CA . 16885 1 933 . 2 2 32 32 ASP CB C 13 40.904 0.300 . 1 . . . . 32 ASP CB . 16885 1 934 . 2 2 32 32 ASP N N 15 117.685 0.300 . 1 . . . . 32 ASP N . 16885 1 935 . 2 2 33 33 LYS H H 1 7.516 0.020 . 1 . . . . 33 LYS HN . 16885 1 936 . 2 2 33 33 LYS HA H 1 4.305 0.020 . 1 . . . . 33 LYS HA . 16885 1 937 . 2 2 33 33 LYS HB2 H 1 1.865 0.020 . 2 . . . . 33 LYS HB2 . 16885 1 938 . 2 2 33 33 LYS HB3 H 1 1.996 0.020 . 2 . . . . 33 LYS HB3 . 16885 1 939 . 2 2 33 33 LYS HD2 H 1 1.721 0.020 . 2 . . . . 33 LYS QD . 16885 1 940 . 2 2 33 33 LYS HD3 H 1 1.721 0.020 . 2 . . . . 33 LYS QD . 16885 1 941 . 2 2 33 33 LYS HE2 H 1 3.144 0.020 . 2 . . . . 33 LYS HE2 . 16885 1 942 . 2 2 33 33 LYS HE3 H 1 3.187 0.020 . 2 . . . . 33 LYS HE3 . 16885 1 943 . 2 2 33 33 LYS HG2 H 1 1.605 0.020 . 2 . . . . 33 LYS QG . 16885 1 944 . 2 2 33 33 LYS HG3 H 1 1.605 0.020 . 2 . . . . 33 LYS QG . 16885 1 945 . 2 2 33 33 LYS CA C 13 58.318 0.300 . 1 . . . . 33 LYS CA . 16885 1 946 . 2 2 33 33 LYS CB C 13 34.065 0.300 . 1 . . . . 33 LYS CB . 16885 1 947 . 2 2 33 33 LYS CD C 13 28.982 0.300 . 1 . . . . 33 LYS CD . 16885 1 948 . 2 2 33 33 LYS CE C 13 42.146 0.300 . 1 . . . . 33 LYS CE . 16885 1 949 . 2 2 33 33 LYS CG C 13 25.258 0.300 . 1 . . . . 33 LYS CG . 16885 1 950 . 2 2 33 33 LYS N N 15 113.387 0.300 . 1 . . . . 33 LYS N . 16885 1 951 . 2 2 34 34 GLU H H 1 8.764 0.020 . 1 . . . . 34 GLU HN . 16885 1 952 . 2 2 34 34 GLU HA H 1 4.577 0.020 . 1 . . . . 34 GLU HA . 16885 1 953 . 2 2 34 34 GLU HB2 H 1 1.678 0.020 . 2 . . . . 34 GLU HB2 . 16885 1 954 . 2 2 34 34 GLU HB3 H 1 2.287 0.020 . 2 . . . . 34 GLU HB3 . 16885 1 955 . 2 2 34 34 GLU HG2 H 1 2.083 0.020 . 2 . . . . 34 GLU HG2 . 16885 1 956 . 2 2 34 34 GLU HG3 H 1 2.192 0.020 . 2 . . . . 34 GLU HG3 . 16885 1 957 . 2 2 34 34 GLU CA C 13 55.247 0.300 . 1 . . . . 34 GLU CA . 16885 1 958 . 2 2 34 34 GLU CB C 13 33.236 0.300 . 1 . . . . 34 GLU CB . 16885 1 959 . 2 2 34 34 GLU CG C 13 36.111 0.300 . 1 . . . . 34 GLU CG . 16885 1 960 . 2 2 34 34 GLU N N 15 111.566 0.300 . 1 . . . . 34 GLU N . 16885 1 961 . 2 2 35 35 GLY H H 1 8.559 0.020 . 1 . . . . 35 GLY HN . 16885 1 962 . 2 2 35 35 GLY HA2 H 1 3.924 0.020 . 2 . . . . 35 GLY HA1 . 16885 1 963 . 2 2 35 35 GLY HA3 H 1 4.147 0.020 . 2 . . . . 35 GLY HA2 . 16885 1 964 . 2 2 35 35 GLY CA C 13 45.902 0.300 . 1 . . . . 35 GLY CA . 16885 1 965 . 2 2 35 35 GLY N N 15 106.728 0.300 . 1 . . . . 35 GLY N . 16885 1 966 . 2 2 36 36 ILE H H 1 6.164 0.020 . 1 . . . . 36 ILE HN . 16885 1 967 . 2 2 36 36 ILE HA H 1 4.399 0.020 . 1 . . . . 36 ILE HA . 16885 1 968 . 2 2 36 36 ILE HB H 1 1.404 0.020 . 1 . . . . 36 ILE HB . 16885 1 969 . 2 2 36 36 ILE HD11 H 1 0.794 0.020 . 1 . . . . 36 ILE QD1 . 16885 1 970 . 2 2 36 36 ILE HD12 H 1 0.794 0.020 . 1 . . . . 36 ILE QD1 . 16885 1 971 . 2 2 36 36 ILE HD13 H 1 0.794 0.020 . 1 . . . . 36 ILE QD1 . 16885 1 972 . 2 2 36 36 ILE HG12 H 1 1.100 0.020 . 2 . . . . 36 ILE HG12 . 16885 1 973 . 2 2 36 36 ILE HG13 H 1 1.398 0.020 . 2 . . . . 36 ILE HG13 . 16885 1 974 . 2 2 36 36 ILE HG21 H 1 0.946 0.020 . 1 . . . . 36 ILE QG2 . 16885 1 975 . 2 2 36 36 ILE HG22 H 1 0.946 0.020 . 1 . . . . 36 ILE QG2 . 16885 1 976 . 2 2 36 36 ILE HG23 H 1 0.946 0.020 . 1 . . . . 36 ILE QG2 . 16885 1 977 . 2 2 36 36 ILE CA C 13 57.903 0.300 . 1 . . . . 36 ILE CA . 16885 1 978 . 2 2 36 36 ILE CB C 13 40.634 0.300 . 1 . . . . 36 ILE CB . 16885 1 979 . 2 2 36 36 ILE CD1 C 13 13.638 0.300 . 1 . . . . 36 ILE CD1 . 16885 1 980 . 2 2 36 36 ILE CG1 C 13 26.866 0.300 . 1 . . . . 36 ILE CG1 . 16885 1 981 . 2 2 36 36 ILE CG2 C 13 17.995 0.300 . 1 . . . . 36 ILE CG2 . 16885 1 982 . 2 2 36 36 ILE N N 15 118.290 0.300 . 1 . . . . 36 ILE N . 16885 1 983 . 2 2 37 37 PRO HA H 1 4.630 0.020 . 1 . . . . 37 PRO HA . 16885 1 984 . 2 2 37 37 PRO HB2 H 1 1.967 0.020 . 2 . . . . 37 PRO HB2 . 16885 1 985 . 2 2 37 37 PRO HB3 H 1 2.428 0.020 . 2 . . . . 37 PRO HB3 . 16885 1 986 . 2 2 37 37 PRO HD2 H 1 3.545 0.020 . 2 . . . . 37 PRO HD2 . 16885 1 987 . 2 2 37 37 PRO HD3 H 1 4.234 0.020 . 2 . . . . 37 PRO HD3 . 16885 1 988 . 2 2 37 37 PRO HG2 H 1 2.056 0.020 . 2 . . . . 37 PRO HG2 . 16885 1 989 . 2 2 37 37 PRO HG3 H 1 2.136 0.020 . 2 . . . . 37 PRO HG3 . 16885 1 990 . 2 2 37 37 PRO CA C 13 61.364 0.300 . 1 . . . . 37 PRO CA . 16885 1 991 . 2 2 37 37 PRO CB C 13 31.860 0.300 . 1 . . . . 37 PRO CB . 16885 1 992 . 2 2 37 37 PRO CD C 13 50.995 0.300 . 1 . . . . 37 PRO CD . 16885 1 993 . 2 2 37 37 PRO CG C 13 28.208 0.300 . 1 . . . . 37 PRO CG . 16885 1 994 . 2 2 38 38 PRO HA H 1 4.132 0.020 . 1 . . . . 38 PRO HA . 16885 1 995 . 2 2 38 38 PRO HB2 H 1 2.031 0.020 . 2 . . . . 38 PRO HB2 . 16885 1 996 . 2 2 38 38 PRO HB3 H 1 2.254 0.020 . 2 . . . . 38 PRO HB3 . 16885 1 997 . 2 2 38 38 PRO HD2 H 1 3.759 0.020 . 2 . . . . 38 PRO QD . 16885 1 998 . 2 2 38 38 PRO HD3 H 1 3.759 0.020 . 2 . . . . 38 PRO QD . 16885 1 999 . 2 2 38 38 PRO HG2 H 1 1.623 0.020 . 2 . . . . 38 PRO HG2 . 16885 1 1000 . 