data_17940 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 17940 _Entry.Title ; 1H, 13C and 15N backbone resonance assignment of the activated p38 mitogen-activated protein kinase ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2011-09-15 _Entry.Accession_date 2011-09-15 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _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 Gerd Nielsen . . . 17940 2 Harald Schwalbe . . . 17940 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'BMRZ, Frankfurt am Main' . 17940 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 17940 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 591 17940 '15N chemical shifts' 188 17940 '1H chemical shifts' 188 17940 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 . . 2012-02-14 2011-09-15 update BMRB 'update entry citation' 17940 1 . . 2011-10-24 2011-09-15 original author 'original release' 17940 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 6468 'mitogen-activated protein kinase p38 alpha' 17940 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 17940 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22012687 _Citation.Full_citation . _Citation.Title 'NMR spectroscopic investigations of the activated p38 mitogen-activated protein kinase.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Chembiochem _Citation.Journal_name_full 'Chembiochem : a European journal of chemical biology' _Citation.Journal_volume 12 _Citation.Journal_issue 17 _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 2599 _Citation.Page_last 2607 _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 Gerd Nielsen . . . 17940 1 2 Harald Schwalbe . . . 17940 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID activation 17940 1 assignment 17940 1 NMR 17940 1 p38 17940 1 phosphorylation 17940 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 17940 _Assembly.ID 1 _Assembly.Name p38alpha _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 40211 _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 p38alpha 1 $p38alpha A . yes native no no . . . 17940 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_p38alpha _Entity.Sf_category entity _Entity.Sf_framecode p38alpha _Entity.Entry_ID 17940 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name p38alpha _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; NSQERPTFYRQELNKTIWEV PERYQNLSPVGSGAYGSVCA AFDTKTGHRVAVKKLSRPFQ SIIHAKRTYRELRLLKHMKH ENVIGLLDVFTPARSLEEFN DVYLVTHLMGADLNNIVKCQ KLTDDHVQFLIYQILRGLKY IHSADIIHRDLKPSNLAVNE DCELKILDFGLARHTDDEMT GYVATRWYRAPEIMLNWMHY NQTVDIWSVGCIMAELLTGR TLFPGTDHIDQLKLILRLVG TPGAELLKKISSESARNYIQ SLAQMPKMNFANVFIGANPL AVDLLEKMLVLDSDKRITAA QALAHAYFAQYHDPDDEPVA DPYDQSFESRDLLIDEWKSL TYDEVISFV ; _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 349 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 17471 . p38_alpha . . . . . 100.00 352 99.14 99.14 0.00e+00 . . . . 17940 1 2 no BMRB 19930 . Non-phosphorylated_human_p38_alpha_(apo) . . . . . 100.00 367 99.14 99.43 0.00e+00 . . . . 17940 1 3 no BMRB 19934 . Dual-phosphorylated_human_p38_alpha_(apo) . . . . . 100.00 367 98.57 98.85 0.00e+00 . . . . 17940 1 4 no BMRB 19935 . Dual-phosphorylated_human_p38_alpha . . . . . 100.00 367 98.57 98.85 0.00e+00 . . . . 17940 1 5 no BMRB 19936 . dual-phosphorylated_human_p38_alpha_(apo) . . . . . 100.00 367 98.57 98.85 0.00e+00 . . . . 17940 1 6 no BMRB 19937 . dual-phosphorylated_human_p38_alpha_(apo) . . . . . 100.00 367 98.57 98.85 0.00e+00 . . . . 17940 1 7 no PDB 1A9U . "The Complex Structure Of The Map Kinase P38SB203580" . . . . . 99.71 379 99.43 99.43 0.00e+00 . . . . 17940 1 8 no PDB 1BL6 . "The Complex Structure Of The Map Kinase P38SB216995" . . . . . 99.71 379 99.43 99.43 0.00e+00 . . . . 17940 1 9 no PDB 1BL7 . "The Complex Structure Of The Map Kinase P38SB220025" . . . . . 99.71 379 99.43 99.43 0.00e+00 . . . . 17940 1 10 no PDB 1BMK . "The Complex Structure Of The Map Kinase P38SB218655" . . . . . 99.71 379 100.00 100.00 0.00e+00 . . . . 17940 1 11 no PDB 1DI9 . "The Structure Of P38 Mitogen-Activated Protein Kinase In Complex With 4-[3-Methylsulfanylanilino]-6,7- Dimethoxyquinazoline" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 12 no PDB 1IAN . "Human P38 Map Kinase Inhibitor Complex" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 13 no PDB 1KV1 . "P38 Map Kinase In Complex With Inhibitor 1" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 14 no PDB 1KV2 . "Human P38 Map Kinase In Complex With Birb 796" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 15 no PDB 1LEW . "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Nuclear Substrate Mef2a" . . . . . 99.71 360 100.00 100.00 0.00e+00 . . . . 17940 1 16 no PDB 1LEZ . "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Activator Mkk3b" . . . . . 99.71 360 100.00 100.00 0.00e+00 . . . . 17940 1 17 no PDB 1M7Q . "Crystal Structure Of P38 Map Kinase In Complex With A Dihydroquinazolinone Inhibitor" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 18 no PDB 1OUK . "The Structure Of P38 Alpha In Complex With A Pyridinylimidazole Inhibitor" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 19 no PDB 1OUY . "The Structure Of P38 Alpha In Complex With A Dihydropyrido- Pyrimidine Inhibitor" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 20 no PDB 1OVE . "The Structure Of P38 Alpha In Complex With A Dihydroquinolinone" . . . . . 99.71 366 99.14 99.14 0.00e+00 . . . . 17940 1 21 no PDB 1OZ1 . "P38 Mitogen-Activated Kinase In Complex With 4-Azaindole Inhibitor" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 22 no PDB 1P38 . "The Structure Of The Map Kinase P38 At 2.1 Angstoms Resolution" . . . . . 99.71 379 100.00 100.00 0.00e+00 . . . . 17940 1 23 no PDB 1R39 . "The Structure Of P38alpha" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 24 no PDB 1R3C . "The Structure Of P38alpha C162s Mutant" . . . . . 99.71 366 99.14 99.14 0.00e+00 . . . . 17940 1 25 no PDB 1W7H . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 26 no PDB 1W82 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 27 no PDB 1W83 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 28 no PDB 1W84 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 29 no PDB 1WBN . "Fragment Based P38 Inhibitors" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 30 no PDB 1WBO . "Fragment Based P38 Inhibitors" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 31 no PDB 1WBS . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 32 no PDB 1WBT . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-based Lead Generation." . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 33 no PDB 1WBV . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 34 no PDB 1WBW . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 35 no PDB 1WFC . "Structure Of Apo, Unphosphorylated, P38 Mitogen Activated Protein Kinase P38 (P38 Map Kinase) The Mammalian Homologue Of The Ye" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 36 no PDB 1YQJ . "Crystal Structure Of P38 Alpha In Complex With A Selective Pyridazine Inhibitor" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 37 no PDB 1YW2 . "Mutated Mus Musculus P38 Kinase (Mp38)" . . . . . 99.71 360 99.43 99.71 0.00e+00 . . . . 17940 1 38 no PDB 1YWR . "Crystal Structure Analysis Of Inactive P38 Kinase Domain In Complex With A Monocyclic Pyrazolone Inhibitor" . . . . . 99.71 360 99.14 99.43 0.00e+00 . . . . 17940 1 39 no PDB 1ZYJ . "Human P38 Map Kinase In Complex With Inhibitor 1a" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 40 no PDB 1ZZ2 . "Two Classes Of P38alpha Map Kinase Inhibitors Having A Common Diphenylether Core But Exhibiting Divergent Binding Modes" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 41 no PDB 1ZZL . "Crystal Structure Of P38 With Triazolopyridine" . . . . . 99.14 351 99.42 99.42 0.00e+00 . . . . 17940 1 42 no PDB 2BAJ . "P38alpha Bound To Pyrazolourea" . . . . . 100.00 365 99.14 99.43 0.00e+00 . . . . 17940 1 43 no PDB 2BAK . "P38alpha Map Kinase Bound To Mpaq" . . . . . 100.00 365 99.14 99.43 0.00e+00 . . . . 17940 1 44 no PDB 2BAL . "P38alpha Map Kinase Bound To Pyrazoloamine" . . . . . 100.00 365 98.85 99.14 0.00e+00 . . . . 17940 1 45 no PDB 2BAQ . "P38alpha Bound To Ro3201195" . . . . . 100.00 365 98.57 99.14 0.00e+00 . . . . 17940 1 46 no PDB 2EWA . "Dual Binding Mode Of Pyridinylimidazole To Map Kinase P38" . . . . . 99.71 379 99.43 99.43 0.00e+00 . . . . 17940 1 47 no PDB 2FSL . "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-A" . . . . . 100.00 367 98.57 98.85 0.00e+00 . . . . 17940 1 48 no PDB 2FSM . "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-B" . . . . . 100.00 367 98.57 98.85 0.00e+00 . . . . 17940 1 49 no PDB 2FSO . "Mitogen Activated Protein Kinase P38alpha (D176a) Activating Mutant" . . . . . 100.00 367 98.85 99.14 0.00e+00 . . . . 17940 1 50 no PDB 2FST . "Mitogen Activated Protein Kinase P38alpha (d176a+f327l) Activating Mutant" . . . . . 100.00 367 98.57 98.85 0.00e+00 . . . . 17940 1 51 no PDB 2GFS . "P38 Kinase Crystal Structure In Complex With Ro3201195" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 52 no PDB 2GHL . "Mutant Mus Musculus P38 Kinase Domain In Complex With Inhibitor Pg-874743" . . . . . 98.85 348 99.42 99.71 0.00e+00 . . . . 17940 1 53 no PDB 2GHM . "Mutated Map Kinase P38 (Mus Musculus) In Complex With Inhbitor Pg-895449" . . . . . 98.85 348 99.42 99.71 0.00e+00 . . . . 17940 1 54 no PDB 2GTM . "Mutated Mouse P38 Map Kinase Domain In Complex With Inhibitor Pg-892579" . . . . . 98.85 348 100.00 100.00 0.00e+00 . . . . 17940 1 55 no PDB 2GTN . "Mutated Map Kinase P38 (mus Musculus) In Complex With Inhbitor Pg-951717" . . . . . 98.85 348 100.00 100.00 0.00e+00 . . . . 17940 1 56 no PDB 2I0H . "The Structure Of P38alpha In Complex With An Arylpyridazinone" . . . . . 99.71 366 99.14 99.14 0.00e+00 . . . . 17940 1 57 no PDB 2LGC . "Joint Nmr And X-Ray Refinement Reveals The Structure Of A Novel Dibenzo[a,D]cycloheptenone InhibitorP38 MAP KINASE COMPLEX IN S" . . . . . 99.71 359 99.43 99.43 0.00e+00 . . . . 17940 1 58 no PDB 2NPQ . "A Novel Lipid Binding Site In The P38 Alpha Map Kinase" . . . . . 100.00 367 99.14 99.43 0.00e+00 . . . . 17940 1 59 no PDB 2OKR . "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 60 no PDB 2ONL . "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 61 no PDB 2OZA . "Structure Of P38alpha Complex" . . . . . 100.00 366 99.71 100.00 0.00e+00 . . . . 17940 1 62 no PDB 2PUU . "Crystal Structure Of P38 Complex With 1-(5-Tert-Butyl-2-P- Tolyl-2h-Pyrazol-3-Yl)-3-[4-(6-Morpholin-4-Ylmethyl- Pyridin-3-Yl)na" . . . . . 98.85 348 99.42 99.42 0.00e+00 . . . . 17940 1 63 no PDB 2QD9 . "P38 Alpha Map Kinase Inhibitor Based On Heterobicyclic Scaffolds" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 64 no PDB 2RG5 . "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11b" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 65 no PDB 2RG6 . "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11j" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 66 no PDB 2Y8O . "Crystal Structure Of Human P38alpha Complexed With A Mapk Docking Peptide" . . . . . 99.71 362 99.14 99.14 0.00e+00 . . . . 17940 1 67 no PDB 2YIS . "Triazolopyridine Inhibitors Of P38 Kinase." . . . . . 99.71 359 99.43 99.43 0.00e+00 . . . . 17940 1 68 no PDB 2YIW . "Triazolopyridine Inhibitors Of P38 Kinase" . . . . . 99.71 359 99.43 99.43 0.00e+00 . . . . 17940 1 69 no PDB 2YIX . "Triazolopyridine Inhibitors Of P38" . . . . . 99.14 351 99.42 99.42 0.00e+00 . . . . 17940 1 70 no PDB 2ZAZ . "Crystal Structure Of P38 In Complex With 4-Anilino Quinoline Inhibitor" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 71 no PDB 2ZB0 . "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 72 no PDB 2ZB1 . "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 73 no PDB 3BV2 . "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 30" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 74 no PDB 3BV3 . "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 2" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 75 no PDB 3BX5 . "P38 Alpha Map Kinase Complexed With Bms-640994" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 76 no PDB 3C5U . "P38 Alpha Map Kinase Complexed With A Benzothiazole Based Inhibitor" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 77 no PDB 3CTQ . "Structure Of Map Kinase P38 In Complex With A 1-O-Tolyl-1,2, 3-Triazole-4-Carboxamide" . . . . . 98.85 348 99.42 99.42 0.00e+00 . . . . 17940 1 78 no PDB 3D7Z . "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 79 no PDB 3D83 . "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" . . . . . 99.71 360 98.85 98.85 0.00e+00 . . . . 17940 1 80 no PDB 3DS6 . "P38 Complex With A Phthalazine Inhibitor" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 81 no PDB 3DT1 . "P38 Complexed With A Quinazoline Inhibitor" . . . . . 99.71 383 99.43 99.43 0.00e+00 . . . . 17940 1 82 no PDB 3E92 . "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" . . . . . 99.71 371 99.14 99.14 0.00e+00 . . . . 17940 1 83 no PDB 3E93 . "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" . . . . . 99.71 371 99.14 99.14 0.00e+00 . . . . 17940 1 84 no PDB 3FC1 . "Crystal Structure Of P38 Kinase Bound To Pyrimido-Pyridazinone Inhibitor" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 85 no PDB 3FI4 . "P38 Kinase Crystal Structure In Complex With Ro4499" . . . . . 99.71 372 99.14 99.43 0.00e+00 . . . . 17940 1 86 no PDB 3FKL . "P38 Kinase Crystal Structure In Complex With Ro9552" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 87 no PDB 3FKN . "P38 Kinase Crystal Structure In Complex With Ro7125" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 88 no PDB 3FKO . "P38 Kinase Crystal Structure In Complex With Ro3668" . . . . . 99.71 372 99.14 99.43 0.00e+00 . . . . 17940 1 89 no PDB 3FL4 . "P38 Kinase Crystal Structure In Complex With Ro5634" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 90 no PDB 3FLN . "P38 Kinase Crystal Structure In Complex With R1487" . . . . . 99.71 372 99.14 99.43 0.00e+00 . . . . 