2 2 38 38 PRO HG3 H 1 2.186 0.020 . 2 . . . . 38 PRO HG3 . 16885 1 1001 . 2 2 38 38 PRO CA C 13 66.056 0.300 . 1 . . . . 38 PRO CA . 16885 1 1002 . 2 2 38 38 PRO CB C 13 32.837 0.300 . 1 . . . . 38 PRO CB . 16885 1 1003 . 2 2 38 38 PRO CD C 13 51.160 0.300 . 1 . . . . 38 PRO CD . 16885 1 1004 . 2 2 38 38 PRO CG C 13 27.624 0.300 . 1 . . . . 38 PRO CG . 16885 1 1005 . 2 2 39 39 ASP H H 1 8.637 0.020 . 1 . . . . 39 ASP HN . 16885 1 1006 . 2 2 39 39 ASP HA H 1 4.390 0.020 . 1 . . . . 39 ASP HA . 16885 1 1007 . 2 2 39 39 ASP HB2 H 1 2.688 0.020 . 2 . . . . 39 ASP HB2 . 16885 1 1008 . 2 2 39 39 ASP HB3 H 1 2.800 0.020 . 2 . . . . 39 ASP HB3 . 16885 1 1009 . 2 2 39 39 ASP CA C 13 55.691 0.300 . 1 . . . . 39 ASP CA . 16885 1 1010 . 2 2 39 39 ASP CB C 13 39.574 0.300 . 1 . . . . 39 ASP CB . 16885 1 1011 . 2 2 39 39 ASP N N 15 111.553 0.300 . 1 . . . . 39 ASP N . 16885 1 1012 . 2 2 40 40 GLN H H 1 7.845 0.020 . 1 . . . . 40 GLN HN . 16885 1 1013 . 2 2 40 40 GLN HA H 1 4.354 0.020 . 1 . . . . 40 GLN HA . 16885 1 1014 . 2 2 40 40 GLN HB2 H 1 1.860 0.020 . 2 . . . . 40 GLN HB2 . 16885 1 1015 . 2 2 40 40 GLN HB3 H 1 2.517 0.020 . 2 . . . . 40 GLN HB3 . 16885 1 1016 . 2 2 40 40 GLN HE21 H 1 6.824 0.020 . 2 . . . . 40 GLN HE21 . 16885 1 1017 . 2 2 40 40 GLN HE22 H 1 7.753 0.020 . 2 . . . . 40 GLN HE22 . 16885 1 1018 . 2 2 40 40 GLN HG2 H 1 2.434 0.020 . 2 . . . . 40 GLN QG . 16885 1 1019 . 2 2 40 40 GLN HG3 H 1 2.434 0.020 . 2 . . . . 40 GLN QG . 16885 1 1020 . 2 2 40 40 GLN CA C 13 55.422 0.300 . 1 . . . . 40 GLN CA . 16885 1 1021 . 2 2 40 40 GLN CB C 13 30.003 0.300 . 1 . . . . 40 GLN CB . 16885 1 1022 . 2 2 40 40 GLN CG C 13 34.101 0.300 . 1 . . . . 40 GLN CG . 16885 1 1023 . 2 2 40 40 GLN N N 15 114.377 0.300 . 1 . . . . 40 GLN N . 16885 1 1024 . 2 2 40 40 GLN NE2 N 15 109.618 0.300 . 1 . . . . 40 GLN NE2 . 16885 1 1025 . 2 2 41 41 GLN H H 1 7.606 0.020 . 1 . . . . 41 GLN HN . 16885 1 1026 . 2 2 41 41 GLN HA H 1 3.995 0.020 . 1 . . . . 41 GLN HA . 16885 1 1027 . 2 2 41 41 GLN HB2 H 1 1.857 0.020 . 2 . . . . 41 GLN HB2 . 16885 1 1028 . 2 2 41 41 GLN HB3 H 1 1.977 0.020 . 2 . . . . 41 GLN HB3 . 16885 1 1029 . 2 2 41 41 GLN HE21 H 1 6.025 0.020 . 2 . . . . 41 GLN HE21 . 16885 1 1030 . 2 2 41 41 GLN HE22 H 1 6.540 0.020 . 2 . . . . 41 GLN HE22 . 16885 1 1031 . 2 2 41 41 GLN HG2 H 1 1.627 0.020 . 2 . . . . 41 GLN HG2 . 16885 1 1032 . 2 2 41 41 GLN HG3 H 1 2.554 0.020 . 2 . . . . 41 GLN HG3 . 16885 1 1033 . 2 2 41 41 GLN CA C 13 56.998 0.300 . 1 . . . . 41 GLN CA . 16885 1 1034 . 2 2 41 41 GLN CB C 13 31.246 0.300 . 1 . . . . 41 GLN CB . 16885 1 1035 . 2 2 41 41 GLN CG C 13 33.398 0.300 . 1 . . . . 41 GLN CG . 16885 1 1036 . 2 2 41 41 GLN N N 15 115.743 0.300 . 1 . . . . 41 GLN N . 16885 1 1037 . 2 2 41 41 GLN NE2 N 15 102.045 0.300 . 1 . . . . 41 GLN NE2 . 16885 1 1038 . 2 2 42 42 ARG H H 1 7.601 0.020 . 1 . . . . 42 ARG HN . 16885 1 1039 . 2 2 42 42 ARG HA H 1 4.531 0.020 . 1 . . . . 42 ARG HA . 16885 1 1040 . 2 2 42 42 ARG HB2 H 1 1.349 0.020 . 2 . . . . 42 ARG HB2 . 16885 1 1041 . 2 2 42 42 ARG HB3 H 1 2.262 0.020 . 2 . . . . 42 ARG HB3 . 16885 1 1042 . 2 2 42 42 ARG HD2 H 1 2.956 0.020 . 2 . . . . 42 ARG HD2 . 16885 1 1043 . 2 2 42 42 ARG HD3 H 1 3.175 0.020 . 2 . . . . 42 ARG HD3 . 16885 1 1044 . 2 2 42 42 ARG HG2 H 1 1.449 0.020 . 2 . . . . 42 ARG HG2 . 16885 1 1045 . 2 2 42 42 ARG HG3 H 1 1.729 0.020 . 2 . . . . 42 ARG HG3 . 16885 1 1046 . 2 2 42 42 ARG CA C 13 55.469 0.300 . 1 . . . . 42 ARG CA . 16885 1 1047 . 2 2 42 42 ARG CB C 13 31.779 0.300 . 1 . . . . 42 ARG CB . 16885 1 1048 . 2 2 42 42 ARG CD C 13 44.271 0.300 . 1 . . . . 42 ARG CD . 16885 1 1049 . 2 2 42 42 ARG CG C 13 26.444 0.300 . 1 . . . . 42 ARG CG . 16885 1 1050 . 2 2 42 42 ARG N N 15 117.888 0.300 . 1 . . . . 42 ARG N . 16885 1 1051 . 2 2 43 43 LEU H H 1 8.863 0.020 . 1 . . . . 43 LEU HN . 16885 1 1052 . 2 2 43 43 LEU HA H 1 5.375 0.020 . 1 . . . . 43 LEU HA . 16885 1 1053 . 2 2 43 43 LEU HB2 H 1 1.160 0.020 . 2 . . . . 43 LEU HB2 . 16885 1 1054 . 2 2 43 43 LEU HB3 H 1 1.509 0.020 . 2 . . . . 43 LEU HB3 . 16885 1 1055 . 2 2 43 43 LEU HD11 H 1 0.771 0.020 . 2 . . . . 43 LEU QD1 . 16885 1 1056 . 2 2 43 43 LEU HD12 H 1 0.771 0.020 . 2 . . . . 43 LEU QD1 . 16885 1 1057 . 2 2 43 43 LEU HD13 H 1 0.771 0.020 . 2 . . . . 43 LEU QD1 . 16885 1 1058 . 2 2 43 43 LEU HD21 H 1 0.804 0.020 . 2 . . . . 43 LEU QD2 . 16885 1 1059 . 2 2 43 43 LEU HD22 H 1 0.804 0.020 . 2 . . . . 43 LEU QD2 . 16885 1 1060 . 2 2 43 43 LEU HD23 H 1 0.804 0.020 . 2 . . . . 43 LEU QD2 . 16885 1 1061 . 2 2 43 43 LEU HG H 1 1.463 0.020 . 1 . . . . 43 LEU HG . 16885 1 1062 . 2 2 43 43 LEU CA C 13 52.839 0.300 . 1 . . . . 43 LEU CA . 16885 1 1063 . 2 2 43 43 LEU CB C 13 45.439 0.300 . 1 . . . . 43 LEU CB . 16885 1 1064 . 2 2 43 43 LEU CD1 C 13 26.553 0.300 . 2 . . . . 43 LEU CD1 . 16885 1 1065 . 2 2 43 43 LEU CD2 C 13 24.146 0.300 . 2 . . . . 43 LEU CD2 . 16885 1 1066 . 2 2 43 43 LEU CG C 13 27.089 0.300 . 1 . . . . 43 LEU CG . 16885 1 1067 . 2 2 43 43 LEU N N 15 120.908 0.300 . 1 . . . . 43 LEU N . 16885 1 1068 . 2 2 44 44 ILE H H 1 9.350 0.020 . 1 . . . . 44 ILE HN . 16885 1 1069 . 2 2 44 44 ILE HA H 1 5.015 0.020 . 1 . . . . 44 ILE HA . 16885 1 1070 . 2 2 44 44 ILE HB H 1 1.872 0.020 . 1 . . . . 44 ILE HB . 16885 1 1071 . 2 2 44 44 ILE HD11 H 1 0.654 0.020 . 1 . . . . 44 ILE QD1 . 16885 1 1072 . 2 2 44 44 ILE HD12 H 1 0.654 0.020 . 1 . . . . 44 ILE QD1 . 16885 1 1073 . 2 2 44 44 ILE HD13 H 1 0.654 0.020 . 1 . . . . 44 ILE QD1 . 16885 1 1074 . 2 2 44 44 ILE HG12 H 1 1.140 0.020 . 2 . . . . 44 ILE HG12 . 16885 1 1075 . 2 2 44 44 ILE HG13 H 1 1.219 0.020 . 2 . . . . 44 ILE HG13 . 16885 1 1076 . 2 2 44 44 ILE HG21 H 1 0.828 0.020 . 1 . . . . 44 ILE QG2 . 16885 1 1077 . 2 2 44 44 ILE HG22 H 1 0.828 0.020 . 1 . . . . 44 ILE QG2 . 16885 1 1078 . 2 2 44 44 ILE HG23 H 1 0.828 0.020 . 1 . . . . 44 ILE QG2 . 16885 1 1079 . 2 2 44 44 ILE CA C 13 58.625 0.300 . 1 . . . . 44 ILE CA . 16885 1 1080 . 2 2 44 44 ILE CB C 13 41.114 0.300 . 1 . . . . 44 ILE CB . 16885 1 1081 . 2 2 44 44 ILE CD1 C 13 13.357 0.300 . 1 . . . . 44 ILE CD1 . 16885 1 1082 . 2 2 44 44 ILE CG1 C 13 29.083 0.300 . 1 . . . . 44 ILE CG1 . 16885 1 1083 . 2 2 44 44 ILE CG2 C 13 19.054 0.300 . 1 . . . . 44 ILE CG2 . 16885 1 1084 . 2 2 44 44 ILE N N 15 121.104 0.300 . 1 . . . . 44 ILE N . 16885 1 1085 . 2 2 45 45 PHE H H 1 8.865 0.020 . 1 . . . . 45 PHE HN . 16885 1 1086 . 2 2 45 45 PHE HA H 1 5.217 0.020 . 1 . . . . 45 PHE HA . 16885 1 1087 . 2 2 45 45 PHE HB2 H 1 2.780 0.020 . 2 . . . . 45 PHE HB2 . 16885 1 1088 . 2 2 45 45 PHE HB3 H 1 3.070 0.020 . 2 . . . . 45 PHE HB3 . 16885 1 1089 . 2 2 45 45 PHE HD1 H 1 7.372 0.020 . 3 . . . . 45 PHE QD . 16885 1 1090 . 2 2 45 45 PHE HD2 H 1 7.372 0.020 . 3 . . . . 45 PHE QD . 16885 1 1091 . 2 2 45 45 PHE HE1 H 1 7.528 0.020 . 3 . . . . 45 PHE QE . 16885 1 1092 . 2 2 45 45 PHE HE2 H 1 7.528 0.020 . 3 . . . . 45 PHE QE . 16885 1 1093 . 2 2 45 45 PHE HZ H 1 7.469 0.020 . 1 . . . . 45 PHE HZ . 16885 1 1094 . 2 2 45 45 PHE CA C 13 57.018 0.300 . 1 . . . . 45 PHE CA . 16885 1 1095 . 2 2 45 45 PHE CB C 13 44.048 0.300 . 1 . . . . 45 PHE CB . 16885 1 1096 . 2 2 45 45 PHE CD1 C 13 132.281 0.300 . 3 . . . . 45 PHE CD1 . 16885 1 1097 . 2 2 45 45 PHE CE1 C 13 132.285 0.300 . 3 . . . . 45 PHE CE1 . 16885 1 1098 . 2 2 45 45 PHE CZ C 13 130.161 0.300 . 1 . . . . 45 PHE CZ . 16885 1 1099 . 2 2 45 45 PHE N N 15 122.480 0.300 . 1 . . . . 45 PHE N . 16885 1 1100 . 2 2 46 46 ALA H H 1 8.804 0.020 . 1 . . . . 46 ALA HN . 16885 1 1101 . 2 2 46 46 ALA HA H 1 3.762 0.020 . 1 . . . . 46 ALA HA . 16885 1 1102 . 2 2 46 46 ALA HB1 H 1 0.944 0.020 . 1 . . . . 46 ALA QB . 16885 1 1103 . 2 2 46 46 ALA HB2 H 1 0.944 0.020 . 1 . . . . 46 ALA QB . 16885 1 1104 . 2 2 46 46 ALA HB3 H 1 0.944 0.020 . 1 . . . . 46 ALA QB . 16885 1 1105 . 2 2 46 46 ALA CA C 13 52.491 0.300 . 1 . . . . 46 ALA CA . 16885 1 1106 . 2 2 46 46 ALA CB C 13 16.550 0.300 . 1 . . . . 46 ALA CB . 16885 1 1107 . 2 2 46 46 ALA N N 15 130.137 0.300 . 1 . . . . 46 ALA N . 16885 1 1108 . 2 2 47 47 GLY H H 1 8.606 0.020 . 1 . . . . 47 GLY HN . 16885 1 1109 . 2 2 47 47 GLY HA2 H 1 3.405 0.020 . 2 . . . . 47 GLY HA1 . 16885 1 1110 . 2 2 47 47 GLY HA3 H 1 4.052 0.020 . 2 . . . . 47 GLY HA2 . 16885 1 1111 . 2 2 47 47 GLY CA C 13 45.422 0.300 . 1 . . . . 47 GLY CA . 16885 1 1112 . 2 2 47 47 GLY N N 15 100.196 0.300 . 1 . . . . 47 GLY N . 16885 1 1113 . 2 2 48 48 LYS H H 1 7.855 0.020 . 1 . . . . 48 LYS HN . 16885 1 1114 . 2 2 48 48 LYS HA H 1 4.716 0.020 . 1 . . . . 48 LYS HA . 16885 1 1115 . 2 2 48 48 LYS HB2 H 1 1.871 0.020 . 2 . . . . 48 LYS QB . 16885 1 1116 . 2 2 48 48 LYS HB3 H 1 1.871 0.020 . 2 . . . . 48 LYS QB . 16885 1 1117 . 2 2 48 48 LYS HD2 H 1 1.838 0.020 . 2 . . . . 48 LYS HD2 . 16885 1 1118 . 2 2 48 48 LYS HD3 H 1 1.866 0.020 . 2 . . . . 48 LYS HD3 . 16885 1 1119 . 2 2 48 48 LYS HE2 H 1 3.163 0.020 . 2 . . . . 48 LYS QE . 16885 1 1120 . 2 2 48 48 LYS HE3 H 1 3.163 0.020 . 2 . . . . 48 LYS QE . 16885 1 1121 . 2 2 48 48 LYS HG2 H 1 1.516 0.020 . 2 . . . . 48 LYS QG . 16885 1 1122 . 2 2 48 48 LYS HG3 H 1 1.516 0.020 . 2 . . . . 48 LYS QG . 16885 1 1123 . 2 2 48 48 LYS CA C 13 54.188 0.300 . 1 . . . . 48 LYS CA . 16885 1 1124 . 2 2 48 48 LYS CB C 13 35.071 0.300 . 1 . . . . 48 LYS CB . 16885 1 1125 . 2 2 48 48 LYS CD C 13 28.973 0.300 . 1 . . . . 48 LYS CD . 16885 1 1126 . 2 2 48 48 LYS CE C 13 42.218 0.300 . 1 . . . . 48 LYS CE . 16885 1 1127 . 2 2 48 48 LYS CG C 13 24.196 0.300 . 1 . . . . 48 LYS CG . 16885 1 1128 . 2 2 48 48 LYS N N 15 117.519 0.300 . 1 . . . . 48 LYS N . 16885 1 1129 . 2 2 49 49 GLN H H 1 8.954 0.020 . 1 . . . . 49 GLN HN . 16885 1 1130 . 2 2 49 49 GLN HA H 1 4.578 0.020 . 1 . . . . 49 GLN HA . 16885 1 1131 . 2 2 49 49 GLN HB2 H 1 1.936 0.020 . 2 . . . . 49 GLN HB2 . 16885 1 1132 . 2 2 49 49 GLN HB3 H 1 2.046 0.020 . 2 . . . . 