17940 1 91 no PDB 3FLQ . "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-((S)-2-Methanesulfonyl-1-Methyl- Ethylamino)-8-Methyl-" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 92 no PDB 3FLS . "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-((R)-2-Methanesulfonyl-1-Methyl- Ethylamino)-8-Methyl-" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 93 no PDB 3FLW . "P38 Kinase Crystal Structure In Complex With Pamapimod" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 94 no PDB 3FLY . "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-Isopropylamino-8-Methyl-8h-Pyrido[2,3- D]pyrimidin-7-O" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 95 no PDB 3FLZ . "P38 Kinase Crystal Structure In Complex With 8-Methyl-6-Phenoxy-2- (Tetrahydro-Pyran-4-Ylamino)-8h-Pyrido[2,3-D]pyrimidin-7-One" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 96 no PDB 3FMH . "P38 Kinase Crystal Structure In Complex With 6-(2,4-Difluoro-Phenoxy)- 8-Methyl-2-((R)-1-Methyl-2-Tetrazol-2-Yl-Ethylamino)-8h-" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 97 no PDB 3FMJ . "P38 Kinase Crystal Structure In Complex With 4-(5-Methyl-3-Phenyl- Isoxazol-4-Yl)-Pyrimidin-2-Ylamine" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 98 no PDB 3FMK . "P38 Kinase Crystal Structure In Complex With 6-(2,4-Difluoro-Phenoxy)- 8-Methyl-2-((S)-1-Methyl-2-Tetrazol-2-Yl-Ethylamino)-8h-" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 99 no PDB 3FML . "P38 Kinase Crystal Structure In Complex With Ro6224" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 100 no PDB 3FMM . "P38 Kinase Crystal Structure In Complex With Ro6226" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 101 no PDB 3FMN . "P38 Kinase Crystal Structure In Complex With Ro2530" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 102 no PDB 3FSF . "P38 Kinase Crystal Structure In Complex With 3-(2,6- Dichloro-Phenyl)-7-[4-(2-Diethylamino-Ethoxy)-Phenylamino]- 1-Methyl-3,4-D" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 103 no PDB 3FSK . "P38 Kinase Crystal Structure In Complex With Ro6257" . . . . . 99.71 372 99.43 99.43 0.00e+00 . . . . 17940 1 104 no PDB 3GC7 . "The Structure Of P38alpha In Complex With A Dihydroquinazolinone" . . . . . 99.71 366 99.14 99.14 0.00e+00 . . . . 17940 1 105 no PDB 3GCP . "Human P38 Map Kinase In Complex With Sb203580" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 106 no PDB 3GCQ . "Human P38 Map Kinase In Complex With Rl45" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 107 no PDB 3GCS . "Human P38 Map Kinase In Complex With Sorafenib" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 108 no PDB 3GCU . "Human P38 Map Kinase In Complex With Rl48" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 109 no PDB 3GCV . "Human P38 Map Kinase In Complex With Rl62" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 110 no PDB 3GFE . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 111 no PDB 3GI3 . "Crystal Structure Of A N-Phenyl-N'-Naphthylurea Analog In Complex With P38 Map Kinase" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 112 no PDB 3HA8 . "The Complex Structure Of The Map Kinase P38COMPOUND 14B" . . . . . 99.71 379 99.43 99.43 0.00e+00 . . . . 17940 1 113 no PDB 3HEC . "P38 In Complex With Imatinib" . . . . . 98.85 348 99.42 99.42 0.00e+00 . . . . 17940 1 114 no PDB 3HEG . "P38 In Complex With Sorafenib" . . . . . 98.85 348 99.42 99.42 0.00e+00 . . . . 17940 1 115 no PDB 3HL7 . "Crystal Structure Of Human P38alpha Complexed With Sd-0006" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 116 no PDB 3HLL . "Crystal Structure Of Human P38alpha Complexed With Ph-797804" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 117 no PDB 3HP2 . "Crystal Structure Of Human P38alpha Complexed With A Pyridinone Compound" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 118 no PDB 3HP5 . "Crystal Structure Of Human P38alpha Complexed With A Pyrimidopyridazinone Compound" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 119 no PDB 3HRB . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 99.71 359 99.43 99.43 0.00e+00 . . . . 17940 1 120 no PDB 3HUB . "Human P38 Map Kinase In Complex With Scios-469" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 121 no PDB 3HUC . "Human P38 Map Kinase In Complex With Rl40" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 122 no PDB 3HV3 . "Human P38 Map Kinase In Complex With Rl49" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 123 no PDB 3HV4 . "Human P38 Map Kinase In Complex With Rl51" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 124 no PDB 3HV5 . "Human P38 Map Kinase In Complex With Rl24" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 125 no PDB 3HV6 . "Human P38 Map Kinase In Complex With Rl39" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 126 no PDB 3HV7 . "Human P38 Map Kinase In Complex With Rl38" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 127 no PDB 3HVC . "Crystal Structure Of Human P38alpha Map Kinase" . . . . . 99.71 362 99.43 99.43 0.00e+00 . . . . 17940 1 128 no PDB 3IPH . "Crystal Structure Of P38 In Complex With A Biphenylamide Inhibitor" . . . . . 99.71 360 98.85 98.85 0.00e+00 . . . . 17940 1 129 no PDB 3ITZ . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridazine Inhibitor" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 130 no PDB 3IW5 . "Human P38 Map Kinase In Complex With An Indole Derivative" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 131 no PDB 3IW6 . "Human P38 Map Kinase In Complex With A Benzylpiperazin- Pyrrol" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 132 no PDB 3IW7 . "Human P38 Map Kinase In Complex With An Imidazo-Pyridine" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 133 no PDB 3IW8 . "Structure Of Inactive Human P38 Map Kinase In Complex With A Thiazole-Urea" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 134 no PDB 3K3I . "P38alpha Bound To Novel Dgf-Out Compound Pf-00215955" . . . . . 98.85 350 99.42 99.42 0.00e+00 . . . . 17940 1 135 no PDB 3K3J . "P38alpha Bound To Novel Dfg-Out Compound Pf-00416121" . . . . . 99.71 362 99.43 99.43 0.00e+00 . . . . 17940 1 136 no PDB 3KF7 . "Crystal Structure Of Human P38alpha Complexed With A Triazolopyrimidine Compound" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 137 no PDB 3KQ7 . "Structure Of Human P38alpha With N-[4-Methyl-3-(6-{[2-(1- Methylpyrrolidin-2-Yl)ethyl]amino}pyridine-3-Amido)phenyl]- 2-(Morpho" . . . . . 99.71 380 99.43 99.43 0.00e+00 . . . . 17940 1 138 no PDB 3L8S . "Human P38 Map Kinase In Complex With Cp-547632" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 139 no PDB 3L8X . "P38 Alpha Kinase Complexed With A Pyrazolo-Pyrimidine Based Inhibitor" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 140 no PDB 3LFA . "Human P38 Map Kinase In Complex With Dasatinib" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 141 no PDB 3LFB . "Human P38 Map Kinase In Complex With Rl98" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 142 no PDB 3LFC . "Human P38 Map Kinase In Complex With Rl99" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 143 no PDB 3LFD . "Human P38 Map Kinase In Complex With Rl113" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 144 no PDB 3LFE . "Human P38 Map Kinase In Complex With Rl116" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 145 no PDB 3LFF . "Human P38 Map Kinase In Complex With Rl166" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 146 no PDB 3LHJ . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor." . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 147 no PDB 3MGY . "Mutagenesis Of P38 Map Kinase Eshtablishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out " . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 148 no PDB 3MH0 . "Mutagenesis Of P38 Map Kinase Eshtablishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out " . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 149 no PDB 3MH1 . "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 150 no PDB 3MH2 . "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" . . . . . 99.71 360 99.14 99.43 0.00e+00 . . . . 17940 1 151 no PDB 3MH3 . "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 152 no PDB 3MPA . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 153 no PDB 3MPT . "Crystal Structure Of P38 Kinase In Complex With A Pyrrole-2- Carboxamide Inhibitor" . . . . . 99.71 371 99.43 99.43 0.00e+00 . . . . 17940 1 154 no PDB 3MVL . "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7k" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 155 no PDB 3MVM . "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7v" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 156 no PDB 3MW1 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 99.71 359 99.43 99.43 0.00e+00 . . . . 17940 1 157 no PDB 3NEW . "P38-Alpha Complexed With Compound 10" . . . . . 99.71 366 99.14 99.14 0.00e+00 . . . . 17940 1 158 no PDB 3NNU . "Crystal Structure Of P38 Alpha In Complex With Dp1376" . . . . . 99.71 354 99.43 99.43 0.00e+00 . . . . 17940 1 159 no PDB 3NNV . "Crystal Structure Of P38 Alpha In Complex With Dp437" . . . . . 99.71 354 99.43 99.43 0.00e+00 . . . . 17940 1 160 no PDB 3NNW . "Crystal Structure Of P38 Alpha In Complex With Dp802" . . . . . 99.71 354 99.43 99.43 0.00e+00 . . . . 17940 1 161 no PDB 3NNX . "Crystal Structure Of Phosphorylated P38 Alpha In Complex With Dp802" . . . . . 99.71 354 99.14 99.14 0.00e+00 . . . . 17940 1 162 no PDB 3NWW . "P38 Alpha Kinase Complexed With A 2-aminothiazol-5-yl-pyrimidine Based Inhibitor" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 163 no PDB 3O8P . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 164 no PDB 3O8T . "Conformational Plasticity Of P38 Map Kinase Dfg-Motif Mutants In Response To Inhibitor Binding" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 165 no PDB 3O8U . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 99.71 360 99.14 99.43 0.00e+00 . . . . 17940 1 166 no PDB 3OBG . "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 167 no PDB 3OBJ . "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 168 no PDB 3OC1 . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 169 no PDB 3OCG . "P38 Alpha Kinase Complexed With A 5-Amino-Pyrazole Based Inhibitor" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 170 no PDB 3OD6 . "Crystal Structure Of P38alpha Y323t Active Mutant" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 171 no PDB 3ODY . "Crystal Structure Of P38alpha Y323q Active Mutant" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 172 no PDB 3ODZ . "Crystal Structure Of P38alpha Y323r Active Mutant" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 173 no PDB 3OEF . "Crystal Structure Of Y323f Inactive Mutant Of P38alpha Map Kinase" . . . . . 99.71 360 99.14 99.43 0.00e+00 . . . . 17940 1 174 no PDB 3P4K . "The Third Conformation Of P38a Map Kinase Observed In Phosphorylated P38a And In Solution" . . . . . 99.71 370 99.71 100.00 0.00e+00 . . . . 17940 1 175 no PDB 3P5K . "P38 Inhibitor-Bound" . . . . . 100.00 366 99.71 100.00 0.00e+00 . . . . 17940 1 176 no PDB 3P78 . "P38 Inhibitor-Bound" . . . . . 100.00 366 99.71 100.00 0.00e+00 . . . . 17940 1 177 no PDB 3P79 . "P38 Inhibitor-Bound" . . . . . 100.00 366 99.71 100.00 0.00e+00 . . . . 17940 1 178 no PDB 3P7A . "P38 Inhibitor-Bound" . . . . . 100.00 366 99.71 100.00 0.00e+00 . . . . 17940 1 179 no PDB 3P7B . "P38 Inhibitor-Bound" . . . . . 100.00 366 99.71 100.00 0.00e+00 . . . . 17940 1 180 no PDB 3P7C . "P38 Inhibitor-Bound" . . . . . 100.00 366 99.71 100.00 0.00e+00 . . . . 17940 1 181 no PDB 3PG3 . "Human P38 Map Kinase In Complex With Rl182" . . . . . 100.00 360 97.99 97.99 0.00e+00 . . . . 17940 1 182 no PDB 3PY3 . "Crystal Structure Of Phosphorylated P38alpha Map Kinase" . . . . . 99.71 380 99.43 99.43 0.00e+00 . . . . 17940 1 183 no PDB 3QUD . "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino-Benzophenone" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 184 no PDB 3QUE . "Human P38 Map Kinase In Complex With Skepinone-l" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 185 no PDB 3RIN . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 186 no PDB 3ROC . "Crystal Structure Of Human P38 Alpha Complexed With A Pyrimidinone Compound" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 187 no PDB 3S3I . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 99.14 349 99.42 99.42 0.00e+00 . . . . 17940 1 188 no PDB 3S4Q . "P38 Alpha Kinase Complexed With A Pyrazolo-Triazine Based Inhibitor" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 189 no PDB 3TG1 . "Crystal Structure Of P38alpha In Complex With A Mapk Docking Partner" . . . . . 99.71 380 100.00 100.00 0.00e+00 . . . . 17940 1 190 no PDB 3U8W . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Triazolopyridazinone Inhibitor" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 191 no PDB 3UVP . "Human P38 Map Kinase In Complex With A Benzamide Substituted Benzosuberone" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 192 no PDB 3UVQ . "Human P38 Map Kinase In Complex With A Dibenzosuberone Derivative" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 193 no PDB 3UVR . "Human P38 Map Kinase In Complex With Km064" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 194 no PDB 3ZS5 . "Structural Basis For Kinase Selectivity Of Three Clinical P38alpha Inhibitors" . . . . . 100.00 362 99.14 99.43 0.00e+00 . . . . 17940 1 195 no PDB 3ZSG . "X-Ray Structure Of P38alpha Bound To Tak-715" . . . . . 100.00 362 99.14 99.43 0.00e+00 . . . . 17940 1 196 no PDB 3ZSH . "X-Ray Structure Of P38alpha Bound To Scio-469" . . . . . 100.00 362 99.14 99.43 0.00e+00 . . . . 17940 1 197 no PDB 3ZSI . "X-Ray Structure Of P38alpha Bound To Vx-745" . . . . . 100.00 362 99.14 99.43 0.00e+00 . . . . 17940 1 198 no PDB 3ZYA . "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino- Dibenzosuberone" . . . . . 99.71 366 99.43 99.43 0.00e+00 . . . . 17940 1 199 no PDB 4A9Y . "P38alpha Map Kinase Bound To Cmpd 8" . . . . . 100.00 365 99.14 99.43 0.00e+00 . . . . 17940 1 200 no PDB 4AA0 . "P38alpha Map Kinase Bound To Cmpd 2" . . . . . 100.00 365 99.14 99.43 0.00e+00 . . . . 17940 1 201 no PDB 4AA4 . "P38alpha Map Kinase Bound To Cmpd 22" . . . . . 100.00 365 99.14 99.43 0.00e+00 . . . . 17940 1 202 no PDB 4AA5 . "P38alpha Map Kinase Bound To Cmpd 33" . . . . . 100.00 365 98.85 99.14 0.00e+00 . . . . 17940 1 203 no PDB 4AAC . "P38alpha Map Kinase Bound To Cmpd 29" . . . . . 100.00 365 99.14 99.43 0.00e+00 . . . . 17940 1 204 no PDB 4DLI . "Human P38 Map Kinase In Complex With Rl87" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 205 no PDB 4DLJ . "Human P38 Map Kinase In Complex With Rl163" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 206 no PDB 4E5A . "The W197a Mutant Of P38a Map Kinase" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 207 no PDB 4E5B . "Structure Of P38a Map Kinase Without Bog" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 208 no PDB 4E6A . "P38a-pia23 Complex" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 209 no PDB 4E6C . "P38a-perifosine Complex" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 210 no PDB 4E8A . "The Crystal Structure Of P38a Map Kinase In Complex With Pia24" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 211 no PDB 4EH2 . "Human P38 Map Kinase In Complex With Np-F1 And Rl87" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 212 no PDB 4EH3 . "Human P38 Map Kinase In Complex With Np-F2 And Rl87" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 213 no PDB 4EH4 . "Human P38 Map Kinase In Complex With Np-F3 And Rl87" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 214 no PDB 4EH5 . "Human P38 Map Kinase In Complex With Np-F4 And Rl87" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 215 no PDB 4EH6 . "Human P38 Map Kinase In Complex With Np-F5 And Rl87" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 216 no PDB 4EH7 . "Human P38 Map Kinase In Complex With Np-F6 And Rl87" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 217 no PDB 4EH8 . "Human P38 Map Kinase In Complex With Np-F7 And Rl87" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 218 no PDB 4EH9 . "Human P38 Map Kinase In Complex With Np-F11 And Rl87" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 219 no PDB 4EHV . "Human P38 Map Kinase In Complex With Np-F10 And Rl87" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 220 no PDB 4EWQ . "Human P38 Alpha Mapk In Complex With A Pyridazine Based Inhibitor" . . . . . 99.71 383 99.14 99.14 0.00e+00 . . . . 17940 1 221 no PDB 4F9W . "Human P38alpha Mapk In Complex With A Novel And Selective Small Molecule Inhibitor" . . . . . 99.71 383 99.43 99.43 0.00e+00 . . . . 17940 1 222 no PDB 4F9Y . "Human P38 Alpha Mapk In Complex With A Novel And Selective Small Molecule Inhibitor" . . . . . 99.71 383 99.43 99.43 0.00e+00 . . . . 17940 1 223 no PDB 4FA2 . "Human P38 Alpha Mitogen-activated Kinase In Complex With Sb239063" . . . . . 99.71 383 99.43 99.43 0.00e+00 . . . . 17940 1 224 no PDB 4GEO . "P38a Map Kinase Def-pocket Penta Mutant (m194a, L195a, H228a, I229a, Y258a)" . . . . . 99.71 367 97.99 97.99 0.00e+00 . . . . 17940 1 225 no PDB 4KA3 . "Structure Of Map Kinase In Complex With A Docking Peptide" . . . . . 99.71 360 100.00 100.00 0.00e+00 . . . . 17940 1 226 no PDB 4KIN . "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 5-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 227 no PDB 4KIP . "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 2-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 228 no PDB 4KIQ . "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With Ethyl 6-((5-(cyclopropylcarbamoyl)-2-methylpheny" . . . . . 100.00 366 99.14 99.43 0.00e+00 . . . . 17940 1 229 no PDB 4L8M . "Human P38 Map Kinase In Complex With A Dibenzoxepinone" . . . . . 100.00 360 99.14 99.14 0.00e+00 . . . . 17940 1 230 no PDB 4LOO . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (monoclinic Crystal Form)" . . . . . 99.71 361 100.00 100.00 0.00e+00 . . . . 17940 1 231 no PDB 4LOP . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form)" . . . . . 99.71 361 100.00 100.00 0.00e+00 . . . . 17940 1 232 no PDB 4LOQ . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form With Bound Sulphate)" . . . . . 99.71 361 100.00 100.00 0.00e+00 . . . . 17940 1 233 no PDB 4R3C . "Crystal Structure Of P38 Alpha Map Kinase In Complex With A Novel Isoform Selective Drug Candidate" . . . . . 99.71 383 99.14 99.14 0.00e+00 . . . . 17940 1 234 no PDB 4TYH . "Ternary Complex Of P38 And Mk2 With A P38 Inhibitor" . . . . . 98.57 348 100.00 100.00 0.00e+00 . . . . 17940 1 235 no DBJ BAB85654 . "Alternative spliced variant of p38alpha EXIP [Homo sapiens]" . . . . . 72.49 307 99.60 99.60 0.00e+00 . . . . 17940 1 236 no DBJ BAE21782 . "unnamed protein product [Mus musculus]" . . . . . 99.71 360 100.00 100.00 0.00e+00 . . . . 17940 1 237 no DBJ BAE30324 . "unnamed protein product [Mus musculus]" . . . . . 77.94 283 100.00 100.00 0.00e+00 . . . . 17940 1 238 no DBJ BAE31659 . "unnamed protein product [Mus musculus]" . . . . . 77.94 283 100.00 100.00 0.00e+00 . . . . 17940 1 239 no DBJ BAF84398 . "unnamed protein product [Homo sapiens]" . . . . . 99.71 360 99.14 99.14 0.00e+00 . . . . 17940 1 240 no EMBL CAG38743 . "MAPK14 [Homo sapiens]" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 241 no GB AAA20888 . "MAP kinase [Mus musculus]" . . . . . 99.71 360 100.00 100.00 0.00e+00 . . . . 17940 1 242 no GB AAA57456 . "CSaids binding protein [Homo sapiens]" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 243 no GB AAA74301 . "MAP kinase [Homo sapiens]" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 244 no GB AAB51285 . "p38 mitogen activated protein kinase [Rattus norvegicus]" . . . . . 99.71 360 98.85 99.43 0.00e+00 . . . . 17940 1 245 no GB AAC36131 . "p38 mitogen activated protein kinase [Canis lupus familiaris]" . . . . . 99.71 360 98.85 99.43 0.00e+00 . . . . 17940 1 246 no PRF 2111247A . "p38 mitogen-activated protein kinase" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 247 no PRF 2124426A . "Mxi2 protein" . . . . . 80.23 297 98.93 98.93 0.00e+00 . . . . 17940 1 248 no REF NP_001003206 . "mitogen-activated protein kinase 14 [Canis lupus familiaris]" . . . . . 99.71 360 98.85 99.43 0.00e+00 . . . . 17940 1 249 no REF NP_001136366 . "mitogen-activated protein kinase 14 [Ovis aries]" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 1 250 no REF NP_001161985 . "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" . . . . . 77.94 283 100.00 100.00 0.00e+00 . . . . 17940 1 251 no REF NP_001161986 . "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" . . . . . 77.94 283 100.00 100.00 0.00e+00 . . . . 17940 1 252 no REF NP_036081 . "mitogen-activated protein kinase 14 isoform 1 [Mus musculus]" . . . . . 99.71 360 100.00 100.00 0.00e+00 . . . . 17940 1 253 no SP O02812 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Mitogen-activated protein " . . . . . 99.71 360 98.85 99.43 0.00e+00 . . . . 17940 1 254 no SP P47811 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=CRK1; AltName: Full=Mitoge" . . . . . 99.71 360 100.00 100.00 0.00e+00 . . . . 17940 1 255 no SP P70618 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=CRK1; AltName: Full=Mitoge" . . . . . 99.71 360 99.14 99.71 0.00e+00 . . . . 17940 1 256 no SP Q16539 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Cytokine suppressive anti-" . . . . . 99.71 360 99.43 99.43 0.00e+00 . . . . 17940 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 . ASN . 17940 1 2 . SER . 17940 1 3 . GLN . 17940 1 4 . GLU . 17940 1 5 . ARG . 17940 1 6 . PRO . 17940 1 7 . THR . 17940 1 8 . PHE . 17940 1 9 . TYR . 17940 1 10 . ARG . 17940 1 11 . GLN . 17940 1 12 . GLU . 17940 1 13 . LEU . 17940 1 14 . ASN . 17940 1 15 . LYS . 17940 1 16 . THR . 17940 1 17 . ILE . 17940 1 18 . TRP . 17940 1 19 . GLU . 17940 1 20 . VAL . 17940 1 21 . PRO . 17940 1 22 . GLU . 17940 1 23 . ARG . 17940 1 24 . TYR . 17940 1 25 . GLN . 17940 1 26 . ASN . 17940 1 27 . LEU . 17940 1 28 . SER . 17940 1 29 . PRO . 17940 1 30 . VAL . 17940 1 31 . GLY . 17940 1 32 . SER . 17940 1 33 . GLY . 17940 1 34 . ALA . 17940 1 35 . TYR . 17940 1 36 . GLY . 17940 1 37 . SER . 17940 1 38 . VAL . 17940 1 39 . CYS . 17940 1 40 . ALA . 17940 1 41 . ALA . 17940 1 42 . PHE . 17940 1 43 . ASP . 17940 1 44 . THR . 17940 1 45 . LYS . 17940 1 46 . THR . 17940 1 47 . GLY . 17940 1 48 . HIS . 17940 1 49 . ARG . 17940 1 50 . VAL . 17940 1 51 . ALA . 17940 1 52 . VAL . 17940 1 53 . LYS . 17940 1 54 . LYS . 17940 1 55 . LEU . 17940 1 56 . SER . 17940 1 57 . ARG . 17940 1 58 . PRO . 17940 1 59 . PHE . 17940 1 60 . GLN . 17940 1 61 . SER . 17940 1 62 . ILE . 17940 1 63 . ILE . 17940 1 64 . HIS . 17940 1 65 . ALA . 17940 1 66 . LYS . 17940 1 67 . ARG . 17940 1 68 . THR . 17940 1 69 . TYR . 17940 1 70 . ARG . 17940 1 71 . GLU . 17940 1 72 . LEU . 17940 1 73 . ARG . 17940 1 74 . LEU . 17940 1 75 . LEU . 17940 1 76 . LYS . 17940 1 77 . HIS . 17940 1 78 . MET . 17940 1 79 . LYS . 17940 1 80 . HIS . 17940 1 81 . GLU . 17940 1 82 . ASN . 17940 1 83 . VAL . 17940 1 84 . ILE . 17940 1 85 . GLY . 17940 1 86 . LEU . 17940 1 87 . LEU . 17940 1 88 . ASP . 17940 1 89 . VAL . 17940 1 90 . PHE . 17940 1 91 . THR . 17940 1 92 . PRO . 17940 1 93 . ALA . 17940 1 94 . ARG . 17940 1 95 . SER . 17940 1 96 . LEU . 17940 1 97 . GLU . 17940 1 98 . GLU . 17940 1 99 . PHE . 17940 1 100 . ASN . 17940 1 101 . ASP . 17940 1 102 . VAL . 17940 1 103 . TYR . 17940 1 104 . LEU . 17940 1 105 . VAL . 17940 1 106 . THR . 17940 1 107 . HIS . 17940 1 108 . LEU . 17940 1 109 . MET . 17940 1 110 . GLY . 17940 1 111 . ALA . 17940 1 112 . ASP . 17940 1 113 . LEU . 17940 1 114 . ASN . 17940 1 115 . ASN . 17940 1 116 . ILE . 17940 1 117 . VAL . 17940 1 118 . LYS . 17940 1 119 . CYS . 17940 1 120 . GLN . 17940 1 121 . LYS . 17940 1 122 . LEU . 17940 1 123 . THR . 17940 1 124 . ASP . 17940 1 125 . ASP . 17940 1 126 . HIS . 17940 1 127 . VAL . 17940 1 128 . GLN . 17940 1 129 . PHE . 17940 1 130 . LEU . 17940 1 131 . ILE . 17940 1 132 . TYR . 17940 1 133 . GLN . 17940 1 134 . ILE . 17940 1 135 . LEU . 17940 1 136 . ARG . 17940 1 137 . GLY . 17940 1 138 . LEU . 17940 1 139 . LYS . 17940 1 140 . TYR . 17940 1 141 . ILE . 17940 1 142 . HIS . 17940 1 143 . SER . 17940 1 144 . ALA . 17940 1 145 . ASP . 17940 1 146 . ILE . 17940 1 147 . ILE . 17940 1 148 . HIS . 17940 1 149 . ARG . 17940 1 150 . ASP . 17940 1 151 . LEU . 17940 1 152 . LYS . 17940 1 153 . PRO . 17940 1 154 . SER . 17940 1 155 . ASN . 17940 1 156 . LEU . 17940 1 157 . ALA . 17940 1 158 . VAL . 17940 1 159 . ASN . 17940 1 160 . GLU . 17940 1 161 . ASP . 17940 1 162 . CYS . 17940 1 163 . GLU . 17940 1 164 . LEU . 17940 1 165 . LYS . 17940 1 166 . ILE . 17940 1 167 . LEU . 17940 1 168 . ASP . 17940 1 169 . PHE . 17940 1 170 . GLY . 17940 1 171 . LEU . 17940 1 172 . ALA . 17940 1 173 . ARG . 17940 1 174 . HIS . 17940 1 175 . THR . 17940 1 176 . ASP . 17940 1 177 . ASP . 17940 1 178 . GLU . 17940 1 179 . MET . 17940 1 180 . THR . 17940 1 181 . GLY . 17940 1 182 . TYR . 17940 1 183 . VAL . 17940 1 184 . ALA . 17940 1 185 . THR . 17940 1 186 . ARG . 17940 1 187 . TRP . 17940 1 188 . TYR . 17940 1 189 . ARG . 17940 1 190 . ALA . 17940 1 191 . PRO . 17940 1 192 . GLU . 17940 1 193 . ILE . 17940 1 194 . MET . 17940 1 195 . LEU . 17940 1 196 . ASN . 17940 1 197 . TRP . 17940 1 198 . MET . 17940 1 199 . HIS . 17940 1 200 . TYR . 17940 1 201 . ASN . 17940 1 202 . GLN . 17940 1 203 . THR . 17940 1 204 . VAL . 17940 1 205 . ASP . 17940 1 206 . ILE . 17940 1 207 . TRP . 17940 1 208 . SER . 17940 1 209 . VAL . 17940 1 210 . GLY . 17940 1 211 . CYS . 17940 1 212 . ILE . 17940 1 213 . MET . 17940 1 214 . ALA . 17940 1 215 . GLU . 17940 1 216 . LEU . 17940 1 217 . LEU . 17940 1 218 . THR . 17940 1 219 . GLY . 17940 1 220 . ARG . 17940 1 221 . THR . 17940 1 222 . LEU . 17940 1 223 . PHE . 17940 1 224 . PRO . 17940 1 225 . GLY . 17940 1 226 . THR . 17940 1 227 . ASP . 17940 1 228 . HIS . 17940 1 229 . ILE . 17940 1 230 . ASP . 17940 1 231 . GLN . 17940 1 232 . LEU . 17940 1 233 . LYS . 17940 1 234 . LEU . 17940 1 235 . ILE . 17940 1 236 . LEU . 17940 1 237 . ARG . 17940 1 238 . LEU . 17940 1 239 . VAL . 17940 1 240 . GLY . 17940 1 241 . THR . 17940 1 242 . PRO . 17940 1 243 . GLY . 17940 1 244 . ALA . 17940 1 245 . GLU . 17940 1 246 . LEU . 17940 1 247 . LEU . 17940 1 248 . LYS . 17940 1 249 . LYS . 17940 1 250 . ILE . 17940 1 251 . SER . 17940 1 252 . SER . 17940 1 253 . GLU . 17940 1 254 . SER . 17940 1 255 . ALA . 17940 1 256 . ARG . 17940 1 257 . ASN . 17940 1 258 . TYR . 17940 1 259 . ILE . 17940 1 260 . GLN . 17940 1 261 . SER . 17940 1 262 . LEU . 17940 1 263 . ALA . 17940 1 264 . GLN . 17940 1 265 . MET . 17940 1 266 . PRO . 17940 1 267 . LYS . 17940 1 268 . MET . 17940 1 269 . ASN . 17940 1 270 . PHE . 17940 1 271 . ALA . 17940 1 272 . ASN . 17940 1 273 . VAL . 17940 1 274 . PHE . 17940 1 275 . ILE . 17940 1 276 . GLY . 17940 1 277 . ALA . 17940 1 278 . ASN . 17940 1 279 . PRO . 17940 1 280 . LEU . 17940 1 281 . ALA . 17940 1 282 . VAL . 17940 1 283 . ASP . 17940 1 284 . LEU . 17940 1 285 . LEU . 17940 1 286 . GLU . 17940 1 287 . LYS . 17940 1 288 . MET . 17940 1 289 . LEU . 17940 1 290 . VAL . 17940 1 291 . LEU . 17940 1 292 . ASP . 17940 1 293 . SER . 17940 1 294 . ASP . 17940 1 295 . LYS . 17940 1 296 . ARG . 17940 1 297 . ILE . 17940 1 298 . THR . 17940 1 299 . ALA . 17940 1 300 . ALA . 17940 1 301 . GLN . 17940 1 302 . ALA . 17940 1 303 . LEU . 17940 1 304 . ALA . 17940 1 305 . HIS . 17940 1 306 . ALA . 17940 1 307 . TYR . 17940 1 308 . PHE . 17940 1 309 . ALA . 17940 1 310 . GLN . 17940 1 311 . TYR . 17940 1 312 . HIS . 17940 1 313 . ASP . 17940 1 314 . PRO . 17940 1 315 . ASP . 17940 1 316 . ASP . 17940 1 317 . GLU . 17940 1 318 . PRO . 17940 1 319 . VAL . 17940 1 320 . ALA . 17940 1 321 . ASP . 17940 1 322 . PRO . 17940 1 323 . TYR . 17940 1 324 . ASP . 17940 1 325 . GLN . 17940 1 326 . SER . 17940 1 327 . PHE . 17940 1 328 . GLU . 17940 1 329 . SER . 17940 1 330 . ARG . 17940 1 331 . ASP . 17940 1 332 . LEU . 17940 1 333 . LEU . 17940 1 334 . ILE . 17940 1 335 . ASP . 17940 1 336 . GLU . 17940 1 337 . TRP . 17940 1 338 . LYS . 17940 1 339 . SER . 17940 1 340 . LEU . 17940 1 341 . THR . 17940 1 342 . TYR . 17940 1 343 . ASP . 17940 1 344 . GLU . 17940 1 345 . VAL . 17940 1 346 . ILE . 17940 1 347 . SER . 17940 1 348 . PHE . 17940 1 349 . VAL . 17940 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 . ASN 1 1 17940 1 . SER 2 2 17940 1 . GLN 3 3 17940 1 . GLU 4 4 17940 1 . ARG 5 5 17940 1 . PRO 6 6 17940 1 . THR 7 7 17940 1 . PHE 8 8 17940 1 . TYR 9 9 17940 1 . ARG 10 10 17940 1 . GLN 11 11 17940 1 . GLU 12 12 17940 1 . LEU 13 13 17940 1 . ASN 14 14 17940 1 . LYS 15 15 17940 1 . THR 16 16 17940 1 . ILE 17 17 17940 1 . TRP 18 18 17940 1 . GLU 19 19 17940 1 . VAL 20 20 17940 1 . PRO 21 21 17940 1 . GLU 22 22 17940 1 . ARG 23 23 17940 1 . TYR 24 24 17940 1 . GLN 25 25 17940 1 . ASN 26 26 17940 1 . LEU 27 27 17940 1 . SER 28 28 17940 1 . PRO 29 29 17940 1 . VAL 30 30 17940 1 . GLY 31 31 17940 1 . SER 32 32 17940 1 . GLY 33 33 17940 1 . ALA 34 34 17940 1 . TYR 35 35 17940 1 . GLY 36 36 17940 1 . SER 37 37 17940 1 . VAL 38 38 17940 1 . CYS 39 39 17940 1 . ALA 40 40 17940 1 . ALA 41 41 17940 1 . PHE 42 42 17940 1 . ASP 43 43 17940 1 . THR 44 44 17940 1 . LYS 45 45 17940 1 . THR 46 46 17940 1 . GLY 47 47 17940 1 . HIS 48 48 17940 1 . ARG 49 49 17940 1 . VAL 50 50 17940 1 . ALA 51 51 17940 1 . VAL 52 52 17940 1 . LYS 53 53 17940 1 . LYS 54 54 17940 1 . LEU 55 55 17940 1 . SER 56 56 17940 1 . ARG 57 57 17940 1 . PRO 58 58 17940 1 . PHE 59 59 17940 1 . GLN 60 60 17940 1 . SER 61 61 17940 1 . ILE 62 62 17940 1 . ILE 63 63 17940 1 . HIS 64 64 17940 1 . ALA 65 65 17940 1 . LYS 66 66 17940 1 . ARG 67 67 17940 1 . THR 68 68 17940 1 . TYR 69 69 17940 1 . ARG 70 70 17940 1 . GLU 71 71 17940 1 . LEU 72 72 17940 1 . ARG 73 73 17940 1 . LEU 74 74 17940 1 . LEU 75 75 17940 1 . LYS 76 76 17940 1 . HIS 77 77 17940 1 . MET 78 78 17940 1 . LYS 79 79 17940 1 . HIS 80 80 17940 1 . GLU 81 81 17940 1 . ASN 82 82 17940 1 . VAL 83 83 17940 1 . ILE 84 84 17940 1 . GLY 85 85 17940 1 . LEU 86 86 17940 1 . LEU 87 87 17940 1 . ASP 88 88 17940 1 . VAL 89 89 17940 1 . PHE 90 90 17940 1 . THR 91 91 17940 1 . PRO 92 92 17940 1 . ALA 93 93 17940 1 . ARG 94 94 17940 1 . SER 95 95 17940 1 . LEU 96 96 17940 1 . GLU 97 97 17940 1 . GLU 98 98 17940 1 . PHE 99 99 17940 1 . ASN 100 100 17940 1 . ASP 101 101 17940 1 . VAL 102 102 17940 1 . TYR 103 103 17940 1 . LEU 104 104 17940 1 . VAL 105 105 17940 1 . THR 106 106 17940 1 . HIS 107 107 17940 1 . LEU 108 108 17940 1 . MET 109 109 17940 1 . GLY 110 110 17940 1 . ALA 111 111 17940 1 . ASP 112 112 17940 1 . LEU 113 113 17940 1 . ASN 114 114 17940 1 . ASN 115 115 17940 1 . ILE 116 116 17940 1 . VAL 117 117 17940 1 . LYS 118 118 17940 1 . CYS 119 119 17940 1 . GLN 120 120 17940 1 . LYS 121 121 17940 1 . LEU 122 122 17940 1 . THR 123 123 17940 1 . ASP 124 124 17940 1 . ASP 125 125 17940 1 . HIS 126 126 17940 1 . VAL 127 127 17940 1 . GLN 128 128 17940 1 . PHE 129 129 17940 1 . LEU 130 130 17940 1 . ILE 131 131 17940 1 . TYR 132 132 17940 