49 GLN HB3 . 16885 1 1133 . 2 2 49 49 GLN HE21 H 1 7.079 0.020 . 2 . . . . 49 GLN HE21 . 16885 1 1134 . 2 2 49 49 GLN HE22 H 1 7.882 0.020 . 2 . . . . 49 GLN HE22 . 16885 1 1135 . 2 2 49 49 GLN HG2 H 1 2.231 0.020 . 2 . . . . 49 GLN HG2 . 16885 1 1136 . 2 2 49 49 GLN HG3 H 1 2.274 0.020 . 2 . . . . 49 GLN HG3 . 16885 1 1137 . 2 2 49 49 GLN CA C 13 56.199 0.300 . 1 . . . . 49 GLN CA . 16885 1 1138 . 2 2 49 49 GLN CB C 13 28.971 0.300 . 1 . . . . 49 GLN CB . 16885 1 1139 . 2 2 49 49 GLN CG C 13 34.937 0.300 . 1 . . . . 49 GLN CG . 16885 1 1140 . 2 2 49 49 GLN N N 15 120.047 0.300 . 1 . . . . 49 GLN N . 16885 1 1141 . 2 2 49 49 GLN NE2 N 15 110.187 0.300 . 1 . . . . 49 GLN NE2 . 16885 1 1142 . 2 2 50 50 LEU H H 1 8.785 0.020 . 1 . . . . 50 LEU HN . 16885 1 1143 . 2 2 50 50 LEU HA H 1 4.141 0.020 . 1 . . . . 50 LEU HA . 16885 1 1144 . 2 2 50 50 LEU HB2 H 1 1.099 0.020 . 2 . . . . 50 LEU HB2 . 16885 1 1145 . 2 2 50 50 LEU HB3 H 1 1.447 0.020 . 2 . . . . 50 LEU HB3 . 16885 1 1146 . 2 2 50 50 LEU HD11 H 1 -0.175 0.020 . 2 . . . . 50 LEU QD1 . 16885 1 1147 . 2 2 50 50 LEU HD12 H 1 -0.175 0.020 . 2 . . . . 50 LEU QD1 . 16885 1 1148 . 2 2 50 50 LEU HD13 H 1 -0.175 0.020 . 2 . . . . 50 LEU QD1 . 16885 1 1149 . 2 2 50 50 LEU HD21 H 1 0.502 0.020 . 2 . . . . 50 LEU QD2 . 16885 1 1150 . 2 2 50 50 LEU HD22 H 1 0.502 0.020 . 2 . . . . 50 LEU QD2 . 16885 1 1151 . 2 2 50 50 LEU HD23 H 1 0.502 0.020 . 2 . . . . 50 LEU QD2 . 16885 1 1152 . 2 2 50 50 LEU HG H 1 1.551 0.020 . 1 . . . . 50 LEU HG . 16885 1 1153 . 2 2 50 50 LEU CA C 13 54.219 0.300 . 1 . . . . 50 LEU CA . 16885 1 1154 . 2 2 50 50 LEU CB C 13 41.916 0.300 . 1 . . . . 50 LEU CB . 16885 1 1155 . 2 2 50 50 LEU CD1 C 13 19.005 0.300 . 2 . . . . 50 LEU CD1 . 16885 1 1156 . 2 2 50 50 LEU CD2 C 13 25.660 0.300 . 2 . . . . 50 LEU CD2 . 16885 1 1157 . 2 2 50 50 LEU CG C 13 25.682 0.300 . 1 . . . . 50 LEU CG . 16885 1 1158 . 2 2 50 50 LEU N N 15 123.531 0.300 . 1 . . . . 50 LEU N . 16885 1 1159 . 2 2 51 51 GLU H H 1 8.536 0.020 . 1 . . . . 51 GLU HN . 16885 1 1160 . 2 2 51 51 GLU HA H 1 4.470 0.020 . 1 . . . . 51 GLU HA . 16885 1 1161 . 2 2 51 51 GLU HB2 H 1 2.018 0.020 . 2 . . . . 51 GLU HB2 . 16885 1 1162 . 2 2 51 51 GLU HB3 H 1 2.239 0.020 . 2 . . . . 51 GLU HB3 . 16885 1 1163 . 2 2 51 51 GLU HG2 H 1 2.356 0.020 . 2 . . . . 51 GLU HG2 . 16885 1 1164 . 2 2 51 51 GLU HG3 H 1 2.437 0.020 . 2 . . . . 51 GLU HG3 . 16885 1 1165 . 2 2 51 51 GLU CA C 13 55.967 0.300 . 1 . . . . 51 GLU CA . 16885 1 1166 . 2 2 51 51 GLU CB C 13 31.792 0.300 . 1 . . . . 51 GLU CB . 16885 1 1167 . 2 2 51 51 GLU CG C 13 36.652 0.300 . 1 . . . . 51 GLU CG . 16885 1 1168 . 2 2 51 51 GLU N N 15 120.476 0.300 . 1 . . . . 51 GLU N . 16885 1 1169 . 2 2 52 52 ASP H H 1 8.268 0.020 . 1 . . . . 52 ASP HN . 16885 1 1170 . 2 2 52 52 ASP HA H 1 4.391 0.020 . 1 . . . . 52 ASP HA . 16885 1 1171 . 2 2 52 52 ASP HB2 H 1 2.532 0.020 . 2 . . . . 52 ASP HB2 . 16885 1 1172 . 2 2 52 52 ASP HB3 H 1 2.625 0.020 . 2 . . . . 52 ASP HB3 . 16885 1 1173 . 2 2 52 52 ASP CA C 13 56.839 0.300 . 1 . . . . 52 ASP CA . 16885 1 1174 . 2 2 52 52 ASP CB C 13 40.860 0.300 . 1 . . . . 52 ASP CB . 16885 1 1175 . 2 2 52 52 ASP N N 15 118.305 0.300 . 1 . . . . 52 ASP N . 16885 1 1176 . 2 2 53 53 GLY HA2 H 1 3.928 0.020 . 2 . . . . 53 GLY HA1 . 16885 1 1177 . 2 2 53 53 GLY HA3 H 1 4.136 0.020 . 2 . . . . 53 GLY HA2 . 16885 1 1178 . 2 2 53 53 GLY CA C 13 45.176 0.300 . 1 . . . . 53 GLY CA . 16885 1 1179 . 2 2 54 54 ARG H H 1 7.424 0.020 . 1 . . . . 54 ARG HN . 16885 1 1180 . 2 2 54 54 ARG HA H 1 4.682 0.020 . 1 . . . . 54 ARG HA . 16885 1 1181 . 2 2 54 54 ARG HB2 H 1 2.010 0.020 . 2 . . . . 54 ARG HB2 . 16885 1 1182 . 2 2 54 54 ARG HB3 H 1 2.177 0.020 . 2 . . . . 54 ARG HB3 . 16885 1 1183 . 2 2 54 54 ARG HD2 H 1 3.049 0.020 . 2 . . . . 54 ARG HD2 . 16885 1 1184 . 2 2 54 54 ARG HD3 H 1 3.122 0.020 . 2 . . . . 54 ARG HD3 . 16885 1 1185 . 2 2 54 54 ARG HE H 1 7.074 0.020 . 1 . . . . 54 ARG HE . 16885 1 1186 . 2 2 54 54 ARG HG2 H 1 1.610 0.020 . 2 . . . . 54 ARG HG2 . 16885 1 1187 . 2 2 54 54 ARG HG3 H 1 1.794 0.020 . 2 . . . . 54 ARG HG3 . 16885 1 1188 . 2 2 54 54 ARG CA C 13 54.341 0.300 . 1 . . . . 54 ARG CA . 16885 1 1189 . 2 2 54 54 ARG CB C 13 32.550 0.300 . 1 . . . . 54 ARG CB . 16885 1 1190 . 2 2 54 54 ARG CD C 13 42.864 0.300 . 1 . . . . 54 ARG CD . 16885 1 1191 . 2 2 54 54 ARG CG C 13 27.437 0.300 . 1 . . . . 54 ARG CG . 16885 1 1192 . 2 2 54 54 ARG N N 15 117.073 0.300 . 1 . . . . 54 ARG N . 16885 1 1193 . 2 2 54 54 ARG NE N 15 82.614 0.300 . 1 . . . . 54 ARG NE . 16885 1 1194 . 2 2 55 55 THR H H 1 8.844 0.020 . 1 . . . . 55 THR HN . 16885 1 1195 . 2 2 55 55 THR HA H 1 5.211 0.020 . 1 . . . . 55 THR HA . 16885 1 1196 . 2 2 55 55 THR HB H 1 4.552 0.020 . 1 . . . . 55 THR HB . 16885 1 1197 . 2 2 55 55 THR HG21 H 1 1.129 0.020 . 1 . . . . 55 THR QG2 . 16885 1 1198 . 2 2 55 55 THR HG22 H 1 1.129 0.020 . 1 . . . . 55 THR QG2 . 16885 1 1199 . 2 2 55 55 THR HG23 H 1 1.129 0.020 . 1 . . . . 55 THR QG2 . 16885 1 1200 . 2 2 55 55 THR CA C 13 59.629 0.300 . 1 . . . . 55 THR CA . 16885 1 1201 . 2 2 55 55 THR CB C 13 72.275 0.300 . 1 . . . . 55 THR CB . 16885 1 1202 . 2 2 55 55 THR CG2 C 13 22.229 0.300 . 1 . . . . 55 THR CG2 . 16885 1 1203 . 2 2 55 55 THR N N 15 106.315 0.300 . 1 . . . . 55 THR N . 16885 1 1204 . 2 2 56 56 LEU H H 1 8.194 0.020 . 1 . . . . 56 LEU HN . 16885 1 1205 . 2 2 56 56 LEU HA H 1 4.053 0.020 . 1 . . . . 56 LEU HA . 16885 1 1206 . 2 2 56 56 LEU HB2 H 1 1.199 0.020 . 2 . . . . 56 LEU HB2 . 16885 1 1207 . 2 2 56 56 LEU HB3 H 1 2.108 0.020 . 2 . . . . 56 LEU HB3 . 16885 1 1208 . 2 2 56 56 LEU HD11 H 1 0.617 0.020 . 2 . . . . 56 LEU QD1 . 16885 1 1209 . 2 2 56 56 LEU HD12 H 1 0.617 0.020 . 2 . . . . 56 LEU QD1 . 16885 1 1210 . 2 2 56 56 LEU HD13 H 1 0.617 0.020 . 2 . . . . 56 LEU QD1 . 16885 1 1211 . 2 2 56 56 LEU HD21 H 1 0.745 0.020 . 2 . . . . 56 LEU QD2 . 16885 1 1212 . 2 2 56 56 LEU HD22 H 1 0.745 0.020 . 2 . . . . 56 LEU QD2 . 16885 1 1213 . 2 2 56 56 LEU HD23 H 1 0.745 0.020 . 2 . . . . 56 LEU QD2 . 16885 1 1214 . 2 2 56 56 LEU HG H 1 1.731 0.020 . 1 . . . . 56 LEU HG . 16885 1 1215 . 2 2 56 56 LEU CA C 13 58.551 0.300 . 1 . . . . 56 LEU CA . 16885 1 1216 . 2 2 56 56 LEU CB C 13 40.034 0.300 . 1 . . . . 56 LEU CB . 16885 1 1217 . 2 2 56 56 LEU CD1 C 13 23.176 0.300 . 2 . . . . 56 LEU CD1 . 16885 1 1218 . 2 2 56 56 LEU CD2 C 13 26.723 0.300 . 2 . . . . 56 LEU CD2 . 16885 1 1219 . 2 2 56 56 LEU CG C 13 26.576 0.300 . 1 . . . . 56 LEU CG . 16885 1 1220 . 2 2 56 56 LEU N N 15 115.531 0.300 . 1 . . . . 56 LEU N . 16885 1 1221 . 2 2 57 57 SER H H 1 8.506 0.020 . 1 . . . . 57 SER HN . 16885 1 1222 . 2 2 57 57 SER HA H 1 4.229 0.020 . 1 . . . . 57 SER HA . 16885 1 1223 . 2 2 57 57 SER HB2 H 1 3.747 0.020 . 2 . . . . 57 SER HB2 . 16885 1 1224 . 2 2 57 57 SER HB3 H 1 3.838 0.020 . 2 . . . . 57 SER HB3 . 16885 1 1225 . 2 2 57 57 SER CA C 13 61.115 0.300 . 1 . . . . 57 SER CA . 16885 1 1226 . 2 2 57 57 SER CB C 13 62.469 0.300 . 1 . . . . 57 SER CB . 16885 1 1227 . 2 2 57 57 SER N N 15 111.067 0.300 . 1 . . . . 57 SER N . 16885 1 1228 . 2 2 58 58 ASP H H 1 8.033 0.020 . 1 . . . . 58 ASP HN . 16885 1 1229 . 2 2 58 58 ASP HA H 1 4.266 0.020 . 1 . . . . 58 ASP HA . 16885 1 1230 . 2 2 58 58 ASP HB2 H 1 2.282 0.020 . 2 . . . . 58 ASP HB2 . 16885 1 1231 . 2 2 58 58 ASP HB3 H 1 3.016 0.020 . 2 . . . . 58 ASP HB3 . 16885 1 1232 . 2 2 58 58 ASP CA C 13 57.338 0.300 . 1 . . . . 58 ASP CA . 16885 1 1233 . 2 2 58 58 ASP CB C 13 40.233 0.300 . 1 . . . . 58 ASP CB . 16885 1 1234 . 2 2 58 58 ASP N N 15 122.415 0.300 . 1 . . . . 58 ASP N . 16885 1 1235 . 2 2 59 59 TYR H H 1 7.275 0.020 . 1 . . . . 59 TYR HN . 16885 1 1236 . 2 2 59 59 TYR HA H 1 4.674 0.020 . 1 . . . . 59 TYR HA . 16885 1 1237 . 2 2 59 59 TYR HB2 H 1 2.532 0.020 . 2 . . . . 59 TYR HB2 . 16885 1 1238 . 2 2 59 59 TYR HB3 H 1 3.477 0.020 . 2 . . . . 59 TYR HB3 . 16885 1 1239 . 2 2 59 59 TYR HD1 H 1 7.252 0.020 . 3 . . . . 59 TYR QD . 16885 1 1240 . 2 2 59 59 TYR HD2 H 1 7.252 0.020 . 3 . . . . 59 TYR QD . 16885 1 1241 . 2 2 59 59 TYR HE1 H 1 6.907 0.020 . 3 . . . . 59 TYR HE1 . 16885 1 1242 . 2 2 59 59 TYR HE2 H 1 6.907 0.020 . 3 . . . . 59 TYR HE2 . 16885 1 1243 . 2 2 59 59 TYR CA C 13 58.296 0.300 . 1 . . . . 59 TYR CA . 16885 1 1244 . 2 2 59 59 TYR CB C 13 39.948 0.300 . 1 . . . . 59 TYR CB . 16885 1 1245 . 2 2 59 59 TYR CD1 C 13 133.504 0.300 . 3 . . . . 59 TYR CD1 . 16885 1 1246 . 2 2 59 59 TYR CE1 C 13 118.736 0.300 . 3 . . . . 59 TYR CE1 . 16885 1 1247 . 2 2 59 59 TYR N N 15 113.435 0.300 . 1 . . . . 59 TYR N . 16885 1 1248 . 2 2 60 60 ASN H H 1 8.210 0.020 . 1 . . . . 60 ASN HN . 16885 1 1249 . 2 2 60 60 ASN HA H 1 4.349 0.020 . 1 . . . . 60 ASN HA . 16885 1 1250 . 2 2 60 60 ASN HB2 H 1 2.824 0.020 . 2 . . . . 60 ASN HB2 . 16885 1 1251 . 2 2 60 60 ASN HB3 H 1 3.329 0.020 . 2 . . . . 60 ASN HB3 . 16885 1 1252 . 2 2 60 60 ASN HD21 H 1 6.892 0.020 . 2 . . . . 60 ASN HD21 . 16885 1 1253 . 2 2 60 60 ASN HD22 H 1 7.650 0.020 . 2 . . . . 60 ASN HD22 . 16885 1 1254 . 2 2 60 60 ASN CA C 13 54.123 0.300 . 1 . . . . 60 ASN CA . 16885 1 1255 . 2 2 60 60 ASN CB C 13 37.278 0.300 . 1 . . . . 60 ASN CB . 16885 1 1256 . 2 2 60 60 ASN N N 15 113.549 0.300 . 1 . . . . 60 ASN N . 16885 1 1257 . 2 2 60 60 ASN ND2 N 15 109.419 0.300 . 1 . . . . 60 ASN ND2 . 16885 1 1258 . 2 2 61 61 ILE H H 1 7.403 0.020 . 1 . . . . 61 ILE HN . 16885 1 1259 . 2 2 61 61 ILE HA H 1 3.338 0.020 . 1 . . . . 61 ILE HA . 16885 1 1260 . 2 2 61 61 ILE HB H 1 1.373 0.020 . 1 . . . . 61 ILE HB . 16885 1 1261 . 2 2 61 61 ILE HD11 H 1 0.423 0.020 . 1 . . . . 61 ILE QD1 . 16885 1 1262 . 2 2 61 61 ILE HD12 H 1 0.423 0.020 . 1 . . . . 61 ILE QD1 . 16885 1 1263 . 2 2 61 61 ILE HD13 H 1 0.423 0.020 . 1 . . . . 61 ILE QD1 . 16885 1 1264 . 2 2 61 61 ILE HG12 H 1 -0.643 0.020 . 2 . . . . 61 ILE HG12 . 16885 1 1265 . 