1 . GLN 133 133 17940 1 . ILE 134 134 17940 1 . LEU 135 135 17940 1 . ARG 136 136 17940 1 . GLY 137 137 17940 1 . LEU 138 138 17940 1 . LYS 139 139 17940 1 . TYR 140 140 17940 1 . ILE 141 141 17940 1 . HIS 142 142 17940 1 . SER 143 143 17940 1 . ALA 144 144 17940 1 . ASP 145 145 17940 1 . ILE 146 146 17940 1 . ILE 147 147 17940 1 . HIS 148 148 17940 1 . ARG 149 149 17940 1 . ASP 150 150 17940 1 . LEU 151 151 17940 1 . LYS 152 152 17940 1 . PRO 153 153 17940 1 . SER 154 154 17940 1 . ASN 155 155 17940 1 . LEU 156 156 17940 1 . ALA 157 157 17940 1 . VAL 158 158 17940 1 . ASN 159 159 17940 1 . GLU 160 160 17940 1 . ASP 161 161 17940 1 . CYS 162 162 17940 1 . GLU 163 163 17940 1 . LEU 164 164 17940 1 . LYS 165 165 17940 1 . ILE 166 166 17940 1 . LEU 167 167 17940 1 . ASP 168 168 17940 1 . PHE 169 169 17940 1 . GLY 170 170 17940 1 . LEU 171 171 17940 1 . ALA 172 172 17940 1 . ARG 173 173 17940 1 . HIS 174 174 17940 1 . THR 175 175 17940 1 . ASP 176 176 17940 1 . ASP 177 177 17940 1 . GLU 178 178 17940 1 . MET 179 179 17940 1 . THR 180 180 17940 1 . GLY 181 181 17940 1 . TYR 182 182 17940 1 . VAL 183 183 17940 1 . ALA 184 184 17940 1 . THR 185 185 17940 1 . ARG 186 186 17940 1 . TRP 187 187 17940 1 . TYR 188 188 17940 1 . ARG 189 189 17940 1 . ALA 190 190 17940 1 . PRO 191 191 17940 1 . GLU 192 192 17940 1 . ILE 193 193 17940 1 . MET 194 194 17940 1 . LEU 195 195 17940 1 . ASN 196 196 17940 1 . TRP 197 197 17940 1 . MET 198 198 17940 1 . HIS 199 199 17940 1 . TYR 200 200 17940 1 . ASN 201 201 17940 1 . GLN 202 202 17940 1 . THR 203 203 17940 1 . VAL 204 204 17940 1 . ASP 205 205 17940 1 . ILE 206 206 17940 1 . TRP 207 207 17940 1 . SER 208 208 17940 1 . VAL 209 209 17940 1 . GLY 210 210 17940 1 . CYS 211 211 17940 1 . ILE 212 212 17940 1 . MET 213 213 17940 1 . ALA 214 214 17940 1 . GLU 215 215 17940 1 . LEU 216 216 17940 1 . LEU 217 217 17940 1 . THR 218 218 17940 1 . GLY 219 219 17940 1 . ARG 220 220 17940 1 . THR 221 221 17940 1 . LEU 222 222 17940 1 . PHE 223 223 17940 1 . PRO 224 224 17940 1 . GLY 225 225 17940 1 . THR 226 226 17940 1 . ASP 227 227 17940 1 . HIS 228 228 17940 1 . ILE 229 229 17940 1 . ASP 230 230 17940 1 . GLN 231 231 17940 1 . LEU 232 232 17940 1 . LYS 233 233 17940 1 . LEU 234 234 17940 1 . ILE 235 235 17940 1 . LEU 236 236 17940 1 . ARG 237 237 17940 1 . LEU 238 238 17940 1 . VAL 239 239 17940 1 . GLY 240 240 17940 1 . THR 241 241 17940 1 . PRO 242 242 17940 1 . GLY 243 243 17940 1 . ALA 244 244 17940 1 . GLU 245 245 17940 1 . LEU 246 246 17940 1 . LEU 247 247 17940 1 . LYS 248 248 17940 1 . LYS 249 249 17940 1 . ILE 250 250 17940 1 . SER 251 251 17940 1 . SER 252 252 17940 1 . GLU 253 253 17940 1 . SER 254 254 17940 1 . ALA 255 255 17940 1 . ARG 256 256 17940 1 . ASN 257 257 17940 1 . TYR 258 258 17940 1 . ILE 259 259 17940 1 . GLN 260 260 17940 1 . SER 261 261 17940 1 . LEU 262 262 17940 1 . ALA 263 263 17940 1 . GLN 264 264 17940 1 . MET 265 265 17940 1 . PRO 266 266 17940 1 . LYS 267 267 17940 1 . MET 268 268 17940 1 . ASN 269 269 17940 1 . PHE 270 270 17940 1 . ALA 271 271 17940 1 . ASN 272 272 17940 1 . VAL 273 273 17940 1 . PHE 274 274 17940 1 . ILE 275 275 17940 1 . GLY 276 276 17940 1 . ALA 277 277 17940 1 . ASN 278 278 17940 1 . PRO 279 279 17940 1 . LEU 280 280 17940 1 . ALA 281 281 17940 1 . VAL 282 282 17940 1 . ASP 283 283 17940 1 . LEU 284 284 17940 1 . LEU 285 285 17940 1 . GLU 286 286 17940 1 . LYS 287 287 17940 1 . MET 288 288 17940 1 . LEU 289 289 17940 1 . VAL 290 290 17940 1 . LEU 291 291 17940 1 . ASP 292 292 17940 1 . SER 293 293 17940 1 . ASP 294 294 17940 1 . LYS 295 295 17940 1 . ARG 296 296 17940 1 . ILE 297 297 17940 1 . THR 298 298 17940 1 . ALA 299 299 17940 1 . ALA 300 300 17940 1 . GLN 301 301 17940 1 . ALA 302 302 17940 1 . LEU 303 303 17940 1 . ALA 304 304 17940 1 . HIS 305 305 17940 1 . ALA 306 306 17940 1 . TYR 307 307 17940 1 . PHE 308 308 17940 1 . ALA 309 309 17940 1 . GLN 310 310 17940 1 . TYR 311 311 17940 1 . HIS 312 312 17940 1 . ASP 313 313 17940 1 . PRO 314 314 17940 1 . ASP 315 315 17940 1 . ASP 316 316 17940 1 . GLU 317 317 17940 1 . PRO 318 318 17940 1 . VAL 319 319 17940 1 . ALA 320 320 17940 1 . ASP 321 321 17940 1 . PRO 322 322 17940 1 . TYR 323 323 17940 1 . ASP 324 324 17940 1 . GLN 325 325 17940 1 . SER 326 326 17940 1 . PHE 327 327 17940 1 . GLU 328 328 17940 1 . SER 329 329 17940 1 . ARG 330 330 17940 1 . ASP 331 331 17940 1 . LEU 332 332 17940 1 . LEU 333 333 17940 1 . ILE 334 334 17940 1 . ASP 335 335 17940 1 . GLU 336 336 17940 1 . TRP 337 337 17940 1 . LYS 338 338 17940 1 . SER 339 339 17940 1 . LEU 340 340 17940 1 . THR 341 341 17940 1 . TYR 342 342 17940 1 . ASP 343 343 17940 1 . GLU 344 344 17940 1 . VAL 345 345 17940 1 . ILE 346 346 17940 1 . SER 347 347 17940 1 . PHE 348 348 17940 1 . VAL 349 349 17940 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 17940 _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 $p38alpha . 10090 organism . 'Mus musculus' Mouse . . Eukaryota Metazoa Mus musculus . . . . . . . . . . . . . . . . . . . . . 17940 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 17940 _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 $p38alpha . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli BL21(DE3) pLysS . . . . . . . . . . . . . . 'pET DUET' . . . 'dual expression of p38 and MKK6 for double phosphorylation of p38' . . 17940 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 17940 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'activated by double phosphorylation (pT180 and pY182)' _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 p38alpha '[U-13C; U-15N; U-2H]' . . 1 $p38alpha . . 0.5 . . mM . . . . 17940 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 17940 _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' 0.15 . M 17940 1 pH 6.8 . pH 17940 1 pressure 1 . atm 17940 1 temperature 298 . K 17940 1 stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 17940 _Software.ID 1 _Software.Name TOPSPIN _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Bruker . . 17940 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 17940 1 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 17940 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 950 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 17940 _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 . 950 . . . 17940 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 17940 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17940 1 2 '3D HNCACB' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17940 1 3 '3D HN(CO)CA' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17940 1 4 '3D HNCO' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17940 1 stop_ save_ save_NMR_spectrometer_expt _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spectrometer_expt _NMR_spec_expt.Entry_ID 17940 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name . _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $spectrometer_1 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $TOPSPIN _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 17940 _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 . . . . . . . . . 17940 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 17940 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 17940 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 17940 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 17940 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 6 6 PRO C C 13 175.705 0.1 . 1 . . . . 6 PRO C . 17940 1 2 . 1 1 6 6 PRO CA C 13 61.801 0.1 . 1 . . . . 6 PRO CA . 17940 1 3 . 1 1 6 6 PRO CB C 13 31.409 0.1 . 1 . . . . 6 PRO CB . 17940 1 4 . 1 1 7 7 THR H H 1 8.491 0.02 . 1 . . . . 7 THR H . 17940 1 5 . 1 1 7 7 THR C C 13 173.882 0.1 . 1 . . . . 7 THR C . 17940 1 6 . 1 1 7 7 THR CA C 13 62.251 0.1 . 1 . . . . 7 THR CA . 17940 1 7 . 1 1 7 7 THR CB C 13 69.022 0.1 . 1 . . . . 7 THR CB . 17940 1 8 . 1 1 7 7 THR N N 15 117.423 0.1 . 1 . . . . 7 THR N . 17940 1 9 . 1 1 8 8 PHE H H 1 8.788 0.02 . 1 . . . . 8 PHE H . 17940 1 10 . 1 1 8 8 PHE C C 13 175.904 0.1 . 1 . . . . 8 PHE C . 17940 1 11 . 1 1 8 8 PHE CA C 13 56.166 0.1 . 1 . . . . 8 PHE CA . 17940 1 12 . 1 1 8 8 PHE CB C 13 41.157 0.1 . 1 . . . . 8 PHE CB . 17940 1 13 . 1 1 8 8 PHE N N 15 127.243 0.1 . 1 . . . . 8 PHE N . 17940 1 14 . 1 1 9 9 TYR H H 1 9.147 0.02 . 1 . . . . 9 TYR H . 17940 1 15 . 1 1 9 9 TYR C C 13 172.51 0.1 . 1 . . . . 9 TYR C . 17940 1 16 . 1 1 9 9 TYR CA C 13 55.102 0.1 . 1 . . . . 9 TYR CA . 17940 1 17 . 1 1 9 9 TYR CB C 13 40.07 0.1 . 1 . . . . 9 TYR CB . 17940 1 18 . 1 1 9 9 TYR N N 15 120.254 0.1 . 1 . . . . 9 TYR N . 17940 1 19 . 1 1 10 10 ARG H H 1 8.442 0.02 . 1 . . . . 10 ARG H . 17940 1 20 . 1 1 10 10 ARG C C 13 176.048 0.1 . 1 . . . . 10 ARG C . 17940 1 21 . 1 1 10 10 ARG CA C 13 53.685 0.1 . 1 . . . . 10 ARG CA . 17940 1 22 . 1 1 10 10 ARG CB C 13 32.739 0.1 . 1 . . . . 10 ARG CB . 17940 1 23 . 1 1 10 10 ARG N N 15 120.053 0.1 . 1 . . . . 10 ARG N . 17940 1 24 . 1 1 11 11 GLN H H 1 9.056 0.02 . 1 . . . . 11 GLN H . 17940 1 25 . 1 1 11 11 GLN C C 13 173.016 0.1 . 1 . . . . 11 GLN C . 17940 1 26 . 1 1 11 11 GLN CA C 13 54.025 0.1 . 1 . . . . 11 GLN CA . 17940 1 27 . 1 1 11 11 GLN CB C 13 32.251 0.1 . 1 . . . . 11 GLN CB . 17940 1 28 . 1 1 11 11 GLN N N 15 122.993 0.1 . 1 . . . . 11 GLN N . 17940 1 29 . 1 1 12 12 GLU H H 1 8.866 0.02 . 1 . . . . 12 GLU H . 17940 1 30 . 1 1 12 12 GLU C C 13 175.741 0.1 . 1 . . . . 12 GLU C . 17940 1 31 . 1 1 12 12 GLU CA C 13 54.758 0.1 . 1 . . . . 12 GLU CA . 17940 1 32 . 1 1 12 12 GLU CB C 13 29.815 0.1 . 1 . . . . 12 GLU CB . 17940 1 33 . 1 1 12 12 GLU N N 15 125.846 0.1 . 1 . . . . 12 GLU N . 17940 1 34 . 1 1 13 13 LEU H H 1 9.021 0.02 . 1 . . . . 13 LEU H . 17940 1 35 . 1 1 13 13 LEU CA C 13 53.341 0.1 . 1 . . . . 13 LEU CA . 17940 1 36 . 1 1 13 13 LEU CB C 13 43.466 0.1 . 1 . . . . 13 LEU CB . 17940 1 37 . 1 1 13 13 LEU N N 15 128.688 0.1 . 1 . . . . 13 LEU N . 17940 1 38 . 1 1 14 14 ASN C C 13 175.055 0.1 . 1 . . . . 14 ASN C . 17940 1 39 . 1 1 14 14 ASN CA C 13 53.822 0.1 . 1 . . . . 14 ASN CA . 17940 1 40 . 1 1 14 14 ASN CB C 13 36.627 0.1 . 1 . . . . 14 ASN CB . 17940 1 41 . 1 1 15 15 LYS H H 1 8.891 0.02 . 1 . . . . 15 LYS H . 17940 1 42 . 1 1 15 15 LYS C C 13 175.489 0.1 . 1 . . . . 15 LYS C . 17940 1 43 . 1 1 15 15 LYS CA C 13 57.229 0.1 . 1 . . . . 15 LYS CA . 17940 1 44 . 1 1 15 15 LYS CB C 13 28.82 0.1 . 1 . . . . 15 LYS CB . 17940 1 45 . 1 1 15 15 LYS N N 15 110.119 0.1 . 1 . . . . 15 LYS N . 17940 1 46 . 1 1 16 16 THR H H 1 7.892 0.02 . 1 . . . . 16 THR H . 17940 1 47 . 1 1 16 16 THR C C 13 172.564 0.1 . 1 . . . . 16 THR C . 17940 1 48 . 1 1 16 16 THR CA C 13 60.61 0.1 . 1 . . . . 16 THR CA . 17940 1 49 . 1 1 16 16 THR CB C 13 70.75 0.1 . 1 . . . . 16 THR CB . 17940 1 50 . 1 1 16 16 THR N N 15 115.832 0.1 . 1 . . . . 16 THR N . 17940 1 51 . 1 1 17 17 ILE H H 1 8.62 0.02 . 1 . . . . 17 ILE H . 17940 1 52 . 1 1 17 17 ILE C C 13 175.579 0.1 . 1 . . . . 17 ILE C . 17940 1 53 . 1 1 17 17 ILE CA C 13 59.658 0.1 . 1 . . . . 17 ILE CA . 17940 1 54 . 1 1 17 17 ILE CB C 13 36.02 0.1 . 1 . . . . 17 ILE CB . 17940 1 55 . 1 1 17 17 ILE N N 15 125.469 0.1 . 1 . . . . 17 ILE N . 17940 1 56 . 1 1 18 18 TRP H H 1 9.31 0.02 . 1 . . . . 18 TRP H . 17940 1 57 . 1 1 18 18 TRP C C 13 174.731 0.1 . 1 . . . . 18 TRP C . 17940 1 58 . 1 1 18 18 TRP CA C 13 56.295 0.1 . 1 . . . . 18 TRP CA . 17940 1 59 . 1 1 18 18 TRP CB C 13 28.416 0.1 . 1 . . . . 18 TRP CB . 17940 1 60 . 1 1 18 18 TRP N N 15 131.223 0.1 . 1 . . . . 18 TRP N . 17940 1 61 . 1 1 19 19 GLU H H 1 8.295 0.02 . 1 . . . . 19 GLU H . 17940 1 62 . 1 1 19 19 GLU C C 13 173.268 0.1 . 1 . . . . 19 GLU C . 17940 1 63 . 1 1 19 19 GLU CA C 13 54.094 0.1 . 1 . . . . 19 GLU CA . 17940 1 64 . 1 1 19 19 GLU CB C 13 30.327 0.1 . 1 . . . . 19 GLU CB . 17940 1 65 . 1 1 19 19 GLU N N 15 128.016 0.1 . 1 . . . . 19 GLU N . 17940 1 66 . 1 1 20 20 VAL H H 1 7.67 0.02 . 1 . . . . 20 VAL H . 17940 1 67 . 1 1 20 20 VAL CA C 13 55.337 0.1 . 1 . . . . 20 VAL CA . 17940 1 68 . 1 1 20 20 VAL CB C 13 33.233 0.1 . 1 . . . . 20 VAL CB . 17940 1 69 . 1 1 20 20 VAL N N 15 112.562 0.1 . 1 . . . . 20 VAL N . 17940 1 70 . 1 1 21 21 PRO C C 13 177.167 0.1 . 1 . . . . 21 PRO C . 17940 1 71 . 1 1 21 21 PRO CA C 13 60.991 0.1 . 1 . . . . 21 PRO CA . 17940 1 72 . 1 1 21 21 PRO CB C 13 31.386 0.1 . 1 . . . . 21 PRO CB . 17940 1 73 . 1 1 22 22 GLU H H 1 8.147 0.02 . 1 . . . . 22 GLU H . 17940 1 74 . 1 1 22 22 GLU C C 13 176.229 0.1 . 1 . . . . 22 GLU C . 17940 1 75 . 1 1 22 22 GLU CA C 13 57.657 0.1 . 1 . . . . 22 GLU CA . 17940 1 76 . 1 1 22 22 GLU CB C 13 28.759 0.1 . 1 . . . . 22 GLU CB . 17940 1 77 . 1 1 22 22 GLU N N 15 119.022 0.1 . 1 . . . . 22 GLU N . 17940 1 78 . 1 1 23 23 ARG H H 1 7.453 0.02 . 1 . . . . 23 ARG H . 17940 1 79 . 1 1 23 23 ARG C C 13 174.767 0.1 . 1 . . . . 23 ARG C . 17940 1 80 . 1 1 23 23 ARG CA C 13 57.139 0.1 . 1 . . . . 23 ARG CA . 17940 1 81 . 1 1 23 23 ARG CB C 13 29.928 0.1 . 1 . . . . 23 ARG CB . 17940 1 82 . 1 1 23 23 ARG N N 15 117.672 0.1 . 1 . . . . 23 ARG N . 17940 1 83 . 1 1 24 24 TYR H H 1 7.834 0.02 . 1 . . . . 24 TYR H . 17940 1 84 . 1 1 24 24 TYR C C 13 174.514 0.1 . 1 . . . . 24 TYR C . 17940 1 85 . 1 1 24 24 TYR CA C 13 56.159 0.1 . 1 . . . . 24 TYR CA . 17940 1 86 . 1 1 24 24 TYR CB C 13 36.882 0.1 . 1 . . . . 24 TYR CB . 17940 1 87 . 1 1 24 24 TYR N N 15 118.072 0.1 . 1 . . . . 24 TYR N . 17940 1 88 . 1 1 25 25 GLN H H 1 9.148 0.02 . 1 . . . . 25 GLN H . 17940 1 89 . 1 1 25 25 GLN C C 13 174.857 0.1 . 1 . . . . 25 GLN C . 17940 1 90 . 1 1 25 25 GLN CA C 13 52.76 0.1 . 1 . . . . 25 GLN CA . 17940 1 91 . 1 1 25 25 GLN CB C 13 32.442 0.1 . 1 . . . . 25 GLN CB . 17940 1 92 . 1 1 25 25 GLN N N 15 122.55 0.1 . 1 . . . . 25 GLN N . 17940 1 93 . 1 1 26 26 ASN H H 1 8.858 0.02 . 1 . . . . 26 ASN H . 17940 1 94 . 1 1 26 26 ASN C C 13 173.99 0.1 . 1 . . . . 26 ASN C . 17940 1 95 . 1 1 26 26 ASN CA C 13 53.186 0.1 . 1 . . . . 26 ASN CA . 17940 1 96 . 1 1 26 26 ASN CB C 13 36.215 0.1 . 1 . . . . 26 ASN CB . 17940 1 97 . 1 1 26 26 ASN N N 15 117.787 0.1 . 1 . . . . 26 ASN N . 17940 1 98 . 1 1 27 27 LEU H H 1 8.53 0.02 . 1 . . . . 27 LEU H . 17940 1 99 . 1 1 27 27 LEU C C 13 179.153 0.1 . 1 . . . . 27 LEU C . 17940 1 100 . 1 1 27 27 LEU CA C 13 56.135 0.1 . 1 . . . . 27 LEU CA . 17940 1 101 . 1 1 27 27 LEU CB C 13 40.405 0.1 . 1 . . . . 27 LEU CB . 17940 1 102 . 1 1 27 27 LEU N N 15 119.89 0.1 . 1 . . . . 27 LEU N . 17940 1 103 . 1 1 28 28 SER H H 1 8.774 0.02 . 1 . . . . 28 SER H . 17940 1 104 . 1 1 28 28 SER CA C 13 53.84 0.1 . 1 . . . . 28 SER CA . 17940 1 105 . 1 1 28 28 SER CB C 13 64.233 0.1 . 1 . . . . 28 SER CB . 17940 1 106 . 1 1 28 28 SER N N 15 116.102 0.1 . 1 . . . . 28 SER N . 17940 1 107 . 1 1 29 29 PRO C C 13 176.12 0.1 . 1 . . . . 29 PRO C . 17940 1 108 . 1 1 29 29 PRO CA C 13 63.773 0.1 . 1 . . . . 29 PRO CA . 17940 1 109 . 1 1 29 29 PRO CB C 13 30.706 0.1 . 1 . . . . 29 PRO CB . 17940 1 110 . 1 1 30 30 VAL H H 1 8.638 0.02 . 1 . . . . 30 VAL H . 17940 1 111 . 1 1 30 30 VAL C C 13 176.193 0.1 . 1 . . . . 30 VAL C . 17940 1 112 . 1 1 30 30 VAL CA C 13 61.125 0.1 . 1 . . . . 30 VAL CA . 17940 1 113 . 