2 2 61 61 ILE HG13 H 1 1.059 0.020 . 2 . . . . 61 ILE HG13 . 16885 1 1266 . 2 2 61 61 ILE HG21 H 1 0.460 0.020 . 1 . . . . 61 ILE QG2 . 16885 1 1267 . 2 2 61 61 ILE HG22 H 1 0.460 0.020 . 1 . . . . 61 ILE QG2 . 16885 1 1268 . 2 2 61 61 ILE HG23 H 1 0.460 0.020 . 1 . . . . 61 ILE QG2 . 16885 1 1269 . 2 2 61 61 ILE CA C 13 62.511 0.300 . 1 . . . . 61 ILE CA . 16885 1 1270 . 2 2 61 61 ILE CB C 13 36.679 0.300 . 1 . . . . 61 ILE CB . 16885 1 1271 . 2 2 61 61 ILE CD1 C 13 14.788 0.300 . 1 . . . . 61 ILE CD1 . 16885 1 1272 . 2 2 61 61 ILE CG1 C 13 28.018 0.300 . 1 . . . . 61 ILE CG1 . 16885 1 1273 . 2 2 61 61 ILE CG2 C 13 17.348 0.300 . 1 . . . . 61 ILE CG2 . 16885 1 1274 . 2 2 61 61 ILE N N 15 116.876 0.300 . 1 . . . . 61 ILE N . 16885 1 1275 . 2 2 62 62 GLN H H 1 7.685 0.020 . 1 . . . . 62 GLN HN . 16885 1 1276 . 2 2 62 62 GLN HA H 1 4.471 0.020 . 1 . . . . 62 GLN HA . 16885 1 1277 . 2 2 62 62 GLN HB2 H 1 1.892 0.020 . 2 . . . . 62 GLN HB2 . 16885 1 1278 . 2 2 62 62 GLN HB3 H 1 2.241 0.020 . 2 . . . . 62 GLN HB3 . 16885 1 1279 . 2 2 62 62 GLN HE21 H 1 6.889 0.020 . 2 . . . . 62 GLN HE21 . 16885 1 1280 . 2 2 62 62 GLN HE22 H 1 7.367 0.020 . 2 . . . . 62 GLN HE22 . 16885 1 1281 . 2 2 62 62 GLN HG2 H 1 2.283 0.020 . 2 . . . . 62 GLN HG2 . 16885 1 1282 . 2 2 62 62 GLN HG3 H 1 2.345 0.020 . 2 . . . . 62 GLN HG3 . 16885 1 1283 . 2 2 62 62 GLN CA C 13 53.516 0.300 . 1 . . . . 62 GLN CA . 16885 1 1284 . 2 2 62 62 GLN CB C 13 31.648 0.300 . 1 . . . . 62 GLN CB . 16885 1 1285 . 2 2 62 62 GLN CG C 13 33.272 0.300 . 1 . . . . 62 GLN CG . 16885 1 1286 . 2 2 62 62 GLN N N 15 122.562 0.300 . 1 . . . . 62 GLN N . 16885 1 1287 . 2 2 62 62 GLN NE2 N 15 110.161 0.300 . 1 . . . . 62 GLN NE2 . 16885 1 1288 . 2 2 63 63 LYS H H 1 8.548 0.020 . 1 . . . . 63 LYS HN . 16885 1 1289 . 2 2 63 63 LYS HA H 1 3.955 0.020 . 1 . . . . 63 LYS HA . 16885 1 1290 . 2 2 63 63 LYS HB2 H 1 1.892 0.020 . 2 . . . . 63 LYS HB2 . 16885 1 1291 . 2 2 63 63 LYS HB3 H 1 2.053 0.020 . 2 . . . . 63 LYS HB3 . 16885 1 1292 . 2 2 63 63 LYS HD2 H 1 1.734 0.020 . 2 . . . . 63 LYS QD . 16885 1 1293 . 2 2 63 63 LYS HD3 H 1 1.734 0.020 . 2 . . . . 63 LYS QD . 16885 1 1294 . 2 2 63 63 LYS HE2 H 1 3.029 0.020 . 2 . . . . 63 LYS QE . 16885 1 1295 . 2 2 63 63 LYS HE3 H 1 3.029 0.020 . 2 . . . . 63 LYS QE . 16885 1 1296 . 2 2 63 63 LYS HG2 H 1 1.490 0.020 . 2 . . . . 63 LYS QG . 16885 1 1297 . 2 2 63 63 LYS HG3 H 1 1.490 0.020 . 2 . . . . 63 LYS QG . 16885 1 1298 . 2 2 63 63 LYS CA C 13 57.875 0.300 . 1 . . . . 63 LYS CA . 16885 1 1299 . 2 2 63 63 LYS CB C 13 32.529 0.300 . 1 . . . . 63 LYS CB . 16885 1 1300 . 2 2 63 63 LYS CD C 13 29.753 0.300 . 1 . . . . 63 LYS CD . 16885 1 1301 . 2 2 63 63 LYS CE C 13 42.014 0.300 . 1 . . . . 63 LYS CE . 16885 1 1302 . 2 2 63 63 LYS CG C 13 23.890 0.300 . 1 . . . . 63 LYS CG . 16885 1 1303 . 2 2 63 63 LYS N N 15 118.229 0.300 . 1 . . . . 63 LYS N . 16885 1 1304 . 2 2 64 64 GLU H H 1 9.394 0.020 . 1 . . . . 64 GLU HN . 16885 1 1305 . 2 2 64 64 GLU HA H 1 3.362 0.020 . 1 . . . . 64 GLU HA . 16885 1 1306 . 2 2 64 64 GLU HB2 H 1 2.409 0.020 . 2 . . . . 64 GLU HB2 . 16885 1 1307 . 2 2 64 64 GLU HB3 H 1 2.553 0.020 . 2 . . . . 64 GLU HB3 . 16885 1 1308 . 2 2 64 64 GLU HG2 H 1 2.252 0.020 . 2 . . . . 64 GLU QG . 16885 1 1309 . 2 2 64 64 GLU HG3 H 1 2.252 0.020 . 2 . . . . 64 GLU QG . 16885 1 1310 . 2 2 64 64 GLU CA C 13 58.262 0.300 . 1 . . . . 64 GLU CA . 16885 1 1311 . 2 2 64 64 GLU CB C 13 25.926 0.300 . 1 . . . . 64 GLU CB . 16885 1 1312 . 2 2 64 64 GLU CG C 13 37.190 0.300 . 1 . . . . 64 GLU CG . 16885 1 1313 . 2 2 64 64 GLU N N 15 112.605 0.300 . 1 . . . . 64 GLU N . 16885 1 1314 . 2 2 65 65 SER H H 1 7.773 0.020 . 1 . . . . 65 SER HN . 16885 1 1315 . 2 2 65 65 SER HA H 1 4.614 0.020 . 1 . . . . 65 SER HA . 16885 1 1316 . 2 2 65 65 SER HB2 H 1 3.663 0.020 . 2 . . . . 65 SER HB2 . 16885 1 1317 . 2 2 65 65 SER HB3 H 1 3.933 0.020 . 2 . . . . 65 SER HB3 . 16885 1 1318 . 2 2 65 65 SER CA C 13 60.923 0.300 . 1 . . . . 65 SER CA . 16885 1 1319 . 2 2 65 65 SER CB C 13 64.989 0.300 . 1 . . . . 65 SER CB . 16885 1 1320 . 2 2 65 65 SER N N 15 112.800 0.300 . 1 . . . . 65 SER N . 16885 1 1321 . 2 2 66 66 THR H H 1 8.743 0.020 . 1 . . . . 66 THR HN . 16885 1 1322 . 2 2 66 66 THR HA H 1 5.302 0.020 . 1 . . . . 66 THR HA . 16885 1 1323 . 2 2 66 66 THR HB H 1 3.980 0.020 . 1 . . . . 66 THR HB . 16885 1 1324 . 2 2 66 66 THR HG21 H 1 0.873 0.020 . 1 . . . . 66 THR QG2 . 16885 1 1325 . 2 2 66 66 THR HG22 H 1 0.873 0.020 . 1 . . . . 66 THR QG2 . 16885 1 1326 . 2 2 66 66 THR HG23 H 1 0.873 0.020 . 1 . . . . 66 THR QG2 . 16885 1 1327 . 2 2 66 66 THR CA C 13 62.343 0.300 . 1 . . . . 66 THR CA . 16885 1 1328 . 2 2 66 66 THR CB C 13 70.295 0.300 . 1 . . . . 66 THR CB . 16885 1 1329 . 2 2 66 66 THR CG2 C 13 21.454 0.300 . 1 . . . . 66 THR CG2 . 16885 1 1330 . 2 2 66 66 THR N N 15 114.987 0.300 . 1 . . . . 66 THR N . 16885 1 1331 . 2 2 67 67 LEU H H 1 9.396 0.020 . 1 . . . . 