1 1 30 30 VAL CB C 13 32.947 0.1 . 1 . . . . 30 VAL CB . 17940 1 114 . 1 1 30 30 VAL N N 15 120.95 0.1 . 1 . . . . 30 VAL N . 17940 1 115 . 1 1 31 31 GLY H H 1 7.394 0.02 . 1 . . . . 31 GLY H . 17940 1 116 . 1 1 31 31 GLY C C 13 172.817 0.1 . 1 . . . . 31 GLY C . 17940 1 117 . 1 1 31 31 GLY CA C 13 44.658 0.1 . 1 . . . . 31 GLY CA . 17940 1 118 . 1 1 31 31 GLY N N 15 108.423 0.1 . 1 . . . . 31 GLY N . 17940 1 119 . 1 1 32 32 SER H H 1 8.417 0.02 . 1 . . . . 32 SER H . 17940 1 120 . 1 1 32 32 SER C C 13 173.774 0.1 . 1 . . . . 32 SER C . 17940 1 121 . 1 1 32 32 SER CA C 13 57.253 0.1 . 1 . . . . 32 SER CA . 17940 1 122 . 1 1 32 32 SER CB C 13 64.487 0.1 . 1 . . . . 32 SER CB . 17940 1 123 . 1 1 32 32 SER N N 15 115.357 0.1 . 1 . . . . 32 SER N . 17940 1 124 . 1 1 33 33 GLY H H 1 8.205 0.02 . 1 . . . . 33 GLY H . 17940 1 125 . 1 1 33 33 GLY CA C 13 44.117 0.1 . 1 . . . . 33 GLY CA . 17940 1 126 . 1 1 33 33 GLY N N 15 110.435 0.1 . 1 . . . . 33 GLY N . 17940 1 127 . 1 1 38 38 VAL H H 1 8.474 0.02 . 1 . . . . 38 VAL H . 17940 1 128 . 1 1 38 38 VAL C C 13 176.337 0.1 . 1 . . . . 38 VAL C . 17940 1 129 . 1 1 38 38 VAL CA C 13 60.649 0.1 . 1 . . . . 38 VAL CA . 17940 1 130 . 1 1 38 38 VAL CB C 13 35.17 0.1 . 1 . . . . 38 VAL CB . 17940 1 131 . 1 1 38 38 VAL N N 15 122.494 0.1 . 1 . . . . 38 VAL N . 17940 1 132 . 1 1 39 39 CYS H H 1 9.342 0.02 . 1 . . . . 39 CYS H . 17940 1 133 . 1 1 39 39 CYS C C 13 173.449 0.1 . 1 . . . . 39 CYS C . 17940 1 134 . 1 1 39 39 CYS CA C 13 57.255 0.1 . 1 . . . . 39 CYS CA . 17940 1 135 . 1 1 39 39 CYS CB C 13 30.418 0.1 . 1 . . . . 39 CYS CB . 17940 1 136 . 1 1 39 39 CYS N N 15 125.274 0.1 . 1 . . . . 39 CYS N . 17940 1 137 . 1 1 40 40 ALA H H 1 8.817 0.02 . 1 . . . . 40 ALA H . 17940 1 138 . 1 1 40 40 ALA C C 13 176.427 0.1 . 1 . . . . 40 ALA C . 17940 1 139 . 1 1 40 40 ALA CA C 13 49.911 0.1 . 1 . . . . 40 ALA CA . 17940 1 140 . 1 1 40 40 ALA CB C 13 19.625 0.1 . 1 . . . . 40 ALA CB . 17940 1 141 . 1 1 40 40 ALA N N 15 125.343 0.1 . 1 . . . . 40 ALA N . 17940 1 142 . 1 1 41 41 ALA H H 1 9.01 0.02 . 1 . . . . 41 ALA H . 17940 1 143 . 1 1 41 41 ALA C C 13 175.218 0.1 . 1 . . . . 41 ALA C . 17940 1 144 . 1 1 41 41 ALA CA C 13 49.725 0.1 . 1 . . . . 41 ALA CA . 17940 1 145 . 1 1 41 41 ALA CB C 13 22.198 0.1 . 1 . . . . 41 ALA CB . 17940 1 146 . 1 1 41 41 ALA N N 15 120.793 0.1 . 1 . . . . 41 ALA N . 17940 1 147 . 1 1 42 42 PHE H H 1 9.351 0.02 . 1 . . . . 42 PHE H . 17940 1 148 . 1 1 42 42 PHE C C 13 174.045 0.1 . 1 . . . . 42 PHE C . 17940 1 149 . 1 1 42 42 PHE CA C 13 56.97 0.1 . 1 . . . . 42 PHE CA . 17940 1 150 . 1 1 42 42 PHE CB C 13 39.929 0.1 . 1 . . . . 42 PHE CB . 17940 1 151 . 1 1 42 42 PHE N N 15 122.124 0.1 . 1 . . . . 42 PHE N . 17940 1 152 . 1 1 43 43 ASP H H 1 8.126 0.02 . 1 . . . . 43 ASP H . 17940 1 153 . 1 1 43 43 ASP C C 13 176.481 0.1 . 1 . . . . 43 ASP C . 17940 1 154 . 1 1 43 43 ASP CA C 13 51.306 0.1 . 1 . . . . 43 ASP CA . 17940 1 155 . 1 1 43 43 ASP CB C 13 41.04 0.1 . 1 . . . . 43 ASP CB . 17940 1 156 . 1 1 43 43 ASP N N 15 126.137 0.1 . 1 . . . . 43 ASP N . 17940 1 157 . 1 1 44 44 THR H H 1 8.898 0.02 . 1 . . . . 44 THR H . 17940 1 158 . 1 1 44 44 THR C C 13 176.463 0.1 . 1 . . . . 44 THR C . 17940 1 159 . 1 1 44 44 THR CA C 13 63.02 0.1 . 1 . . . . 44 THR CA . 17940 1 160 . 1 1 44 44 THR CB C 13 68.711 0.1 . 1 . . . . 44 THR CB . 17940 1 161 . 1 1 44 44 THR N N 15 117.658 0.1 . 1 . . . . 44 THR N . 17940 1 162 . 1 1 45 45 LYS H H 1 7.997 0.02 . 1 . . . . 45 LYS H . 17940 1 163 . 1 1 45 45 LYS C C 13 177.799 0.1 . 1 . . . . 45 LYS C . 17940 1 164 . 1 1 45 45 LYS CA C 13 57.875 0.1 . 1 . . . . 45 LYS CA . 17940 1 165 . 1 1 45 45 LYS CB C 13 31.536 0.1 . 1 . . . . 45 LYS CB . 17940 1 166 . 1 1 45 45 LYS N N 15 121.957 0.1 . 1 . . . . 45 LYS N . 17940 1 167 . 1 1 46 46 THR H H 1 6.638 0.02 . 1 . . . . 46 THR H . 17940 1 168 . 1 1 46 46 THR C C 13 176.066 0.1 . 1 . . . . 46 THR C . 17940 1 169 . 1 1 46 46 THR CA C 13 60.827 0.1 . 1 . . . . 46 THR CA . 17940 1 170 . 1 1 46 46 THR CB C 13 70.253 0.1 . 1 . . . . 46 THR CB . 17940 1 171 . 1 1 46 46 THR N N 15 105.024 0.1 . 1 . . . . 46 THR N . 17940 1 172 . 1 1 47 47 GLY H H 1 8.333 0.02 . 1 . . . . 47 GLY H . 17940 1 173 . 1 1 47 47 GLY C C 13 173.633 0.1 . 1 . . . . 47 GLY C . 17940 1 174 . 1 1 47 47 GLY CA C 13 45.206 0.1 . 1 . . . . 47 GLY CA . 17940 1 175 . 1 1 47 47 GLY N N 15 111.313 0.1 . 1 . . . . 47 GLY N . 17940 1 176 . 1 1 48 48 HIS H H 1 7.137 0.02 . 1 . . . . 48 HIS H . 17940 1 177 . 1 1 48 48 HIS C C 13 174.063 0.1 . 1 . . . . 48 HIS C . 17940 1 178 . 1 1 48 48 HIS CA C 13 53.073 0.1 . 1 . . . . 48 HIS CA . 17940 1 179 . 1 1 48 48 HIS CB C 13 31.281 0.1 . 1 . . . . 48 HIS CB . 17940 1 180 . 1 1 48 48 HIS N N 15 116.761 0.1 . 1 . . . . 48 HIS N . 17940 1 181 . 1 1 49 49 ARG H H 1 8.703 0.02 . 1 . . . . 49 ARG H . 17940 1 182 . 1 1 49 49 ARG CA C 13 55.442 0.1 . 1 . . . . 49 ARG CA . 17940 1 183 . 1 1 49 49 ARG CB C 13 30.056 0.1 . 1 . . . . 49 ARG CB . 17940 1 184 . 1 1 49 49 ARG N N 15 121.012 0.1 . 1 . . . . 49 ARG N . 17940 1 185 . 1 1 50 50 VAL H H 1 8.974 0.02 . 1 . . . . 50 VAL H . 17940 1 186 . 1 1 50 50 VAL C C 13 172.907 0.1 . 1 . . . . 50 VAL C . 17940 1 187 . 1 1 50 50 VAL N N 15 116.464 0.1 . 1 . . . . 50 VAL N . 17940 1 188 . 1 1 51 51 ALA H H 1 8.75 0.02 . 1 . . . . 51 ALA H . 17940 1 189 . 1 1 51 51 ALA C C 13 175.814 0.1 . 1 . . . . 51 ALA C . 17940 1 190 . 1 1 51 51 ALA N N 15 122.476 0.1 . 1 . . . . 51 ALA N . 17940 1 191 . 1 1 52 52 VAL H H 1 9.256 0.02 . 1 . . . . 52 VAL H . 17940 1 192 . 1 1 52 52 VAL C C 13 171.879 0.1 . 1 . . . . 52 VAL C . 17940 1 193 . 1 1 52 52 VAL N N 15 122.187 0.1 . 1 . . . . 52 VAL N . 17940 1 194 . 1 1 53 53 LYS C C 13 174.37 0.1 . 1 . . . . 53 LYS C . 17940 1 195 . 1 1 53 53 LYS CA C 13 53.342 0.1 . 1 . . . . 53 LYS CA . 17940 1 196 . 1 1 53 53 LYS CB C 13 34.275 0.1 . 1 . . . . 53 LYS CB . 17940 1 197 . 1 1 54 54 LYS H H 1 8.587 0.02 . 1 . . . . 54 LYS H . 17940 1 198 . 1 1 54 54 LYS C C 13 176.283 0.1 . 1 . . . . 54 LYS C . 17940 1 199 . 1 1 54 54 LYS CA C 13 53.798 0.1 . 1 . . . . 54 LYS CA . 17940 1 200 . 1 1 54 54 LYS CB C 13 32.781 0.1 . 1 . . . . 54 LYS CB . 17940 1 201 . 1 1 54 54 LYS N N 15 128.383 0.1 . 1 . . . . 54 LYS N . 17940 1 202 . 1 1 55 55 LEU C C 13 176.481 0.1 . 1 . . . . 55 LEU C . 17940 1 203 . 1 1 55 55 LEU CA C 13 54.546 0.1 . 1 . . . . 55 LEU CA . 17940 1 204 . 1 1 55 55 LEU CB C 13 39.12 0.1 . 1 . . . . 55 LEU CB . 17940 1 205 . 1 1 56 56 SER H H 1 8.1 0.02 . 1 . . . . 56 SER H . 17940 1 206 . 1 1 56 56 SER C C 13 173.81 0.1 . 1 . . . . 56 SER C . 17940 1 207 . 1 1 56 56 SER CA C 13 56.678 0.1 . 1 . . . . 56 SER CA . 17940 1 208 . 1 1 56 56 SER CB C 13 62.736 0.1 . 1 . . . . 56 SER CB . 17940 1 209 . 1 1 56 56 SER N N 15 117.895 0.1 . 1 . . . . 56 SER N . 17940 1 210 . 1 1 57 57 ARG H H 1 8.749 0.02 . 1 . . . . 57 ARG H . 17940 1 211 . 1 1 57 57 ARG CA C 13 55.294 0.1 . 1 . . . . 57 ARG CA . 17940 1 212 . 1 1 57 57 ARG CB C 13 28.417 0.1 . 1 . . . . 57 ARG CB . 17940 1 213 . 1 1 57 57 ARG N N 15 122.957 0.1 . 1 . . . . 57 ARG N . 17940 1 214 . 1 1 58 58 PRO C C 13 175.38 0.1 . 1 . . . . 58 PRO C . 17940 1 215 . 1 1 58 58 PRO CA C 13 59.387 0.1 . 1 . . . . 58 PRO CA . 17940 1 216 . 1 1 58 58 PRO CB C 13 30.458 0.1 . 1 . . . . 58 PRO CB . 17940 1 217 . 1 1 59 59 PHE H H 1 7.931 0.02 . 1 . . . . 59 PHE H . 17940 1 218 . 1 1 59 59 PHE C C 13 176.583 0.1 . 1 . . . . 59 PHE C . 17940 1 219 . 1 1 59 59 PHE CA C 13 53.775 0.1 . 1 . . . . 59 PHE CA . 17940 1 220 . 1 1 59 59 PHE CB C 13 37.137 0.1 . 1 . . . . 59 PHE CB . 17940 1 221 . 1 1 59 59 PHE N N 15 112.261 0.1 . 1 . . . . 59 PHE N . 17940 1 222 . 1 1 60 60 GLN H H 1 7.026 0.02 . 1 . . . . 60 GLN H . 17940 1 223 . 1 1 60 60 GLN C C 13 174.46 0.1 . 1 . . . . 60 GLN C . 17940 1 224 . 1 1 60 60 GLN CA C 13 56.774 0.1 . 1 . . . . 60 GLN CA . 17940 1 225 . 1 1 60 60 GLN CB C 13 28.772 0.1 . 1 . . . . 60 GLN CB . 17940 1 226 . 1 1 60 60 GLN N N 15 115.971 0.1 . 1 . . . . 60 GLN N . 17940 1 227 . 1 1 61 61 SER H H 1 7.453 0.02 . 1 . . . . 61 SER H . 17940 1 228 . 1 1 61 61 SER CA C 13 55.81 0.1 . 1 . . . . 61 SER CA . 17940 1 229 . 1 1 61 61 SER CB C 13 66.412 0.1 . 1 . . . . 61 SER CB . 17940 1 230 . 1 1 61 61 SER N N 15 110.103 0.1 . 1 . . . . 61 SER N . 17940 1 231 . 1 1 63 63 ILE C C 13 179.047 0.1 . 1 . . . . 63 ILE C . 17940 1 232 . 1 1 63 63 ILE CA C 13 62.992 0.1 . 1 . . . . 63 ILE CA . 17940 1 233 . 1 1 64 64 HIS H H 1 7.703 0.02 . 1 . . . . 64 HIS H . 17940 1 234 . 1 1 64 64 HIS C C 13 177.113 0.1 . 1 . . . . 64 HIS C . 17940 1 235 . 1 1 64 64 HIS CA C 13 60.869 0.1 . 1 . . . . 64 HIS CA . 17940 1 236 . 1 1 64 64 HIS CB C 13 34.705 0.1 . 1 . . . . 64 HIS CB . 17940 1 237 . 1 1 64 64 HIS N N 15 119.633 0.1 . 1 . . . . 64 HIS N . 17940 1 238 . 1 1 65 65 ALA H H 1 8.635 0.02 . 1 . . . . 65 ALA H . 17940 1 239 . 1 1 65 65 ALA CA C 13 54.405 0.1 . 1 . . . . 65 ALA CA . 17940 1 240 . 1 1 65 65 ALA CB C 13 18.524 0.1 . 1 . . . . 65 ALA CB . 17940 1 241 . 1 1 65 65 ALA N N 15 123.619 0.1 . 1 . . . . 65 ALA N . 17940 1 242 . 1 1 78 78 MET C C 13 176.301 0.1 . 1 . . . . 78 MET C . 17940 1 243 . 1 1 79 79 LYS H H 1 8.489 0.02 . 1 . . . . 79 LYS H . 17940 1 244 . 1 1 79 79 LYS C C 13 173.196 0.1 . 1 . . . . 79 LYS C . 17940 1 245 . 1 1 79 79 LYS CA C 13 53.92 0.1 . 1 . . . . 79 LYS CA . 17940 1 246 . 1 1 79 79 LYS CB C 13 31.822 0.1 . 1 . . . . 79 LYS CB . 17940 1 247 . 1 1 79 79 LYS N N 15 128.524 0.1 . 1 . . . . 79 LYS N . 17940 1 248 . 1 1 80 80 HIS H H 1 8.707 0.02 . 1 . . . . 80 HIS H . 17940 1 249 . 1 1 80 80 HIS C C 13 175.344 0.1 . 1 . . . . 80 HIS C . 17940 1 250 . 1 1 80 80 HIS CA C 13 56.716 0.1 . 1 . . . . 80 HIS CA . 17940 1 251 . 1 1 80 80 HIS CB C 13 32.667 0.1 . 1 . . . . 80 HIS CB . 17940 1 252 . 1 1 80 80 HIS N N 15 124.068 0.1 . 1 . . . . 80 HIS N . 17940 1 253 . 1 1 81 81 GLU H H 1 8.075 0.02 . 1 . . . . 81 GLU H . 17940 1 254 . 1 1 81 81 GLU C C 13 177.889 0.1 . 1 . . . . 81 GLU C . 17940 1 255 . 1 1 81 81 GLU CA C 13 58.493 0.1 . 1 . . . . 81 GLU CA . 17940 1 256 . 1 1 81 81 GLU CB C 13 29.082 0.1 . 1 . . . . 81 GLU CB . 17940 1 257 . 1 1 81 81 GLU N N 15 125.671 0.1 . 1 . . . . 81 GLU N . 17940 1 258 . 1 1 82 82 ASN H H 1 11.396 0.02 . 1 . . . . 82 ASN H . 17940 1 259 . 1 1 82 82 ASN C C 13 174.171 0.1 . 1 . . . . 82 ASN C . 17940 1 260 . 1 1 82 82 ASN CA C 13 53.006 0.1 . 1 . . . . 82 ASN CA . 17940 1 261 . 1 1 82 82 ASN CB C 13 40.327 0.1 . 1 . . . . 82 ASN CB . 17940 1 262 . 1 1 82 82 ASN N N 15 118.341 0.1 . 1 . . . . 82 ASN N . 17940 1 263 . 1 1 83 83 VAL H H 1 7.696 0.02 . 1 . . . . 83 VAL H . 17940 1 264 . 1 1 83 83 VAL CA C 13 60.809 0.1 . 1 . . . . 83 VAL CA . 17940 1 265 . 1 1 83 83 VAL CB C 13 34.793 0.1 . 1 . . . . 83 VAL CB . 17940 1 266 . 1 1 83 83 VAL N N 15 119.773 0.1 . 1 . . . . 83 VAL N . 17940 1 267 . 1 1 84 84 ILE C C 13 171.588 0.1 . 1 . . . . 84 ILE C . 17940 1 268 . 1 1 84 84 ILE CA C 13 59.507 0.1 . 1 . . . . 84 ILE CA . 17940 1 269 . 1 1 85 85 GLY H H 1 7.629 0.02 . 1 . . . . 85 GLY H . 17940 1 270 . 1 1 85 85 GLY CA C 13 43.105 0.1 . 1 . . . . 85 GLY CA . 17940 1 271 . 1 1 85 85 GLY N N 15 109.601 0.1 . 1 . . . . 85 GLY N . 17940 1 272 . 1 1 86 86 LEU C C 13 176.445 0.1 . 1 . . . . 86 LEU C . 17940 1 273 . 1 1 86 86 LEU CA C 13 53.154 0.1 . 1 . . . . 86 LEU CA . 17940 1 274 . 1 1 86 86 LEU CB C 13 42.722 0.1 . 1 . . . . 86 LEU CB . 17940 1 275 . 1 1 87 87 LEU H H 1 9.09 0.02 . 1 . . . . 87 LEU H . 17940 1 276 . 1 1 87 87 LEU CA C 13 54.766 0.1 . 1 . . . . 87 LEU CA . 17940 1 277 . 1 1 87 87 LEU CB C 13 40.029 0.1 . 1 . . . . 87 LEU CB . 17940 1 278 . 1 1 87 87 LEU N N 15 126.437 0.1 . 1 . . . . 87 LEU N . 17940 1 279 . 1 1 88 88 ASP C C 13 172.607 0.1 . 1 . . . . 88 ASP C . 17940 1 280 . 1 1 88 88 ASP CA C 13 51.912 0.1 . 1 . . . . 88 ASP CA . 17940 1 281 . 1 1 88 88 ASP CB C 13 41.833 0.1 . 1 . . . . 88 ASP CB . 17940 1 282 . 1 1 89 89 VAL H H 1 7.914 0.02 . 1 . . . . 89 VAL H . 17940 1 283 . 1 1 89 89 VAL CA C 13 58.759 0.1 . 1 . . . . 89 VAL CA . 17940 1 284 . 1 1 89 89 VAL CB C 13 32.742 0.1 . 1 . . . . 89 VAL CB . 17940 1 285 . 1 1 89 89 VAL N N 15 120.34 0.1 . 1 . . . . 89 VAL N . 17940 1 286 . 1 1 90 90 PHE H H 1 8.285 0.02 . 1 . . . . 90 PHE H . 17940 1 287 . 1 1 90 90 PHE C C 13 172.799 0.1 . 1 . . . . 90 PHE C . 17940 1 288 . 1 1 90 90 PHE CA C 13 54.74 0.1 . 1 . . . . 90 PHE CA . 17940 1 289 . 1 1 90 90 PHE CB C 13 41.013 0.1 . 1 . . . . 90 PHE CB . 17940 1 290 . 1 1 90 90 PHE N N 15 119.08 0.1 . 1 . . . . 90 PHE N . 17940 1 291 . 1 1 91 91 THR H H 1 8.971 0.02 . 1 . . . . 91 THR H . 17940 1 292 . 1 1 91 91 THR CA C 13 56.791 0.1 . 1 . . . . 91 THR CA . 17940 1 293 . 1 1 91 91 THR CB C 13 71.767 0.1 . 1 . . . . 91 THR CB . 17940 1 294 . 1 1 91 91 THR N N 15 113.621 0.1 . 1 . . . . 91 THR N . 17940 1 295 . 1 1 92 92 PRO C C 13 176.572 0.1 . 1 . . . . 92 PRO C . 17940 1 296 . 1 1 92 92 PRO CA C 13 61.92 0.1 . 1 . . . . 92 PRO CA . 17940 1 297 . 1 1 92 92 PRO CB C 13 30.446 0.1 . 1 . . . . 92 PRO CB . 17940 1 298 . 1 1 93 93 ALA H H 1 7.733 0.02 . 1 . . . . 93 ALA H . 17940 1 299 . 1 1 93 93 ALA C C 13 178.503 0.1 . 1 . . . . 93 ALA C . 17940 1 300 . 1 1 93 93 ALA CA C 13 52.177 0.1 . 1 . . . . 93 ALA CA . 17940 1 301 . 1 1 93 93 ALA CB C 13 19.62 0.1 . 1 . . . . 93 ALA CB . 17940 1 302 . 1 1 93 93 ALA N N 15 122.401 0.1 . 1 . . . . 93 ALA N . 17940 1 303 . 1 1 94 94 ARG H H 1 9.291 0.02 . 1 . . . . 94 ARG H . 17940 1 304 . 1 1 94 94 ARG C C 13 175.073 0.1 . 1 . . . . 94 ARG C . 17940 1 305 . 1 1 94 94 ARG CA C 13 55.314 0.1 . 1 . . . . 94 ARG CA . 17940 1 306 . 1 1 94 94 ARG CB C 13 29.799 0.1 . 1 . . . . 94 ARG CB . 17940 1 307 . 1 1 94 94 ARG N N 15 121.34 0.1 . 1 . . . . 94 ARG N . 17940 1 308 . 1 1 95 95 SER H H 1 7.406 0.02 . 1 . . . . 95 SER H . 17940 1 309 . 1 1 95 95 SER C C 13 173.659 0.1 . 1 . . . . 95 SER C . 17940 1 310 . 1 1 95 95 SER CA C 13 55.81 0.1 . 1 . . . . 95 SER CA . 17940 1 311 . 1 1 95 95 SER CB C 13 65.428 0.1 . 1 . . . . 95 SER CB . 17940 1 312 . 1 1 95 95 SER N N 15 111.322 0.1 . 1 . . . . 95 SER N . 17940 1 313 . 1 1 96 96 LEU H H 1 8.484 0.02 . 1 . . . . 96 LEU H . 17940 1 314 . 1 1 96 96 LEU C C 13 178.864 0.1 . 1 . . . . 96 LEU C . 17940 1 315 . 1 1 96 96 LEU CA C 13 56.212 0.1 . 1 . . . . 96 LEU CA . 17940 1 316 . 1 1 96 96 LEU CB C 13 40.165 0.1 . 1 . . . . 96 LEU CB . 17940 1 317 . 1 1 96 96 LEU N N 15 122.532 0.1 . 1 . . . . 96 LEU N . 17940 1 318 . 1 1 97 97 GLU H H 1 8.333 0.02 . 1 . . . . 97 GLU H . 17940 1 319 . 1 1 97 97 GLU C C 13 177.51 0.1 . 1 . . . . 97 GLU C . 17940 1 320 . 1 1 97 97 GLU CA C 13 58.598 0.1 . 1 . . . . 97 GLU CA . 17940 1 321 . 1 1 97 97 GLU CB C 13 27.819 0.1 . 1 . . . . 97 GLU CB . 17940 1 322 . 1 1 97 97 GLU N N 15 117.359 0.1 . 1 . . . . 97 GLU N . 17940 1 323 . 1 1 98 98 GLU H H 1 7.052 0.02 . 1 . . . . 98 GLU H . 17940 1 324 . 1 1 98 98 GLU C C 13 175.398 0.1 . 1 . . . . 98 GLU C . 17940 1 325 . 1 1 98 98 GLU CA C 13 54.067 0.1 . 1 . . . . 98 GLU CA . 17940 1 326 . 1 1 98 98 GLU CB C 13 30.301 0.1 . 1 . . . . 98 GLU CB . 17940 1 327 . 1 1 98 98 GLU N N 15 115.472 0.1 . 1 . . . . 98 GLU N . 17940 1 328 . 1 1 99 99 PHE H H 1 7.322 0.02 . 1 . . . . 99 PHE H . 17940 1 329 . 1 1 99 99 PHE C C 13 173.142 0.1 . 