67 LEU HN . 16885 1 1332 . 2 2 67 67 LEU HA H 1 4.988 0.020 . 1 . . . . 67 LEU HA . 16885 1 1333 . 2 2 67 67 LEU HB2 H 1 1.560 0.020 . 2 . . . . 67 LEU HB2 . 16885 1 1334 . 2 2 67 67 LEU HB3 H 1 1.653 0.020 . 2 . . . . 67 LEU HB3 . 16885 1 1335 . 2 2 67 67 LEU HD11 H 1 0.638 0.020 . 2 . . . . 67 LEU QD1 . 16885 1 1336 . 2 2 67 67 LEU HD12 H 1 0.638 0.020 . 2 . . . . 67 LEU QD1 . 16885 1 1337 . 2 2 67 67 LEU HD13 H 1 0.638 0.020 . 2 . . . . 67 LEU QD1 . 16885 1 1338 . 2 2 67 67 LEU HD21 H 1 0.683 0.020 . 2 . . . . 67 LEU QD2 . 16885 1 1339 . 2 2 67 67 LEU HD22 H 1 0.683 0.020 . 2 . . . . 67 LEU QD2 . 16885 1 1340 . 2 2 67 67 LEU HD23 H 1 0.683 0.020 . 2 . . . . 67 LEU QD2 . 16885 1 1341 . 2 2 67 67 LEU HG H 1 1.758 0.020 . 1 . . . . 67 LEU HG . 16885 1 1342 . 2 2 67 67 LEU CA C 13 53.746 0.300 . 1 . . . . 67 LEU CA . 16885 1 1343 . 2 2 67 67 LEU CB C 13 44.572 0.300 . 1 . . . . 67 LEU CB . 16885 1 1344 . 2 2 67 67 LEU CD1 C 13 25.426 0.300 . 2 . . . . 67 LEU CD1 . 16885 1 1345 . 2 2 67 67 LEU CD2 C 13 24.831 0.300 . 2 . . . . 67 LEU CD2 . 16885 1 1346 . 2 2 67 67 LEU CG C 13 29.689 0.300 . 1 . . . . 67 LEU CG . 16885 1 1347 . 2 2 67 67 LEU N N 15 125.642 0.300 . 1 . . . . 67 LEU N . 16885 1 1348 . 2 2 68 68 HIS H H 1 9.164 0.020 . 1 . . . . 68 HIS HN . 16885 1 1349 . 2 2 68 68 HIS HA H 1 5.544 0.020 . 1 . . . . 68 HIS HA . 16885 1 1350 . 2 2 68 68 HIS HB2 H 1 2.634 0.020 . 2 . . . . 68 HIS HB2 . 16885 1 1351 . 2 2 68 68 HIS HB3 H 1 2.845 0.020 . 2 . . . . 68 HIS HB3 . 16885 1 1352 . 2 2 68 68 HIS HD2 H 1 6.818 0.020 . 1 . . . . 68 HIS HD2 . 16885 1 1353 . 2 2 68 68 HIS HE1 H 1 7.586 0.020 . 1 . . . . 68 HIS HE1 . 16885 1 1354 . 2 2 68 68 HIS CA C 13 56.573 0.300 . 1 . . . . 68 HIS CA . 16885 1 1355 . 2 2 68 68 HIS CB C 13 32.816 0.300 . 1 . . . . 68 HIS CB . 16885 1 1356 . 2 2 68 68 HIS CD2 C 13 119.483 0.300 . 1 . . . . 68 HIS CD2 . 16885 1 1357 . 2 2 68 68 HIS CE1 C 13 138.173 0.300 . 1 . . . . 68 HIS CE1 . 16885 1 1358 . 2 2 68 68 HIS N N 15 116.015 0.300 . 1 . . . . 68 HIS N . 16885 1 1359 . 2 2 69 69 LEU H H 1 8.532 0.020 . 1 . . . . 69 LEU HN . 16885 1 1360 . 2 2 69 69 LEU HA H 1 5.310 0.020 . 1 . . . . 69 LEU HA . 16885 1 1361 . 2 2 69 69 LEU HB2 H 1 1.080 0.020 . 2 . . . . 69 LEU HB2 . 16885 1 1362 . 2 2 69 69 LEU HB3 H 1 1.476 0.020 . 2 . . . . 69 LEU HB3 . 16885 1 1363 . 2 2 69 69 LEU HD11 H 1 0.724 0.020 . 2 . . . . 69 LEU QD1 . 16885 1 1364 . 2 2 69 69 LEU HD12 H 1 0.724 0.020 . 2 . . . . 69 LEU QD1 . 16885 1 1365 . 2 2 69 69 LEU HD13 H 1 0.724 0.020 . 2 . . . . 69 LEU QD1 . 16885 1 1366 . 2 2 69 69 LEU HD21 H 1 0.821 0.020 . 2 . . . . 69 LEU QD2 . 16885 1 1367 . 2 2 69 69 LEU HD22 H 1 0.821 0.020 . 2 . . . . 69 LEU QD2 . 16885 1 1368 . 2 2 69 69 LEU HD23 H 1 0.821 0.020 . 2 . . . . 69 LEU QD2 . 16885 1 1369 . 2 2 69 69 LEU HG H 1 1.330 0.020 . 1 . . . . 69 LEU HG . 16885 1 1370 . 2 2 69 69 LEU CA C 13 53.244 0.300 . 1 . . . . 69 LEU CA . 16885 1 1371 . 2 2 69 69 LEU CB C 13 44.851 0.300 . 1 . . . . 69 LEU CB . 16885 1 1372 . 2 2 69 69 LEU CD1 C 13 26.042 0.300 . 2 . . . . 69 LEU CD1 . 16885 1 1373 . 2 2 69 69 LEU CD2 C 13 23.648 0.300 . 2 . . . . 69 LEU CD2 . 16885 1 1374 . 2 2 69 69 LEU CG C 13 27.739 0.300 . 1 . . . . 69 LEU CG . 16885 1 1375 . 2 2 69 69 LEU N N 15 121.946 0.300 . 1 . . . . 69 LEU N . 16885 1 1376 . 2 2 70 70 VAL H H 1 8.982 0.020 . 1 . . . . 70 VAL HN . 16885 1 1377 . 2 2 70 70 VAL HA H 1 4.374 0.020 . 1 . . . . 70 VAL HA . 16885 1 1378 . 2 2 70 70 VAL HB H 1 1.837 0.020 . 1 . . . . 70 VAL HB . 16885 1 1379 . 2 2 70 70 VAL HG11 H 1 0.876 0.020 . 2 . . . . 70 VAL QG1 . 16885 1 1380 . 2 2 70 70 VAL HG12 H 1 0.876 0.020 . 2 . . . . 70 VAL QG1 . 16885 1 1381 . 2 2 70 70 VAL HG13 H 1 0.876 0.020 . 2 . . . . 70 VAL QG1 . 16885 1 1382 . 2 2 70 70 VAL HG21 H 1 1.024 0.020 . 2 . . . . 70 VAL QG2 . 16885 1 1383 . 2 2 70 70 VAL HG22 H 1 1.024 0.020 . 2 . . . . 70 VAL QG2 . 16885 1 1384 . 2 2 70 70 VAL HG23 H 1 1.024 0.020 . 2 . . . . 70 VAL QG2 . 16885 1 1385 . 2 2 70 70 VAL CA C 13 60.771 0.300 . 1 . . . . 70 VAL CA . 16885 1 1386 . 2 2 70 70 VAL CB C 13 34.815 0.300 . 1 . . . . 70 VAL CB . 16885 1 1387 . 2 2 70 70 VAL CG1 C 13 21.805 0.300 . 2 . . . . 70 VAL CG1 . 16885 1 1388 . 2 2 70 70 VAL CG2 C 13 21.821 0.300 . 2 . . . . 70 VAL CG2 . 16885 1 1389 . 2 2 70 70 VAL N N 15 124.540 0.300 . 1 . . . . 70 VAL N . 16885 1 1390 . 2 2 71 71 LEU H H 1 9.082 0.020 . 1 . . . . 71 LEU HN . 16885 1 1391 . 2 2 71 71 LEU HA H 1 4.968 0.020 . 1 . . . . 71 LEU HA . 16885 1 1392 . 2 2 71 71 LEU HB2 H 1 1.598 0.020 . 2 . . . . 71 LEU HB2 . 16885 1 1393 . 2 2 71 71 LEU HB3 H 1 1.769 0.020 . 2 . . . . 71 LEU HB3 . 16885 1 1394 . 2 2 71 71 LEU HD11 H 1 0.851 0.020 . 2 . . . . 71 LEU QD1 . 16885 1 1395 . 2 2 71 71 LEU HD12 H 1 0.851 0.020 . 2 . . . . 71 LEU QD1 . 16885 1 1396 . 2 2 71 71 LEU HD13 H 1 0.851 0.020 . 2 . . . . 71 LEU QD1 . 16885 1 1397 . 2 2 71 71 LEU HD21 H 1 0.977 0.020 . 2 . . . . 71 LEU QD2 . 16885 1 1398 . 2 2 71 71 LEU HD22 H 1 0.977 0.020 . 2 . . . . 71 LEU QD2 . 16885 1 1399 . 2 2 71 71 LEU HD23 H 1 0.977 0.020 . 2 . . . . 71 LEU QD2 . 16885 1 1400 . 2 2 71 71 LEU HG H 1 1.809 0.020 . 1 . . . . 71 LEU HG . 16885 1 1401 . 2 2 71 71 LEU CA C 13 54.618 0.300 . 1 . . . . 71 LEU CA . 16885 1 1402 . 2 2 71 71 LEU CB C 13 41.706 0.300 . 1 . . . . 71 LEU CB . 16885 1 1403 . 2 2 71 71 LEU CD1 C 13 23.631 0.300 . 2 . . . . 71 LEU CD1 . 16885 1 1404 . 2 2 71 71 LEU CD2 C 13 25.171 0.300 . 2 . . . . 71 LEU CD2 . 16885 1 1405 . 2 2 71 71 LEU CG C 13 27.774 0.300 . 1 . . . . 71 LEU CG . 16885 1 1406 . 2 2 71 71 LEU N N 15 125.441 0.300 . 1 . . . . 71 LEU N . 16885 1 1407 . 2 2 72 72 ARG H H 1 8.665 0.020 . 1 . . . . 72 ARG HN . 16885 1 1408 . 2 2 72 72 ARG HA H 1 4.178 0.020 . 1 . . . . 72 ARG HA . 16885 1 1409 . 2 2 72 72 ARG HB2 H 1 1.587 0.020 . 2 . . . . 72 ARG HB2 . 16885 1 1410 . 2 2 72 72 ARG HB3 H 1 1.790 0.020 . 2 . . . . 72 ARG HB3 . 16885 1 1411 . 2 2 72 72 ARG HD2 H 1 3.230 0.020 . 2 . . . . 72 ARG QD . 16885 1 1412 . 2 2 72 72 ARG HD3 H 1 3.230 0.020 . 2 . . . . 72 ARG QD . 16885 1 1413 . 2 2 72 72 ARG HE H 1 7.160 0.020 . 1 . . . . 72 ARG HE . 16885 1 1414 . 2 2 72 72 ARG HG2 H 1 1.547 0.020 . 2 . . . . 72 ARG QG . 16885 1 1415 . 2 2 72 72 ARG HG3 H 1 1.547 0.020 . 2 . . . . 72 ARG QG . 16885 1 1416 . 2 2 72 72 ARG CA C 13 56.602 0.300 . 1 . . . . 72 ARG CA . 16885 1 1417 . 2 2 72 72 ARG CB C 13 31.198 0.300 . 1 . . . . 72 ARG CB . 16885 1 1418 . 2 2 72 72 ARG CD C 13 43.285 0.300 . 1 . . . . 72 ARG CD . 16885 1 1419 . 2 2 72 72 ARG CG C 13 28.359 0.300 . 1 . . . . 72 ARG CG . 16885 1 1420 . 2 2 72 72 ARG N N 15 120.040 0.300 . 1 . . . . 72 ARG N . 16885 1 1421 . 2 2 72 72 ARG NE N 15 81.696 0.300 . 1 . . . . 72 ARG NE . 16885 1 1422 . 2 2 73 73 LEU H H 1 8.660 0.020 . 1 . . . . 73 LEU HN . 16885 1 1423 . 2 2 73 73 LEU HA H 1 4.314 0.020 . 1 . . . . 73 LEU HA . 16885 1 1424 . 2 2 73 73 LEU HB2 H 1 1.527 0.020 . 2 . . . . 73 LEU HB2 . 16885 1 1425 . 2 2 73 73 LEU HB3 H 1 1.643 0.020 . 2 . . . . 73 LEU HB3 . 16885 1 1426 . 2 2 73 73 LEU HD11 H 1 0.835 0.020 . 2 . . . . 73 LEU QD1 . 16885 1 1427 . 2 2 73 73 LEU HD12 H 1 0.835 0.020 . 2 . . . . 73 LEU QD1 . 16885 1 1428 . 2 2 73 73 LEU HD13 H 1 0.835 0.020 . 2 . . . . 73 LEU QD1 . 16885 1 1429 . 2 2 73 73 LEU HD21 H 1 0.870 0.020 . 2 . . . . 73 LEU QD2 . 16885 1 1430 . 2 2 73 73 LEU HD22 H 1 0.870 0.020 . 2 . . . . 73 LEU QD2 . 16885 1 1431 . 2 2 73 73 LEU HD23 H 1 0.870 0.020 . 2 . . . . 73 LEU QD2 . 16885 1 1432 . 2 2 73 73 LEU HG H 1 1.643 0.020 . 1 . . . . 73 LEU HG . 16885 1 1433 . 2 2 73 73 LEU CA C 13 55.067 0.300 . 1 . . . . 73 LEU CA . 16885 1 1434 . 2 2 73 73 LEU CB C 13 41.967 0.300 . 1 . . . . 73 LEU CB . 16885 1 1435 . 2 2 73 73 LEU CD1 C 13 23.341 0.300 . 2 . . . . 73 LEU CD1 . 16885 1 1436 . 2 2 73 73 LEU CD2 C 13 25.243 0.300 . 2 . . . . 73 LEU CD2 . 16885 1 1437 . 2 2 73 73 LEU CG C 13 27.123 0.300 . 1 . . . . 73 LEU CG . 16885 1 1438 . 2 2 73 73 LEU N N 15 121.484 0.300 . 1 . . . . 73 LEU N . 16885 1 1439 . 2 2 74 74 ARG H H 1 8.554 0.020 . 1 . . . . 74 ARG HN . 16885 1 1440 . 2 2 74 74 ARG HA H 1 4.317 0.020 . 1 . . . . 74 ARG HA . 16885 1 1441 . 2 2 74 74 ARG HB2 H 1 1.783 0.020 . 2 . . . . 74 ARG HB2 . 16885 1 1442 . 2 2 74 74 ARG HB3 H 1 1.867 0.020 . 2 . . . . 74 ARG HB3 . 16885 1 1443 . 2 2 74 74 ARG HD2 H 1 3.209 0.020 . 2 . . . . 74 ARG QD . 16885 1 1444 . 2 2 74 74 ARG HD3 H 1 3.209 0.020 . 2 . . . . 74 ARG QD . 16885 1 1445 . 2 2 74 74 ARG HE H 1 7.317 0.020 . 1 . . . . 74 ARG HE . 16885 1 1446 . 2 2 74 74 ARG HG2 H 1 1.647 0.020 . 2 . . . . 74 ARG QG . 16885 1 1447 . 2 2 74 74 ARG HG3 H 1 1.647 0.020 . 2 . . . . 74 ARG QG . 16885 1 1448 . 2 2 74 74 ARG CA C 13 56.394 0.300 . 1 . . . . 74 ARG CA . 16885 1 1449 . 2 2 74 74 ARG CB C 13 30.859 0.300 . 1 . . . . 74 ARG CB . 16885 1 1450 . 2 2 74 74 ARG CD C 13 43.286 0.300 . 1 . . . . 74 ARG CD . 16885 1 1451 . 2 2 74 74 ARG CG C 13 27.030 0.300 . 1 . . . . 74 ARG CG . 16885 1 1452 . 2 2 74 74 ARG N N 15 119.586 0.300 . 1 . . . . 74 ARG N . 16885 1 1453 . 2 2 74 74 ARG NE N 15 82.088 0.300 . 1 . . . . 74 ARG NE . 16885 1 1454 . 2 2 75 75 GLY H H 1 8.581 0.020 . 1 . . . . 75 GLY HN . 16885 1 1455 . 2 2 75 75 GLY HA2 H 1 3.972 0.020 . 2 . . . . 75 GLY QA . 16885 1 1456 . 2 2 75 75 GLY HA3 H 1 3.972 0.020 . 2 . . . . 75 GLY QA . 16885 1 1457 . 2 2 75 75 GLY CA C 13 45.182 0.300 . 1 . . . . 75 GLY CA . 16885 1 1458 . 2 2 75 75 GLY N N 15 108.783 0.300 . 1 . . . . 75 GLY N . 16885 1 1459 . 2 2 76 76 GLY H H 1 8.047 0.020 . 1 . . . . 76 GLY HN . 16885 1 1460 . 2 2 76 76 GLY HA2 H 1 3.753 0.020 . 2 . . . . 76 GLY HA1 . 16885 1 1461 . 2 2 76 76 GLY HA3 H 1 3.804 0.020 . 2 . . . . 76 GLY HA2 . 16885 1 1462 . 2 2 76 76 GLY CA C 13 45.972 0.300 . 1 . . . . 76 GLY CA . 16885 1 1463 . 2 2 76 76 GLY N N 15 112.764 0.300 . 1 . . . . 76 GLY N . 16885 1 stop_ save_