1 . . . . 99 PHE C . 17940 1 330 . 1 1 99 99 PHE CA C 13 56.315 0.1 . 1 . . . . 99 PHE CA . 17940 1 331 . 1 1 99 99 PHE CB C 13 37.987 0.1 . 1 . . . . 99 PHE CB . 17940 1 332 . 1 1 99 99 PHE N N 15 122.242 0.1 . 1 . . . . 99 PHE N . 17940 1 333 . 1 1 100 100 ASN H H 1 8.571 0.02 . 1 . . . . 100 ASN H . 17940 1 334 . 1 1 100 100 ASN C C 13 172.456 0.1 . 1 . . . . 100 ASN C . 17940 1 335 . 1 1 100 100 ASN CA C 13 53.415 0.1 . 1 . . . . 100 ASN CA . 17940 1 336 . 1 1 100 100 ASN CB C 13 41.836 0.1 . 1 . . . . 100 ASN CB . 17940 1 337 . 1 1 100 100 ASN N N 15 125.659 0.1 . 1 . . . . 100 ASN N . 17940 1 338 . 1 1 101 101 ASP H H 1 7.626 0.02 . 1 . . . . 101 ASP H . 17940 1 339 . 1 1 101 101 ASP C C 13 174.406 0.1 . 1 . . . . 101 ASP C . 17940 1 340 . 1 1 101 101 ASP CA C 13 52.501 0.1 . 1 . . . . 101 ASP CA . 17940 1 341 . 1 1 101 101 ASP CB C 13 43.824 0.1 . 1 . . . . 101 ASP CB . 17940 1 342 . 1 1 101 101 ASP N N 15 115.842 0.1 . 1 . . . . 101 ASP N . 17940 1 343 . 1 1 102 102 VAL H H 1 8.468 0.02 . 1 . . . . 102 VAL H . 17940 1 344 . 1 1 102 102 VAL CA C 13 60.908 0.1 . 1 . . . . 102 VAL CA . 17940 1 345 . 1 1 102 102 VAL CB C 13 34.523 0.1 . 1 . . . . 102 VAL CB . 17940 1 346 . 1 1 102 102 VAL N N 15 121.302 0.1 . 1 . . . . 102 VAL N . 17940 1 347 . 1 1 103 103 TYR CA C 13 54.796 0.1 . 1 . . . . 103 TYR CA . 17940 1 348 . 1 1 104 104 LEU H H 1 8.862 0.02 . 1 . . . . 104 LEU H . 17940 1 349 . 1 1 104 104 LEU C C 13 174.586 0.1 . 1 . . . . 104 LEU C . 17940 1 350 . 1 1 104 104 LEU CA C 13 56.316 0.1 . 1 . . . . 104 LEU CA . 17940 1 351 . 1 1 104 104 LEU N N 15 119.46 0.1 . 1 . . . . 104 LEU N . 17940 1 352 . 1 1 105 105 VAL H H 1 8.349 0.02 . 1 . . . . 105 VAL H . 17940 1 353 . 1 1 105 105 VAL C C 13 175.561 0.1 . 1 . . . . 105 VAL C . 17940 1 354 . 1 1 105 105 VAL CA C 13 60.206 0.1 . 1 . . . . 105 VAL CA . 17940 1 355 . 1 1 105 105 VAL CB C 13 31.199 0.1 . 1 . . . . 105 VAL CB . 17940 1 356 . 1 1 105 105 VAL N N 15 123.588 0.1 . 1 . . . . 105 VAL N . 17940 1 357 . 1 1 106 106 THR H H 1 9.144 0.02 . 1 . . . . 106 THR H . 17940 1 358 . 1 1 106 106 THR CA C 13 58.705 0.1 . 1 . . . . 106 THR CA . 17940 1 359 . 1 1 106 106 THR CB C 13 73.265 0.1 . 1 . . . . 106 THR CB . 17940 1 360 . 1 1 106 106 THR N N 15 118.256 0.1 . 1 . . . . 106 THR N . 17940 1 361 . 1 1 110 110 GLY C C 13 172.962 0.1 . 1 . . . . 110 GLY C . 17940 1 362 . 1 1 110 110 GLY CA C 13 45.076 0.1 . 1 . . . . 110 GLY CA . 17940 1 363 . 1 1 111 111 ALA H H 1 7.915 0.02 . 1 . . . . 111 ALA H . 17940 1 364 . 1 1 111 111 ALA CA C 13 50.914 0.1 . 1 . . . . 111 ALA CA . 17940 1 365 . 1 1 111 111 ALA CB C 13 20.171 0.1 . 1 . . . . 111 ALA CB . 17940 1 366 . 1 1 111 111 ALA N N 15 123.725 0.1 . 1 . . . . 111 ALA N . 17940 1 367 . 1 1 114 114 ASN C C 13 175.718 0.1 . 1 . . . . 114 ASN C . 17940 1 368 . 1 1 115 115 ASN H H 1 7.887 0.02 . 1 . . . . 115 ASN H . 17940 1 369 . 1 1 115 115 ASN C C 13 176.856 0.1 . 1 . . . . 115 ASN C . 17940 1 370 . 1 1 115 115 ASN CA C 13 58.362 0.1 . 1 . . . . 115 ASN CA . 17940 1 371 . 1 1 115 115 ASN CB C 13 39.622 0.1 . 1 . . . . 115 ASN CB . 17940 1 372 . 1 1 115 115 ASN N N 15 122.109 0.1 . 1 . . . . 115 ASN N . 17940 1 373 . 1 1 116 116 ILE H H 1 7.526 0.02 . 1 . . . . 116 ILE H . 17940 1 374 . 1 1 116 116 ILE C C 13 177.456 0.1 . 1 . . . . 116 ILE C . 17940 1 375 . 1 1 116 116 ILE CA C 13 62.678 0.1 . 1 . . . . 116 ILE CA . 17940 1 376 . 1 1 116 116 ILE CB C 13 40.585 0.1 . 1 . . . . 116 ILE CB . 17940 1 377 . 1 1 116 116 ILE N N 15 118.713 0.1 . 1 . . . . 116 ILE N . 17940 1 378 . 1 1 117 117 VAL H H 1 7.593 0.02 . 1 . . . . 117 VAL H . 17940 1 379 . 1 1 117 117 VAL C C 13 177.42 0.1 . 1 . . . . 117 VAL C . 17940 1 380 . 1 1 117 117 VAL CA C 13 64.038 0.1 . 1 . . . . 117 VAL CA . 17940 1 381 . 1 1 117 117 VAL CB C 13 30.607 0.1 . 1 . . . . 117 VAL CB . 17940 1 382 . 1 1 117 117 VAL N N 15 116.648 0.1 . 1 . . . . 117 VAL N . 17940 1 383 . 1 1 118 118 LYS H H 1 7.381 0.02 . 1 . . . . 118 LYS H . 17940 1 384 . 1 1 118 118 LYS C C 13 178.16 0.1 . 1 . . . . 118 LYS C . 17940 1 385 . 1 1 118 118 LYS CA C 13 57.312 0.1 . 1 . . . . 118 LYS CA . 17940 1 386 . 1 1 118 118 LYS CB C 13 31.557 0.1 . 1 . . . . 118 LYS CB . 17940 1 387 . 1 1 118 118 LYS N N 15 117.325 0.1 . 1 . . . . 118 LYS N . 17940 1 388 . 1 1 119 119 CYS H H 1 7.622 0.02 . 1 . . . . 119 CYS H . 17940 1 389 . 1 1 119 119 CYS C C 13 174.192 0.1 . 1 . . . . 119 CYS C . 17940 1 390 . 1 1 119 119 CYS CA C 13 59.035 0.1 . 1 . . . . 119 CYS CA . 17940 1 391 . 1 1 119 119 CYS CB C 13 28.549 0.1 . 1 . . . . 119 CYS CB . 17940 1 392 . 1 1 119 119 CYS N N 15 114.389 0.1 . 1 . . . . 119 CYS N . 17940 1 393 . 1 1 120 120 GLN H H 1 8.042 0.02 . 1 . . . . 120 GLN H . 17940 1 394 . 1 1 120 120 GLN C C 13 173.81 0.1 . 1 . . . . 120 GLN C . 17940 1 395 . 1 1 120 120 GLN CA C 13 54.396 0.1 . 1 . . . . 120 GLN CA . 17940 1 396 . 1 1 120 120 GLN CB C 13 29.995 0.1 . 1 . . . . 120 GLN CB . 17940 1 397 . 1 1 120 120 GLN N N 15 119.596 0.1 . 1 . . . . 120 GLN N . 17940 1 398 . 1 1 121 121 LYS H H 1 8.23 0.02 . 1 . . . . 121 LYS H . 17940 1 399 . 1 1 121 121 LYS C C 13 176.283 0.1 . 1 . . . . 121 LYS C . 17940 1 400 . 1 1 121 121 LYS CA C 13 54.815 0.1 . 1 . . . . 121 LYS CA . 17940 1 401 . 1 1 121 121 LYS CB C 13 31.263 0.1 . 1 . . . . 121 LYS CB . 17940 1 402 . 1 1 121 121 LYS N N 15 121.946 0.1 . 1 . . . . 121 LYS N . 17940 1 403 . 1 1 122 122 LEU H H 1 8.567 0.02 . 1 . . . . 122 LEU H . 17940 1 404 . 1 1 122 122 LEU C C 13 173.954 0.1 . 1 . . . . 122 LEU C . 17940 1 405 . 1 1 122 122 LEU CA C 13 53.836 0.1 . 1 . . . . 122 LEU CA . 17940 1 406 . 1 1 122 122 LEU CB C 13 41.602 0.1 . 1 . . . . 122 LEU CB . 17940 1 407 . 1 1 122 122 LEU N N 15 126.678 0.1 . 1 . . . . 122 LEU N . 17940 1 408 . 1 1 123 123 THR H H 1 8.984 0.02 . 1 . . . . 123 THR H . 17940 1 409 . 1 1 123 123 THR C C 13 175.814 0.1 . 1 . . . . 123 THR C . 17940 1 410 . 1 1 123 123 THR CA C 13 59.784 0.1 . 1 . . . . 123 THR CA . 17940 1 411 . 1 1 123 123 THR CB C 13 72.263 0.1 . 1 . . . . 123 THR CB . 17940 1 412 . 1 1 123 123 THR N N 15 121.526 0.1 . 1 . . . . 123 THR N . 17940 1 413 . 1 1 124 124 ASP H H 1 8.993 0.02 . 1 . . . . 124 ASP H . 17940 1 414 . 1 1 124 124 ASP C C 13 177.637 0.1 . 1 . . . . 124 ASP C . 17940 1 415 . 1 1 124 124 ASP CA C 13 57.626 0.1 . 1 . . . . 124 ASP CA . 17940 1 416 . 1 1 124 124 ASP CB C 13 42.075 0.1 . 1 . . . . 124 ASP CB . 17940 1 417 . 1 1 124 124 ASP N N 15 120.993 0.1 . 1 . . . . 124 ASP N . 17940 1 418 . 1 1 125 125 ASP H H 1 8.014 0.02 . 1 . . . . 125 ASP H . 17940 1 419 . 1 1 125 125 ASP C C 13 177.406 0.1 . 1 . . . . 125 ASP C . 17940 1 420 . 1 1 125 125 ASP CA C 13 56.436 0.1 . 1 . . . . 125 ASP CA . 17940 1 421 . 1 1 125 125 ASP CB C 13 39.895 0.1 . 1 . . . . 125 ASP CB . 17940 1 422 . 1 1 125 125 ASP N N 15 115.472 0.1 . 1 . . . . 125 ASP N . 17940 1 423 . 1 1 126 126 HIS H H 1 7.576 0.02 . 1 . . . . 126 HIS H . 17940 1 424 . 1 1 126 126 HIS C C 13 177.998 0.1 . 1 . . . . 126 HIS C . 17940 1 425 . 1 1 126 126 HIS CA C 13 59.477 0.1 . 1 . . . . 126 HIS CA . 17940 1 426 . 1 1 126 126 HIS N N 15 118.366 0.1 . 1 . . . . 126 HIS N . 17940 1 427 . 1 1 127 127 VAL H H 1 8.162 0.02 . 1 . . . . 127 VAL H . 17940 1 428 . 1 1 127 127 VAL C C 13 177.601 0.1 . 1 . . . . 127 VAL C . 17940 1 429 . 1 1 127 127 VAL CA C 13 67.987 0.1 . 1 . . . . 127 VAL CA . 17940 1 430 . 1 1 127 127 VAL CB C 13 29.96 0.1 . 1 . . . . 127 VAL CB . 17940 1 431 . 1 1 127 127 VAL N N 15 120.118 0.1 . 1 . . . . 127 VAL N . 17940 1 432 . 1 1 128 128 GLN H H 1 8.437 0.02 . 1 . . . . 128 GLN H . 17940 1 433 . 1 1 128 128 GLN C C 13 177.889 0.1 . 1 . . . . 128 GLN C . 17940 1 434 . 1 1 128 128 GLN CA C 13 58.598 0.1 . 1 . . . . 128 GLN CA . 17940 1 435 . 1 1 128 128 GLN CB C 13 29.346 0.1 . 1 . . . . 128 GLN CB . 17940 1 436 . 1 1 128 128 GLN N N 15 118.324 0.1 . 1 . . . . 128 GLN N . 17940 1 437 . 1 1 129 129 PHE H H 1 7.464 0.02 . 1 . . . . 129 PHE H . 17940 1 438 . 1 1 129 129 PHE C C 13 179.532 0.1 . 1 . . . . 129 PHE C . 17940 1 439 . 1 1 129 129 PHE CA C 13 57.633 0.1 . 1 . . . . 129 PHE CA . 17940 1 440 . 1 1 129 129 PHE CB C 13 38.784 0.1 . 1 . . . . 129 PHE CB . 17940 1 441 . 1 1 129 129 PHE N N 15 116.242 0.1 . 1 . . . . 129 PHE N . 17940 1 442 . 1 1 130 130 LEU H H 1 8.805 0.02 . 1 . . . . 130 LEU H . 17940 1 443 . 1 1 130 130 LEU CA C 13 57.711 0.1 . 1 . . . . 130 LEU CA . 17940 1 444 . 1 1 130 130 LEU CB C 13 41.429 0.1 . 1 . . . . 130 LEU CB . 17940 1 445 . 1 1 130 130 LEU N N 15 120.687 0.1 . 1 . . . . 130 LEU N . 17940 1 446 . 1 1 136 136 ARG C C 13 179.785 0.1 . 1 . . . . 136 ARG C . 17940 1 447 . 1 1 136 136 ARG CA C 13 59.697 0.1 . 1 . . . . 136 ARG CA . 17940 1 448 . 1 1 136 136 ARG CB C 13 28.881 0.1 . 1 . . . . 136 ARG CB . 17940 1 449 . 1 1 137 137 GLY H H 1 8.152 0.02 . 1 . . . . 137 GLY H . 17940 1 450 . 1 1 137 137 GLY C C 13 174.911 0.1 . 1 . . . . 137 GLY C . 17940 1 451 . 1 1 137 137 GLY CA C 13 46.153 0.1 . 1 . . . . 137 GLY CA . 17940 1 452 . 1 1 137 137 GLY N N 15 107.288 0.1 . 1 . . . . 137 GLY N . 17940 1 453 . 1 1 138 138 LEU H H 1 8.687 0.02 . 1 . . . . 138 LEU H . 17940 1 454 . 1 1 138 138 LEU C C 13 177.366 0.1 . 1 . . . . 138 LEU C . 17940 1 455 . 1 1 138 138 LEU CA C 13 56.271 0.1 . 1 . . . . 138 LEU CA . 17940 1 456 . 1 1 138 138 LEU CB C 13 40.345 0.1 . 1 . . . . 138 LEU CB . 17940 1 457 . 1 1 138 138 LEU N N 15 121.615 0.1 . 1 . . . . 138 LEU N . 17940 1 458 . 1 1 139 139 LYS C C 13 179.406 0.1 . 1 . . . . 139 LYS C . 17940 1 459 . 1 1 139 139 LYS CA C 13 59.165 0.1 . 1 . . . . 139 LYS CA . 17940 1 460 . 1 1 139 139 LYS CB C 13 31.112 0.1 . 1 . . . . 139 LYS CB . 17940 1 461 . 1 1 140 140 TYR H H 1 6.853 0.02 . 1 . . . . 140 TYR H . 17940 1 462 . 1 1 140 140 TYR CA C 13 60.819 0.1 . 1 . . . . 140 TYR CA . 17940 1 463 . 1 1 140 140 TYR CB C 13 37.124 0.1 . 1 . . . . 140 TYR CB . 17940 1 464 . 1 1 140 140 TYR N N 15 118.302 0.1 . 1 . . . . 140 TYR N . 17940 1 465 . 1 1 141 141 ILE C C 13 177.194 0.1 . 1 . . . . 141 ILE C . 17940 1 466 . 1 1 141 141 ILE CA C 13 65.583 0.1 . 1 . . . . 141 ILE CA . 17940 1 467 . 1 1 142 142 HIS H H 1 9.521 0.02 . 1 . . . . 142 HIS H . 17940 1 468 . 1 1 142 142 HIS CA C 13 56.442 0.1 . 1 . . . . 142 HIS CA . 17940 1 469 . 1 1 142 142 HIS CB C 13 30.116 0.1 . 1 . . . . 142 HIS CB . 17940 1 470 . 1 1 142 142 HIS N N 15 119.549 0.1 . 1 . . . . 142 HIS N . 17940 1 471 . 1 1 143 143 SER C C 13 174.568 0.1 . 1 . . . . 143 SER C . 17940 1 472 . 1 1 143 143 SER CA C 13 60.533 0.1 . 1 . . . . 143 SER CA . 17940 1 473 . 1 1 143 143 SER CB C 13 62.095 0.1 . 1 . . . . 143 SER CB . 17940 1 474 . 1 1 144 144 ALA H H 1 7.441 0.02 . 1 . . . . 144 ALA H . 17940 1 475 . 1 1 144 144 ALA CA C 13 50.473 0.1 . 1 . . . . 144 ALA CA . 17940 1 476 . 1 1 144 144 ALA CB C 13 17.18 0.1 . 1 . . . . 144 ALA CB . 17940 1 477 . 1 1 144 144 ALA N N 15 126.251 0.1 . 1 . . . . 144 ALA N . 17940 1 478 . 1 1 145 145 ASP H H 1 8.19 0.02 . 1 . . . . 145 ASP H . 17940 1 479 . 1 1 145 145 ASP CA C 13 54.721 0.1 . 1 . . . . 145 ASP CA . 17940 1 480 . 1 1 145 145 ASP CB C 13 38.33 0.1 . 1 . . . . 145 ASP CB . 17940 1 481 . 1 1 145 145 ASP N N 15 115.105 0.1 . 1 . . . . 145 ASP N . 17940 1 482 . 1 1 156 156 LEU H H 1 7.07 0.02 . 1 . . . . 156 LEU H . 17940 1 483 . 1 1 156 156 LEU C C 13 175.471 0.1 . 1 . . . . 156 LEU C . 17940 1 484 . 1 1 156 156 LEU CA C 13 51.423 0.1 . 1 . . . . 156 LEU CA . 17940 1 485 . 1 1 156 156 LEU N N 15 119.414 0.1 . 1 . . . . 156 LEU N . 17940 1 486 . 1 1 157 157 ALA H H 1 8.537 0.02 . 1 . . . . 157 ALA H . 17940 1 487 . 1 1 157 157 ALA CA C 13 49.577 0.1 . 1 . . . . 157 ALA CA . 17940 1 488 . 1 1 157 157 ALA CB C 13 20.749 0.1 . 1 . . . . 157 ALA CB . 17940 1 489 . 1 1 157 157 ALA N N 15 125.164 0.1 . 1 . . . . 157 ALA N . 17940 1 490 . 1 1 158 158 VAL CA C 13 67.496 0.1 . 1 . . . . 158 VAL CA . 17940 1 491 . 1 1 175 175 THR C C 13 176.915 0.1 . 1 . . . . 175 THR C . 17940 1 492 . 1 1 175 175 THR CA C 13 62.246 0.1 . 1 . . . . 175 THR CA . 17940 1 493 . 1 1 175 175 THR CB C 13 63.104 0.1 . 1 . . . . 175 THR CB . 17940 1 494 . 1 1 176 176 ASP H H 1 8.352 0.02 . 1 . . . . 176 ASP H . 17940 1 495 . 1 1 176 176 ASP C C 13 175.896 0.1 . 1 . . . . 176 ASP C . 17940 1 496 . 1 1 176 176 ASP CA C 13 55.377 0.1 . 1 . . . . 176 ASP CA . 17940 1 497 . 1 1 176 176 ASP CB C 13 29.5 0.1 . 1 . . . . 176 ASP CB . 17940 1 498 . 1 1 176 176 ASP N N 15 122.004 0.1 . 1 . . . . 176 ASP N . 17940 1 499 . 1 1 177 177 ASP H H 1 8.359 0.02 . 1 . . . . 177 ASP H . 17940 1 500 . 1 1 177 177 ASP C C 13 176.509 0.1 . 1 . . . . 177 ASP C . 17940 1 501 . 1 1 177 177 ASP CA C 13 52.898 0.1 . 1 . . . . 177 ASP CA . 17940 1 502 . 1 1 177 177 ASP CB C 13 27.912 0.1 . 1 . . . . 177 ASP CB . 17940 1 503 . 1 1 177 177 ASP N N 15 122.642 0.1 . 1 . . . . 177 ASP N . 17940 1 504 . 1 1 178 178 GLU H H 1 8.83 0.02 . 1 . . . . 178 GLU H . 17940 1 505 . 1 1 178 178 GLU C C 13 174.23 0.1 . 1 . . . . 178 GLU C . 17940 1 506 . 1 1 178 178 GLU CA C 13 52.928 0.1 . 1 . . . . 178 GLU CA . 17940 1 507 . 1 1 178 178 GLU CB C 13 32.541 0.1 . 1 . . . . 178 GLU CB . 17940 1 508 . 1 1 178 178 GLU N N 15 117.549 0.1 . 1 . . . . 178 GLU N . 17940 1 509 . 1 1 179 179 MET H H 1 8.571 0.02 . 1 . . . . 179 MET H . 17940 1 510 . 1 1 179 179 MET C C 13 174.731 0.1 . 1 . . . . 179 MET C . 17940 1 511 . 1 1 179 179 MET CA C 13 52.92 0.1 . 1 . . . . 179 MET CA . 17940 1 512 . 1 1 179 179 MET CB C 13 32.463 0.1 . 1 . . . . 179 MET CB . 17940 1 513 . 1 1 179 179 MET N N 15 120.449 0.1 . 1 . . . . 179 MET N . 17940 1 514 . 1 1 180 180 THR H H 1 8.833 0.02 . 1 . . . . 180 THR H . 17940 1 515 . 1 1 180 180 THR C C 13 177.059 0.1 . 1 . . . . 180 THR C . 17940 1 516 . 1 1 180 180 THR CA C 13 63.12 0.1 . 1 . . . . 180 THR CA . 17940 1 517 . 1 1 180 180 THR CB C 13 68.853 0.1 . 1 . . . . 180 THR CB . 17940 1 518 . 1 1 180 180 THR N N 15 117.374 0.1 . 1 . . . . 180 THR N . 17940 1 519 . 1 1 181 181 GLY H H 1 8.259 0.02 . 1 . . . . 181 GLY H . 17940 1 520 . 1 1 181 181 GLY C C 13 174.168 0.1 . 1 . . . . 181 GLY C . 17940 1 521 . 1 1 181 181 GLY CA C 13 45.06 0.1 . 1 . . . . 181 GLY CA . 17940 1 522 . 1 1 181 181 GLY N N 15 108.384 0.1 . 1 . . . . 181 GLY N . 17940 1 523 . 1 1 182 182 TYR H H 1 7.716 0.02 . 1 . . . . 182 TYR H . 17940 1 524 . 1 1 182 182 TYR C C 13 176.14 0.1 . 1 . . . . 182 TYR C . 17940 1 525 . 1 1 182 182 TYR CA C 13 53.439 0.1 . 1 . . . . 182 TYR CA . 17940 1 526 . 1 1 182 182 TYR CB C 13 42.512 0.1 . 1 . . . . 182 TYR CB . 17940 1 527 . 1 1 182 182 TYR N N 15 121.649 0.1 . 1 . . . . 182 TYR N . 17940 1 528 . 1 1 183 183 VAL H H 1 8.118 0.02 . 1 . . . . 183 VAL H . 17940 1 529 . 1 1 183 183 VAL CA C 13 61.339 0.1 . 1 . . . . 183 VAL CA . 17940 1 530 . 1 1 183 183 VAL CB C 13 31.815 0.1 . 1 . . . . 183 VAL CB . 17940 1 531 . 1 1 183 183 VAL N N 15 125.111 0.1 . 1 . . . . 183 VAL N . 17940 1 532 . 1 1 206 206 ILE C C 13 177.975 0.1 . 1 . . . . 206 ILE C . 17940 1 533 . 1 1 207 207 TRP H H 1 7.529 0.02 . 1 . . . . 207 TRP H . 17940 1 534 . 1 1 207 207 TRP N N 15 121.064 0.1 . 1 . . . . 207 TRP N . 17940 1 535 . 1 1 208 208 SER C C 13 176.48 0.1 . 1 . . . . 208 SER C . 17940 1 536 . 1 1 208 208 SER CA C 13 61.708 0.1 . 1 . . . . 208 SER CA . 17940 1 537 . 1 1 209 209 VAL H H 1 8.019 0.02 . 1 . . . . 209 VAL H . 17940 1 538 . 1 1 209 209 VAL C C 13 177.085 0.1 . 1 . . . . 209 VAL C . 17940 1 539 . 1 1 209 209 VAL CA C 13 67.061 0.1 . 1 . . . . 209 VAL CA . 17940 1 540 . 1 1 209 209 VAL CB C 13 29.336 0.1 . 1 . . . . 209 VAL CB . 17940 1 541 . 1 1 209 209 VAL N N 15 119.904 0.1 . 1 . . . . 209 VAL N . 17940 1 542 . 1 1 210 210 GLY H H 1 8.541 0.02 . 1 . . . . 210 GLY H . 17940 1 543 . 1 1 210 210 GLY C C 13 174.586 0.1 . 1 . . . . 210 GLY C . 17940 1 544 . 1 1 210 210 GLY CA C 13 47.393 0.1 . 1 . . . . 210 GLY CA . 17940 1 545 . 1 1 210 210 GLY N N 15 110.328 0.1 . 1 . . . . 210 GLY N . 17940 1 546 . 1 1 211 211 CYS H H 1 7.938 0.02 . 1 . . . . 211 CYS H . 17940 1 547 . 1 1 211 211 CYS C C 13 179.153 0.1 . 1 . . . . 211 CYS C . 17940 1 548 . 1 1 211 211 CYS CA C 13 63.446 0.1 . 1 . . . . 211 CYS CA . 17940 1 549 . 1 1 211 211 CYS CB C 13 27.462 0.1 . 1 . . . . 211 CYS CB . 17940 1 550 . 1 1 211 211 CYS N N 15 119.114 0.1 . 1 . . . . 211 CYS N . 17940 1 551 . 1 1 212 212 ILE H H 1 8.449 0.02 . 1 . . . . 212 ILE H . 17940 1 552 . 1 1 212 212 ILE C C 13 176.278 0.1 . 1 . . . . 212 ILE C . 17940 1 553 . 1 1 212 212 ILE CA C 13 65.066 0.1 . 1 . . . . 212 ILE CA . 17940 1 554 . 1 1 212 212 ILE CB C 13 37.52 0.1 . 1 . . . . 212 ILE CB . 17940 1 555 . 1 1 212 212 ILE N N 15 124.304 0.1 . 1 . . . . 212 ILE N . 17940 1 556 . 1 1 213 213 MET H H 1 9.323 0.02 . 1 . . . . 213 MET H . 17940 1 557 . 1 1 213 213 MET C C 13 176.969 0.1 . 1 . . . . 213 MET C . 17940 1 558 . 1 1 213 213 MET CA C 13 59.622 0.1 . 1 . . . . 213 MET CA . 17940 1 559 . 1 1 213 213 MET CB C 13 31.041 0.1 . 1 . . . . 213 MET CB . 17940 1 560 . 1 1 213 213 MET N N 15 120.528 0.1 . 1 . . . . 213 MET N . 17940 1 561 . 1 1 214 214 ALA H H 1 8.189 0.02 . 1 . . . . 214 ALA H . 17940 1 562 . 1 1 214 214 ALA C C 13 178.823 0.1 . 1 . . . . 214 ALA C . 17940 1 563 . 1 1 214 214 ALA CA C 13 54.805 0.1 . 1 . . . . 214 ALA CA . 17940 1 564 . 1 1 214 214 ALA CB C 13 19.504 0.1 . 1 . . . . 214 ALA CB . 17940 1 565 . 1 1 214 214 ALA N N 15 118.323 0.1 . 1 . . . . 214 ALA N . 17940 1 566 . 1 1 215 215 GLU H H 1 7.155 0.02 . 1 . . . . 215 GLU H . 17940 1 567 . 1 1 215 215 GLU CA C 13 57.18 0.1 . 1 . . . . 215 GLU CA . 17940 1 568 . 1 1 215 215 GLU CB C 13 28.584 0.1 . 1 . . . . 215 GLU CB . 17940 1 569 . 1 1 215 215 GLU N N 15 120.016 0.1 . 1 . . . . 215 GLU N . 17940 1 570 . 1 1 216 216 LEU C C 13 178.846 0.1 . 1 . . . . 216 LEU C . 17940 1 571 . 1 1 216 216 LEU CA C 13 58.004 0.1 . 1 . . . . 216 LEU CA . 17940 1 572 . 1 1 216 216 LEU CB C 13 40.794 0.1 . 1 . . . . 216 LEU CB . 17940 1 573 . 1 1 217 217 LEU H H 1 7.853 0.02 . 1 . . . . 217 LEU H . 17940 1 574 . 1 1 217 217 LEU C C 13 179.369 0.1 . 1 . . . . 217 LEU C . 17940 1 575 . 1 1 217 217 LEU CA C 13 56.301 0.1 . 1 . . . . 217 LEU CA . 17940 1 576 . 1 1 217 217 LEU CB C 13 42.001 0.1 . 1 . . . . 217 LEU CB . 17940 1 577 . 1 1 217 217 LEU N N 15 115.897 0.1 . 1 . . . . 217 LEU N . 17940 1 578 . 1 1 218 218 THR H H 1 7.962 0.02 . 1 . . . . 218 THR H . 17940 1 579 . 1 1 218 218 THR C C 13 176.463 0.1 . 1 . . . . 218 THR C . 17940 1 580 . 1 1 218 218 THR CA C 13 61.553 0.1 . 1 . . . . 218 THR CA . 17940 1 581 . 1 1 218 218 THR CB C 13 71.339 0.1 . 1 . . . . 218 THR CB . 17940 1 582 . 1 1 218 218 THR N N 15 106.011 0.1 . 1 . . . . 218 THR N . 17940 1 583 . 1 1 219 219 GLY H H 1 8.454 0.02 . 1 . . . . 219 GLY H . 17940 1 584 . 1 1 219 219 GLY C C 13 173.395 0.1 . 1 . . . . 219 GLY C . 17940 1 585 . 1 1 219 219 GLY CA C 13 44.956 0.1 . 1 . . . . 219 GLY CA . 17940 1 586 . 1 1 219 219 GLY N N 15 112.802 0.1 . 1 . . . . 219 GLY N . 17940 1 587 . 1 1 220 220 ARG H H 1 8.032 0.02 . 1 . . . . 220 ARG H . 17940 1 588 . 1 1 220 220 ARG C C 13 174.478 0.1 . 1 . . . . 220 ARG C . 17940 1 589 . 1 1 220 220 ARG CA C 13 53.187 0.1 . 1 . . . . 220 ARG CA . 17940 1 590 . 1 1 220 220 ARG CB C 13 31.944 0.1 . 1 . . . . 220 ARG CB . 17940 1 591 . 1 1 220 220 ARG N N 15 119.089 0.1 . 1 . . . . 220 ARG N . 17940 1 592 . 1 1 221 221 THR H H 1 7.948 0.02 . 1 . . . . 221 THR H . 17940 1 593 . 1 1 221 221 THR C C 13 174.388 0.1 . 1 . . . . 221 THR C . 17940 1 594 . 1 1 221 221 THR CA C 13 63.014 0.1 . 1 . . . . 221 THR CA . 17940 1 595 . 1 1 221 221 THR CB C 13 68.86 0.1 . 1 . . . . 221 THR CB . 17940 1 596 . 1 1 221 221 THR N N 15 119.967 0.1 . 1 . . . . 221 THR N . 17940 1 597 . 1 1 222 222 LEU H H 1 7.856 0.02 . 1 . . . . 222 LEU H . 17940 1 598 . 1 1 222 222 LEU C C 13 177.546 0.1 . 1 . . . . 222 LEU C . 17940 1 599 . 1 1 222 222 LEU CA C 13 52.374 0.1 . 1 . . . . 222 LEU CA . 17940 1 600 . 1 1 222 222 LEU CB C 13 41.007 0.1 . 1 . . . . 222 LEU CB . 17940 1 601 . 1 1 222 222 LEU N N 15 117.881 0.1 . 1 . . . . 222 LEU N . 17940 1 602 . 1 1 223 223 PHE H H 1 9.448 0.02 . 1 . . . . 223 PHE H . 17940 1 603 . 1 1 223 223 PHE CA C 13 58.788 0.1 . 1 . . . . 223 PHE CA . 17940 1 604 . 1 1 223 223 PHE CB C 13 36.84 0.1 . 1 . . . . 223 PHE CB . 17940 1 605 . 1 1 223 223 PHE N N 15 130.026 0.1 . 1 . . . . 223 PHE N . 17940 1 606 . 1 1 224 224 PRO C C 13 178.28 0.1 . 1 . . . . 224 PRO C . 17940 1 607 . 1 1 224 224 PRO CA C 13 55.631 0.1 . 1 . . . . 224 PRO CA . 17940 1 608 . 1 1 225 225 GLY H H 1 8.373 0.02 . 1 . . . . 225 GLY H . 17940 1 609 . 1 1 225 225 GLY C C 13 176.175 0.1 . 1 . . . . 225 GLY C . 17940 1 610 . 1 1 225 225 GLY CA C 13 44.439 0.1 . 1 . . . . 225 GLY CA . 17940 1 611 . 1 1 225 225 GLY N N 15 113.907 0.1 . 1 . . . . 225 GLY N . 17940 1 612 . 1 1 226 226 THR H H 1 10.134 0.02 . 1 . . . . 226 THR H . 17940 1 613 . 1 1 226 226 THR CA C 13 61.677 0.1 . 1 . . . . 226 THR CA . 17940 1 614 . 1 1 226 226 THR CB C 13 64.997 0.1 . 1 . . . . 226 THR CB . 17940 1 615 . 1 1 226 226 THR N N 15 116.918 0.1 . 1 . . . . 226 THR N . 17940 1 616 . 1 1 254 254 SER C C 13 177.601 0.1 . 1 . . . . 254 SER C . 17940 1 617 . 1 1 254 254 SER CA C 13 60.285 0.1 . 1 . . . . 254 SER CA . 17940 1 618 . 1 1 254 254 SER CB C 13 69.291 0.1 . 1 . . . . 254 SER CB . 17940 1 619 . 1 1 255 255 ALA H H 1 7.716 0.02 . 1 . . . . 255 ALA H . 17940 1 620 . 1 1 255 255 ALA CA C 13 53.98 0.1 . 1 . . . . 255 ALA CA . 17940 1 621 . 1 1 255 255 ALA CB C 13 17.746 0.1 . 1 . . . . 255 ALA CB . 17940 1 622 . 1 1 255 255 ALA N N 15 125.593 0.1 . 1 . . . . 255 ALA N . 17940 1 623 . 1 1 259 259 ILE C C 13 178.286 0.1 . 1 . . . . 259 ILE C . 17940 1 624 . 1 1 260 260 GLN H H 1 8.121 0.02 . 1 . . . . 260 GLN H . 17940 1 625 . 1 1 260 260 GLN C C 13 176.301 0.1 . 1 . . . . 260 GLN C . 17940 1 626 . 1 1 260 260 GLN CA C 13 57.699 0.1 . 1 . . . . 260 GLN CA . 17940 1 627 . 1 1 260 260 GLN CB C 13 27.273 0.1 . 1 . . . . 260 GLN CB . 17940 1 628 . 1 1 260 260 GLN N N 15 118.169 0.1 . 1 . . . . 260 GLN N . 17940 1 629 . 1 1 261 261 SER H H 1 7.47 0.02 . 1 . . . . 261 SER H . 17940 1 630 . 1 1 261 261 SER C C 13 174.153 0.1 . 1 . . . . 261 SER C . 17940 1 631 . 1 1 261 261 SER CA C 13 58.793 0.1 . 1 . . . . 261 SER CA . 17940 1 632 . 1 1 261 261 SER CB C 13 63.151 0.1 . 1 . . . . 261 SER CB . 17940 1 633 . 1 1 261 261 SER N N 15 114.073 0.1 . 1 . . . . 261 SER N . 17940 1 634 . 1 1 262 262 LEU H H 1 6.995 0.02 . 1 . . . . 262 LEU H . 17940 1 635 . 1 1 262 262 LEU C C 13 177.221 0.1 . 1 . . . . 262 LEU C . 17940 1 636 . 1 1 262 262 LEU CA C 13 53.747 0.1 . 1 . . . . 262 LEU CA . 17940 1 637 . 1 1 262 262 LEU CB C 13 41.192 0.1 . 1 . . . . 262 LEU CB . 17940 1 638 . 1 1 262 262 LEU N N 15 123.13 0.1 . 1 . . . . 262 LEU N . 17940 1 639 . 1 1 263 263 ALA H H 1 8.054 0.02 . 1 . . . . 263 ALA H . 17940 1 640 . 1 1 263 263 ALA C C 13 175.434 0.1 . 1 . . . . 263 ALA C . 17940 1 641 . 1 1 263 263 ALA CA C 13 51.858 0.1 . 1 . . . . 263 ALA CA . 17940 1 642 . 1 1 263 263 ALA CB C 13 17.487 0.1 . 1 . . . . 263 ALA CB . 17940 1 643 . 1 1 263 263 ALA N N 15 124.239 0.1 . 1 . . . . 263 ALA N . 17940 1 644 . 1 1 264 264 GLN H H 1 8.246 0.02 . 1 . . . . 264 GLN H . 17940 1 645 . 1 1 264 264 GLN C C 13 176.213 0.1 . 1 . . . . 264 GLN C . 17940 1 646 . 1 1 264 264 GLN CA C 13 53.909 0.1 . 1 . . . . 264 GLN CA . 17940 1 647 . 1 1 264 264 GLN CB C 13 28.246 0.1 . 1 . . . . 264 GLN CB . 17940 1 648 . 1 1 264 264 GLN N N 15 119.579 0.1 . 1 . . . . 264 GLN N . 17940 1 649 . 1 1 265 265 MET H H 1 8.726 0.02 . 1 . . . . 265 MET H . 17940 1 650 . 1 1 265 265 MET CA C 13 54.473 0.1 . 1 . . . . 265 MET CA . 17940 1 651 . 1 1 265 265 MET N N 15 124.682 0.1 . 1 . . . . 265 MET N . 17940 1 652 . 1 1 266 266 PRO C C 13 175.868 0.1 . 1 . . . . 266 PRO C . 17940 1 653 . 1 1 266 266 PRO CA C 13 61.087 0.1 . 1 . . . . 266 PRO CA . 17940 1 654 . 1 1 266 266 PRO CB C 13 30.967 0.1 . 1 . . . . 266 PRO CB . 17940 1 655 . 1 1 267 267 LYS H H 1 8.282 0.02 . 1 . . . . 267 LYS H . 17940 1 656 . 1 1 267 267 LYS C C 13 177.691 0.1 . 1 . . . . 267 LYS C . 17940 1 657 . 1 1 267 267 LYS CA C 13 56.057 0.1 . 1 . . . . 267 LYS CA . 17940 1 658 . 1 1 267 267 LYS CB C 13 32.237 0.1 . 1 . . . . 267 LYS CB . 17940 1 659 . 1 1 267 267 LYS N N 15 120.658 0.1 . 1 . . . . 267 LYS N . 17940 1 660 . 1 1 268 268 MET H H 1 8.427 0.02 . 1 . . . . 268 MET H . 17940 1 661 . 1 1 268 268 MET C C 13 174.478 0.1 . 1 . . . . 268 MET C . 17940 1 662 . 1 1 268 268 MET CA C 13 55.243 0.1 . 1 . . . . 268 MET CA . 17940 1 663 . 1 1 268 268 MET CB C 13 32.241 0.1 . 1 . . . . 268 MET CB . 17940 1 664 . 1 1 268 268 MET N N 15 126.083 0.1 . 1 . . . . 268 MET N . 17940 1 665 . 1 1 269 269 ASN H H 1 8.652 0.02 . 1 . . . . 269 ASN H . 17940 1 666 . 1 1 269 269 ASN C C 13 176.084 0.1 . 1 . . . . 269 ASN C . 17940 1 667 . 1 1 269 269 ASN CA C 13 50.947 0.1 . 1 . . . . 269 ASN CA . 17940 1 668 . 1 1 269 269 ASN CB C 13 39.821 0.1 . 1 . . . . 269 ASN CB . 17940 1 669 . 1 1 269 269 ASN N N 15 130.749 0.1 . 1 . . . . 269 ASN N . 17940 1 670 . 1 1 270 270 PHE H H 1 8.572 0.02 . 1 . . . . 270 PHE H . 17940 1 671 . 1 1 270 270 PHE C C 13 177.925 0.1 . 1 . . . . 270 PHE C . 17940 1 672 . 1 1 270 270 PHE CA C 13 59.174 0.1 . 1 . . . . 270 PHE CA . 17940 1 673 . 1 1 270 270 PHE CB C 13 39.591 0.1 . 1 . . . . 270 PHE CB . 17940 1 674 . 1 1 270 270 PHE N N 15 114.416 0.1 . 1 . . . . 270 PHE N . 17940 1 675 . 1 1 271 271 ALA H H 1 8.561 0.02 . 1 . . . . 271 ALA H . 17940 1 676 . 1 1 271 271 ALA C C 13 178.611 0.1 . 1 . . . . 271 ALA C . 17940 1 677 . 1 1 271 271 ALA CA C 13 53.752 0.1 . 1 . . . . 271 ALA CA . 17940 1 678 . 1 1 271 271 ALA CB C 13 16.78 0.1 . 1 . . . . 271 ALA CB . 17940 1 679 . 1 1 271 271 ALA N N 15 122.315 0.1 . 1 . . . . 271 ALA N . 17940 1 680 . 1 1 272 272 ASN H H 1 7.483 0.02 . 1 . . . . 272 ASN H . 17940 1 681 . 1 1 272 272 ASN C C 13 175.344 0.1 . 1 . . . . 272 ASN C . 17940 1 682 . 1 1 272 272 ASN CA C 13 52.827 0.1 . 1 . . . . 272 ASN CA . 17940 1 683 . 1 1 272 272 ASN CB C 13 37.935 0.1 . 1 . . . . 272 ASN CB . 17940 1 684 . 1 1 272 272 ASN N N 15 113.241 0.1 . 1 . . . . 272 ASN N . 17940 1 685 . 1 1 273 273 VAL H H 1 7.235 0.02 . 1 . . . . 273 VAL H . 17940 1 686 . 1 1 273 273 VAL C C 13 176.499 0.1 . 1 . . . . 273 VAL C . 17940 1 687 . 1 1 273 273 VAL CA C 13 63.471 0.1 . 1 . . . . 273 VAL CA . 17940 1 688 . 1 1 273 273 VAL CB C 13 31.837 0.1 . 1 . . . . 273 VAL CB . 17940 1 689 . 1 1 273 273 VAL N N 15 120.104 0.1 . 1 . . . . 273 VAL N . 17940 1 690 . 1 1 274 274 PHE H H 1 7.635 0.02 . 1 . . . . 274 PHE H . 17940 1 691 . 1 1 274 274 PHE C C 13 175.471 0.1 . 1 . . . . 274 PHE C . 17940 1 692 . 1 1 274 274 PHE CA C 13 55.22 0.1 . 1 . . . . 274 PHE CA . 17940 1 693 . 1 1 274 274 PHE CB C 13 36.094 0.1 . 1 . . . . 274 PHE CB . 17940 1 694 . 1 1 274 274 PHE N N 15 120.723 0.1 . 1 . . . . 274 PHE N . 17940 1 695 . 1 1 275 275 ILE H H 1 6.9 0.02 . 1 . . . . 275 ILE H . 17940 1 696 . 1 1 275 275 ILE C C 13 177.889 0.1 . 1 . . . . 275 ILE C . 17940 1 697 . 1 1 275 275 ILE CA C 13 61.579 0.1 . 1 . . . . 275 ILE CA . 17940 1 698 . 1 1 275 275 ILE CB C 13 36.596 0.1 . 1 . . . . 275 ILE CB . 17940 1 699 . 1 1 275 275 ILE N N 15 120.929 0.1 . 1 . . . . 275 ILE N . 17940 1 700 . 1 1 276 276 GLY H H 1 9.012 0.02 . 1 . . . . 276 GLY H . 17940 1 701 . 1 1 276 276 GLY C C 13 173.99 0.1 . 1 . . . . 276 GLY C . 17940 1 702 . 1 1 276 276 GLY CA C 13 44.198 0.1 . 1 . . . . 276 GLY CA . 17940 1 703 . 1 1 276 276 GLY N N 15 116.306 0.1 . 1 . . . . 276 GLY N . 17940 1 704 . 1 1 277 277 ALA H H 1 7.438 0.02 . 1 . . . . 277 ALA H . 17940 1 705 . 1 1 277 277 ALA C C 13 176.915 0.1 . 1 . . . . 277 ALA C . 17940 1 706 . 1 1 277 277 ALA CA C 13 50.418 0.1 . 1 . . . . 277 ALA CA . 17940 1 707 . 1 1 277 277 ALA CB C 13 18.843 0.1 . 1 . . . . 277 ALA CB . 17940 1 708 . 1 1 277 277 ALA N N 15 122.042 0.1 . 1 . . . . 277 ALA N . 17940 1 709 . 1 1 278 278 ASN H H 1 9.101 0.02 . 1 . . . . 278 ASN H . 17940 1 710 . 1 1 278 278 ASN CA C 13 50.39 0.1 . 1 . . . . 278 ASN CA . 17940 1 711 . 1 1 278 278 ASN CB C 13 38.628 0.1 . 1 . . . . 278 ASN CB . 17940 1 712 . 1 1 278 278 ASN N N 15 122.591 0.1 . 1 . . . . 278 ASN N . 17940 1 713 . 1 1 279 279 PRO C C 13 179.893 0.1 . 1 . . . . 279 PRO C . 17940 1 714 . 1 1 279 279 PRO CA C 13 64.533 0.1 . 1 . . . . 279 PRO CA . 17940 1 715 . 1 1 279 279 PRO CB C 13 31.335 0.1 . 1 . . . . 279 PRO CB . 17940 1 716 . 1 1 280 280 LEU H H 1 8.462 0.02 . 1 . . . . 280 LEU H . 17940 1 717 . 1 1 280 280 LEU C C 13 178.684 0.1 . 1 . . . . 280 LEU C . 17940 1 718 . 1 1 280 280 LEU CA C 13 56.397 0.1 . 1 . . . . 280 LEU CA . 17940 1 719 . 1 1 280 280 LEU CB C 13 41.704 0.1 . 1 . . . . 280 LEU CB . 17940 1 720 . 1 1 280 280 LEU N N 15 117.197 0.1 . 1 . . . . 280 LEU N . 17940 1 721 . 1 1 281 281 ALA H H 1 7.133 0.02 . 1 . . . . 281 ALA H . 17940 1 722 . 1 1 281 281 ALA C C 13 178.972 0.1 . 1 . . . . 281 ALA C . 17940 1 723 . 1 1 281 281 ALA CA C 13 53.147 0.1 . 1 . . . . 281 ALA CA . 17940 1 724 . 1 1 281 281 ALA CB C 13 16.767 0.1 . 1 . . . . 281 ALA CB . 17940 1 725 . 1 1 281 281 ALA N N 15 121.128 0.1 . 1 . . . . 281 ALA N . 17940 1 726 . 1 1 282 282 VAL H H 1 7.114 0.02 . 1 . . . . 282 VAL H . 17940 1 727 . 1 1 282 282 VAL C C 13 176.283 0.1 . 1 . . . . 282 VAL C . 17940 1 728 . 1 1 282 282 VAL CA C 13 65.984 0.1 . 1 . . . . 282 VAL CA . 17940 1 729 . 1 1 282 282 VAL CB C 13 30.298 0.1 . 1 . . . . 282 VAL CB . 17940 1 730 . 1 1 282 282 VAL N N 15 116.421 0.1 . 1 . . . . 282 VAL N . 17940 1 731 . 1 1 290 290 VAL C C 13 176.77 0.1 . 1 . . . . 290 VAL C . 17940 1 732 . 1 1 290 290 VAL CA C 13 66.113 0.1 . 1 . . . . 290 VAL CA . 17940 1 733 . 1 1 290 290 VAL CB C 13 30.263 0.1 . 1 . . . . 290 VAL CB . 17940 1 734 . 1 1 291 291 LEU H H 1 7.512 0.02 . 1 . . . . 291 LEU H . 17940 1 735 . 1 1 291 291 LEU CA C 13 57.281 0.1 . 1 . . . . 291 LEU CA . 17940 1 736 . 1 1 291 291 LEU CB C 13 42.589 0.1 . 1 . . . . 291 LEU CB . 17940 1 737 . 1 1 291 291 LEU N N 15 118.023 0.1 . 1 . . . . 291 LEU N . 17940 1 738 . 1 1 294 294 ASP C C 13 177.077 0.1 . 1 . . . . 294 ASP C . 17940 1 739 . 1 1 294 294 ASP CA C 13 55.711 0.1 . 1 . . . . 294 ASP CA . 17940 1 740 . 1 1 295 295 LYS H H 1 7.651 0.02 . 1 . . . . 295 LYS H . 17940 1 741 . 1 1 295 295 LYS C C 13 176.283 0.1 . 1 . . . . 295 LYS C . 17940 1 742 . 1 1 295 295 LYS CA C 13 54.282 0.1 . 1 . . . . 295 LYS CA . 17940 1 743 . 1 1 295 295 LYS CB C 13 32.651 0.1 . 1 . . . . 295 LYS CB . 17940 1 744 . 1 1 295 295 LYS N N 15 117.449 0.1 . 1 . . . . 295 LYS N . 17940 1 745 . 1 1 296 296 ARG H H 1 7.07 0.02 . 1 . . . . 296 ARG H . 17940 1 746 . 1 1 296 296 ARG C C 13 174.64 0.1 . 1 . . . . 296 ARG C . 17940 1 747 . 1 1 296 296 ARG CA C 13 56.791 0.1 . 1 . . . . 296 ARG CA . 17940 1 748 . 1 1 296 296 ARG CB C 13 29.534 0.1 . 1 . . . . 296 ARG CB . 17940 1 749 . 1 1 296 296 ARG N N 15 122.488 0.1 . 1 . . . . 296 ARG N . 17940 1 750 . 1 1 297 297 ILE H H 1 7.102 0.02 . 1 . . . . 297 ILE H . 17940 1 751 . 1 1 297 297 ILE C C 13 172.023 0.1 . 1 . . . . 297 ILE C . 17940 1 752 . 1 1 297 297 ILE N N 15 125.047 0.1 . 1 . . . . 297 ILE N . 17940 1 753 . 1 1 298 298 THR H H 1 7.392 0.02 . 1 . . . . 298 THR H . 17940 1 754 . 1 1 298 298 THR C C 13 175.94 0.1 . 1 . . . . 298 THR C . 17940 1 755 . 1 1 298 298 THR CA C 13 59.565 0.1 . 1 . . . . 298 THR CA . 17940 1 756 . 1 1 298 298 THR CB C 13 70.819 0.1 . 1 . . . . 298 THR CB . 17940 1 757 . 1 1 298 298 THR N N 15 109.234 0.1 . 1 . . . . 298 THR N . 17940 1 758 . 1 1 299 299 ALA H H 1 9.529 0.02 . 1 . . . . 299 ALA H . 17940 1 759 . 1 1 299 299 ALA C C 13 178.774 0.1 . 1 . . . . 299 ALA C . 17940 1 760 . 1 1 299 299 ALA CA C 13 55.836 0.1 . 1 . . . . 299 ALA CA . 17940 1 761 . 1 1 299 299 ALA CB C 13 15.656 0.1 . 1 . . . . 299 ALA CB . 17940 1 762 . 1 1 299 299 ALA N N 15 122.251 0.1 . 1 . . . . 299 ALA N . 17940 1 763 . 1 1 300 300 ALA H H 1 8.653 0.02 . 1 . . . . 300 ALA H . 17940 1 764 . 1 1 300 300 ALA C C 13 180.633 0.1 . 1 . . . . 300 ALA C . 17940 1 765 . 1 1 300 300 ALA CA C 13 54.477 0.1 . 1 . . . . 300 ALA CA . 17940 1 766 . 1 1 300 300 ALA CB C 13 17.436 0.1 . 1 . . . . 300 ALA CB . 17940 1 767 . 1 1 300 300 ALA N N 15 116.194 0.1 . 1 . . . . 300 ALA N . 17940 1 768 . 1 1 301 301 GLN H H 1 7.445 0.02 . 1 . . . . 301 GLN H . 17940 1 769 . 1 1 301 301 GLN C C 13 179.55 0.1 . 1 . . . . 301 GLN C . 17940 1 770 . 1 1 301 301 GLN CA C 13 57.377 0.1 . 1 . . . . 301 GLN CA . 17940 1 771 . 1 1 301 301 GLN CB C 13 28.01 0.1 . 1 . . . . 301 GLN CB . 17940 1 772 . 1 1 301 301 GLN N N 15 116.039 0.1 . 1 . . . . 301 GLN N . 17940 1 773 . 1 1 302 302 ALA H H 1 8.711 0.02 . 1 . . . . 302 ALA H . 17940 1 774 . 1 1 302 302 ALA C C 13 178.936 0.1 . 1 . . . . 302 ALA C . 17940 1 775 . 1 1 302 302 ALA CA C 13 54.307 0.1 . 1 . . . . 302 ALA CA . 17940 1 776 . 1 1 302 302 ALA CB C 13 18.424 0.1 . 1 . . . . 302 ALA CB . 17940 1 777 . 1 1 302 302 ALA N N 15 123.83 0.1 . 1 . . . . 302 ALA N . 17940 1 778 . 1 1 303 303 LEU H H 1 7.679 0.02 . 1 . . . . 303 LEU H . 17940 1 779 . 1 1 303 303 LEU C C 13 175.814 0.1 . 1 . . . . 303 LEU C . 17940 1 780 . 1 1 303 303 LEU CA C 13 57.01 0.1 . 1 . . . . 303 LEU CA . 17940 1 781 . 1 1 303 303 LEU CB C 13 40.904 0.1 . 1 . . . . 303 LEU CB . 17940 1 782 . 1 1 303 303 LEU N N 15 116.261 0.1 . 1 . . . . 303 LEU N . 17940 1 783 . 1 1 304 304 ALA H H 1 6.661 0.02 . 1 . . . . 304 ALA H . 17940 1 784 . 1 1 304 304 ALA C C 13 176.734 0.1 . 1 . . . . 304 ALA C . 17940 1 785 . 1 1 304 304 ALA CA C 13 50.411 0.1 . 1 . . . . 304 ALA CA . 17940 1 786 . 1 1 304 304 ALA CB C 13 17.983 0.1 . 1 . . . . 304 ALA CB . 17940 1 787 . 1 1 304 304 ALA N N 15 115.372 0.1 . 1 . . . . 304 ALA N . 17940 1 788 . 1 1 305 305 HIS H H 1 7.988 0.02 . 1 . . . . 305 HIS H . 17940 1 789 . 1 1 305 305 HIS C C 13 177.33 0.1 . 1 . . . . 305 HIS C . 17940 1 790 . 1 1 305 305 HIS CA C 13 58.25 0.1 . 1 . . . . 305 HIS CA . 17940 1 791 . 1 1 305 305 HIS CB C 13 32.117 0.1 . 1 . . . . 305 HIS CB . 17940 1 792 . 1 1 305 305 HIS N N 15 122.726 0.1 . 1 . . . . 305 HIS N . 17940 1 793 . 1 1 306 306 ALA H H 1 8.35 0.02 . 1 . . . . 306 ALA H . 17940 1 794 . 1 1 306 306 ALA C C 13 179.333 0.1 . 1 . . . . 306 ALA C . 17940 1 795 . 1 1 306 306 ALA CA C 13 54.727 0.1 . 1 . . . . 306 ALA CA . 17940 1 796 . 1 1 306 306 ALA CB C 13 18.055 0.1 . 1 . . . . 306 ALA CB . 17940 1 797 . 1 1 306 306 ALA N N 15 132.765 0.1 . 1 . . . . 306 ALA N . 17940 1 798 . 1 1 307 307 TYR H H 1 11.672 0.02 . 1 . . . . 307 TYR H . 17940 1 799 . 1 1 307 307 TYR C C 13 176.211 0.1 . 1 . . . . 307 TYR C . 17940 1 800 . 1 1 307 307 TYR CA C 13 59.591 0.1 . 1 . . . . 307 TYR CA . 17940 1 801 . 1 1 307 307 TYR CB C 13 37.733 0.1 . 1 . . . . 307 TYR CB . 17940 1 802 . 1 1 307 307 TYR N N 15 125.113 0.1 . 1 . . . . 307 TYR N . 17940 1 803 . 1 1 308 308 PHE H H 1 7.696 0.02 . 1 . . . . 308 PHE H . 17940 1 804 . 1 1 308 308 PHE C C 13 176.915 0.1 . 1 . . . . 308 PHE C . 17940 1 805 . 1 1 308 308 PHE CA C 13 55.179 0.1 . 1 . . . . 308 PHE CA . 17940 1 806 . 1 1 308 308 PHE CB C 13 37.979 0.1 . 1 . . . . 308 PHE CB . 17940 1 807 . 1 1 308 308 PHE N N 15 110.604 0.1 . 1 . . . . 308 PHE N . 17940 1 808 . 1 1 309 309 ALA H H 1 7.561 0.02 . 1 . . . . 309 ALA H . 17940 1 809 . 1 1 309 309 ALA C C 13 179.045 0.1 . 1 . . . . 309 ALA C . 17940 1 810 . 1 1 309 309 ALA CA C 13 54.998 0.1 . 1 . . . . 309 ALA CA . 17940 1 811 . 1 1 309 309 ALA CB C 13 18.078 0.1 . 1 . . . . 309 ALA CB . 17940 1 812 . 1 1 309 309 ALA N N 15 123.686 0.1 . 1 . . . . 309 ALA N . 17940 1 813 . 1 1 310 310 GLN H H 1 8.671 0.02 . 1 . . . . 310 GLN H . 17940 1 814 . 1 1 310 310 GLN C C 13 175.344 0.1 . 1 . . . . 310 GLN C . 17940 1 815 . 1 1 310 310 GLN CA C 13 56.438 0.1 . 1 . . . . 310 GLN CA . 17940 1 816 . 1 1 310 310 GLN CB C 13 27.322 0.1 . 1 . . . . 310 GLN CB . 17940 1 817 . 1 1 310 310 GLN N N 15 114.054 0.1 . 1 . . . . 310 GLN N . 17940 1 818 . 1 1 311 311 TYR H H 1 7.478 0.02 . 1 . . . . 311 TYR H . 17940 1 819 . 1 1 311 311 TYR C C 13 177.98 0.1 . 1 . . . . 311 TYR C . 17940 1 820 . 1 1 311 311 TYR CA C 13 57.792 0.1 . 1 . . . . 311 TYR CA . 17940 1 821 . 1 1 311 311 TYR CB C 13 39.585 0.1 . 1 . . . . 311 TYR CB . 17940 1 822 . 1 1 311 311 TYR N N 15 115.945 0.1 . 1 . . . . 311 TYR N . 17940 1 823 . 1 1 314 314 PRO C C 13 177.98 0.1 . 1 . . . . 314 PRO C . 17940 1 824 . 1 1 314 314 PRO CA C 13 63.254 0.1 . 1 . . . . 314 PRO CA . 17940 1 825 . 1 1 314 314 PRO CB C 13 30.935 0.1 . 1 . . . . 314 PRO CB . 17940 1 826 . 1 1 315 315 ASP H H 1 7.99 0.02 . 1 . . . . 315 ASP H . 17940 1 827 . 1 1 315 315 ASP C C 13 175.832 0.1 . 1 . . . . 315 ASP C . 17940 1 828 . 1 1 315 315 ASP CA C 13 54.687 0.1 . 1 . . . . 315 ASP CA . 17940 1 829 . 1 1 315 315 ASP CB C 13 39.945 0.1 . 1 . . . . 315 ASP CB . 17940 1 830 . 1 1 315 315 ASP N N 15 117.456 0.1 . 1 . . . . 315 ASP N . 17940 1 831 . 1 1 316 316 ASP H H 1 8.03 0.02 . 1 . . . . 316 ASP H . 17940 1 832 . 1 1 316 316 ASP C C 13 175.868 0.1 . 1 . . . . 316 ASP C . 17940 1 833 . 1 1 316 316 ASP CA C 13 52.061 0.1 . 1 . . . . 316 ASP CA . 17940 1 834 . 1 1 316 316 ASP CB C 13 41.675 0.1 . 1 . . . . 316 ASP CB . 17940 1 835 . 1 1 316 316 ASP N N 15 121.204 0.1 . 1 . . . . 316 ASP N . 17940 1 836 . 1 1 317 317 GLU H H 1 7.792 0.02 . 1 . . . . 317 GLU H . 17940 1 837 . 1 1 317 317 GLU CA C 13 53.007 0.1 . 1 . . . . 317 GLU CA . 17940 1 838 . 1 1 317 317 GLU CB C 13 28.863 0.1 . 1 . . . . 317 GLU CB . 17940 1 839 . 1 1 317 317 GLU N N 15 121.453 0.1 . 1 . . . . 317 GLU N . 17940 1 840 . 1 1 318 318 PRO C C 13 177.131 0.1 . 1 . . . . 318 PRO C . 17940 1 841 . 1 1 318 318 PRO CA C 13 62.838 0.1 . 1 . . . . 318 PRO CA . 17940 1 842 . 1 1 318 318 PRO CB C 13 32.718 0.1 . 1 . . . . 318 PRO CB . 17940 1 843 . 1 1 319 319 VAL H H 1 7.87 0.02 . 1 . . . . 319 VAL H . 17940 1 844 . 1 1 319 319 VAL C C 13 175.073 0.1 . 1 . . . . 319 VAL C . 17940 1 845 . 1 1 319 319 VAL CA C 13 58.813 0.1 . 1 . . . . 319 VAL CA . 17940 1 846 . 1 1 319 319 VAL CB C 13 33.131 0.1 . 1 . . . . 319 VAL CB . 17940 1 847 . 1 1 319 319 VAL N N 15 109.286 0.1 . 1 . . . . 319 VAL N . 17940 1 848 . 1 1 320 320 ALA H H 1 8.47 0.02 . 1 . . . . 320 ALA H . 17940 1 849 . 1 1 320 320 ALA C C 13 178.611 0.1 . 1 . . . . 320 ALA C . 17940 1 850 . 1 1 320 320 ALA CA C 13 50.075 0.1 . 1 . . . . 320 ALA CA . 17940 1 851 . 1 1 320 320 ALA CB C 13 19.329 0.1 . 1 . . . . 320 ALA CB . 17940 1 852 . 1 1 320 320 ALA N N 15 123.674 0.1 . 1 . . . . 320 ALA N . 17940 1 853 . 1 1 321 321 ASP H H 1 8.063 0.02 . 1 . . . . 321 ASP H . 17940 1 854 . 1 1 321 321 ASP CA C 13 53.445 0.1 . 1 . . . . 321 ASP CA . 17940 1 855 . 1 1 321 321 ASP CB C 13 38.767 0.1 . 1 . . . . 321 ASP CB . 17940 1 856 . 1 1 321 321 ASP N N 15 120.833 0.1 . 1 . . . . 321 ASP N . 17940 1 857 . 1 1 326 326 SER C C 13 176.842 0.1 . 1 . . . . 326 SER C . 17940 1 858 . 1 1 326 326 SER CA C 13 63.023 0.1 . 1 . . . . 326 SER CA . 17940 1 859 . 1 1 326 326 SER CB C 13 66.147 0.1 . 1 . . . . 326 SER CB . 17940 1 860 . 1 1 327 327 PHE H H 1 7.815 0.02 . 1 . . . . 327 PHE H . 17940 1 861 . 1 1 327 327 PHE CA C 13 58.652 0.1 . 1 . . . . 327 PHE CA . 17940 1 862 . 1 1 327 327 PHE N N 15 118.994 0.1 . 1 . . . . 327 PHE N . 17940 1 863 . 1 1 328 328 GLU C C 13 178.611 0.1 . 1 . . . . 328 GLU C . 17940 1 864 . 1 1 329 329 SER H H 1 7.465 0.02 . 1 . . . . 329 SER H . 17940 1 865 . 1 1 329 329 SER C C 13 174.37 0.1 . 1 . . . . 329 SER C . 17940 1 866 . 1 1 329 329 SER CA C 13 57.314 0.1 . 1 . . . . 329 SER CA . 17940 1 867 . 1 1 329 329 SER CB C 13 63.105 0.1 . 1 . . . . 329 SER CB . 17940 1 868 . 1 1 329 329 SER N N 15 111.88 0.1 . 1 . . . . 329 SER N . 17940 1 869 . 1 1 330 330 ARG H H 1 7.634 0.02 . 1 . . . . 330 ARG H . 17940 1 870 . 1 1 330 330 ARG C C 13 175.073 0.1 . 1 . . . . 330 ARG C . 17940 1 871 . 1 1 330 330 ARG CA C 13 55.392 0.1 . 1 . . . . 330 ARG CA . 17940 1 872 . 1 1 330 330 ARG CB C 13 30.226 0.1 . 1 . . . . 330 ARG CB . 17940 1 873 . 1 1 330 330 ARG N N 15 121.918 0.1 . 1 . . . . 330 ARG N . 17940 1 874 . 1 1 331 331 ASP H H 1 8.561 0.02 . 1 . . . . 331 ASP H . 17940 1 875 . 1 1 331 331 ASP C C 13 174.37 0.1 . 1 . . . . 331 ASP C . 17940 1 876 . 1 1 331 331 ASP CA C 13 52.088 0.1 . 1 . . . . 331 ASP CA . 17940 1 877 . 1 1 331 331 ASP CB C 13 40.527 0.1 . 1 . . . . 331 ASP CB . 17940 1 878 . 1 1 331 331 ASP N N 15 124.757 0.1 . 1 . . . . 331 ASP N . 17940 1 879 . 1 1 332 332 LEU H H 1 7.833 0.02 . 1 . . . . 332 LEU H . 17940 1 880 . 1 1 332 332 LEU C C 13 177.005 0.1 . 1 . . . . 332 LEU C . 17940 1 881 . 1 1 332 332 LEU CA C 13 52.328 0.1 . 1 . . . . 332 LEU CA . 17940 1 882 . 1 1 332 332 LEU CB C 13 41.234 0.1 . 1 . . . . 332 LEU CB . 17940 1 883 . 1 1 332 332 LEU N N 15 123.212 0.1 . 1 . . . . 332 LEU N . 17940 1 884 . 1 1 333 333 LEU H H 1 8.796 0.02 . 1 . . . . 333 LEU H . 17940 1 885 . 1 1 333 333 LEU C C 13 179.785 0.1 . 1 . . . . 333 LEU C . 17940 1 886 . 1 1 333 333 LEU CA C 13 53.394 0.1 . 1 . . . . 333 LEU CA . 17940 1 887 . 1 1 333 333 LEU CB C 13 41.46 0.1 . 1 . . . . 333 LEU CB . 17940 1 888 . 1 1 333 333 LEU N N 15 119.962 0.1 . 1 . . . . 333 LEU N . 17940 1 889 . 1 1 334 334 ILE H H 1 8.989 0.02 . 1 . . . . 334 ILE H . 17940 1 890 . 1 1 334 334 ILE C C 13 177.366 0.1 . 1 . . . . 334 ILE C . 17940 1 891 . 1 1 334 334 ILE CA C 13 66.415 0.1 . 1 . . . . 334 ILE CA . 17940 1 892 . 1 1 334 334 ILE CB C 13 37.068 0.1 . 1 . . . . 334 ILE CB . 17940 1 893 . 1 1 334 334 ILE N N 15 121.824 0.1 . 1 . . . . 334 ILE N . 17940 1 894 . 1 1 335 335 ASP H H 1 8.386 0.02 . 1 . . . . 335 ASP H . 17940 1 895 . 1 1 335 335 ASP C C 13 178.954 0.1 . 1 . . . . 335 ASP C . 17940 1 896 . 1 1 335 335 ASP CA C 13 56.651 0.1 . 1 . . . . 335 ASP CA . 17940 1 897 . 1 1 335 335 ASP CB C 13 39.299 0.1 . 1 . . . . 335 ASP CB . 17940 1 898 . 1 1 335 335 ASP N N 15 116.044 0.1 . 1 . . . . 335 ASP N . 17940 1 899 . 1 1 336 336 GLU H H 1 7.146 0.02 . 1 . . . . 336 GLU H . 17940 1 900 . 1 1 336 336 GLU C C 13 179.063 0.1 . 1 . . . . 336 GLU C . 17940 1 901 . 1 1 336 336 GLU CA C 13 58.014 0.1 . 1 . . . . 336 GLU CA . 17940 1 902 . 1 1 336 336 GLU CB C 13 28.938 0.1 . 1 . . . . 336 GLU CB . 17940 1 903 . 1 1 336 336 GLU N N 15 120.648 0.1 . 1 . . . . 336 GLU N . 17940 1 904 . 1 1 337 337 TRP H H 1 7.753 0.02 . 1 . . . . 337 TRP H . 17940 1 905 . 1 1 337 337 TRP C C 13 180.705 0.1 . 1 . . . . 337 TRP C . 17940 1 906 . 1 1 337 337 TRP CA C 13 59.427 0.1 . 1 . . . . 337 TRP CA . 17940 1 907 . 1 1 337 337 TRP CB C 13 30.184 0.1 . 1 . . . . 337 TRP CB . 17940 1 908 . 1 1 337 337 TRP N N 15 119.77 0.1 . 1 . . . . 337 TRP N . 17940 1 909 . 1 1 338 338 LYS H H 1 8.778 0.02 . 1 . . . . 338 LYS H . 17940 1 910 . 1 1 338 338 LYS C C 13 177.438 0.1 . 1 . . . . 338 LYS C . 17940 1 911 . 1 1 338 338 LYS CA C 13 59.909 0.1 . 1 . . . . 338 LYS CA . 17940 1 912 . 1 1 338 338 LYS CB C 13 31.444 0.1 . 1 . . . . 338 LYS CB . 17940 1 913 . 1 1 338 338 LYS N N 15 121.418 0.1 . 1 . . . . 338 LYS N . 17940 1 914 . 1 1 339 339 SER H H 1 7.662 0.02 . 1 . . . . 339 SER H . 17940 1 915 . 1 1 339 339 SER C C 13 176.644 0.1 . 1 . . . . 339 SER C . 17940 1 916 . 1 1 339 339 SER CA C 13 60.701 0.1 . 1 . . . . 339 SER CA . 17940 1 917 . 1 1 339 339 SER CB C 13 61.965 0.1 . 1 . . . . 339 SER CB . 17940 1 918 . 1 1 339 339 SER N N 15 114.588 0.1 . 1 . . . . 339 SER N . 17940 1 919 . 1 1 340 340 LEU H H 1 7.97 0.02 . 1 . . . . 340 LEU H . 17940 1 920 . 1 1 340 340 LEU C C 13 180.687 0.1 . 1 . . . . 340 LEU C . 17940 1 921 . 1 1 340 340 LEU CA C 13 57.262 0.1 . 1 . . . . 340 LEU CA . 17940 1 922 . 1 1 340 340 LEU CB C 13 41.304 0.1 . 1 . . . . 340 LEU CB . 17940 1 923 . 1 1 340 340 LEU N N 15 120.453 0.1 . 1 . . . . 340 LEU N . 17940 1 924 . 1 1 341 341 THR H H 1 8.182 0.02 . 1 . . . . 341 THR H . 17940 1 925 . 1 1 341 341 THR C C 13 175.796 0.1 . 1 . . . . 341 THR C . 17940 1 926 . 1 1 341 341 THR CA C 13 67.93 0.1 . 1 . . . . 341 THR CA . 17940 1 927 . 1 1 341 341 THR CB C 13 67.473 0.1 . 1 . . . . 341 THR CB . 17940 1 928 . 1 1 341 341 THR N N 15 116.213 0.1 . 1 . . . . 341 THR N . 17940 1 929 . 1 1 342 342 TYR H H 1 8.846 0.02 . 1 . . . . 342 TYR H . 17940 1 930 . 1 1 342 342 TYR C C 13 177.221 0.1 . 1 . . . . 342 TYR C . 17940 1 931 . 1 1 342 342 TYR CA C 13 61.263 0.1 . 1 . . . . 342 TYR CA . 17940 1 932 . 1 1 342 342 TYR CB C 13 37.232 0.1 . 1 . . . . 342 TYR CB . 17940 1 933 . 1 1 342 342 TYR N N 15 124.824 0.1 . 1 . . . . 342 TYR N . 17940 1 934 . 1 1 343 343 ASP H H 1 8.084 0.02 . 1 . . . . 343 ASP H . 17940 1 935 . 1 1 343 343 ASP C C 13 179.821 0.1 . 1 . . . . 343 ASP C . 17940 1 936 . 1 1 343 343 ASP CA C 13 56.711 0.1 . 1 . . . . 343 ASP CA . 17940 1 937 . 1 1 343 343 ASP CB C 13 39.535 0.1 . 1 . . . . 343 ASP CB . 17940 1 938 . 1 1 343 343 ASP N N 15 117.358 0.1 . 1 . . . . 343 ASP N . 17940 1 939 . 1 1 344 344 GLU H H 1 7.545 0.02 . 1 . . . . 344 GLU H . 17940 1 940 . 1 1 344 344 GLU C C 13 178.774 0.1 . 1 . . . . 344 GLU C . 17940 1 941 . 1 1 344 344 GLU CA C 13 57.51 0.1 . 1 . . . . 344 GLU CA . 17940 1 942 . 1 1 344 344 GLU CB C 13 28.964 0.1 . 1 . . . . 344 GLU CB . 17940 1 943 . 1 1 344 344 GLU N N 15 118.326 0.1 . 1 . . . . 344 GLU N . 17940 1 944 . 1 1 345 345 VAL H H 1 8.106 0.02 . 1 . . . . 345 VAL H . 17940 1 945 . 1 1 345 345 VAL C C 13 178.684 0.1 . 1 . . . . 345 VAL C . 17940 1 946 . 1 1 345 345 VAL CA C 13 65.444 0.1 . 1 . . . . 345 VAL CA . 17940 1 947 . 1 1 345 345 VAL CB C 13 30.593 0.1 . 1 . . . . 345 VAL CB . 17940 1 948 . 1 1 345 345 VAL N N 15 121.218 0.1 . 1 . . . . 345 VAL N . 17940 1 949 . 1 1 346 346 ILE H H 1 8.125 0.02 . 1 . . . . 346 ILE H . 17940 1 950 . 1 1 346 346 ILE C C 13 177.619 0.1 . 1 . . . . 346 ILE C . 17940 1 951 . 1 1 346 346 ILE CA C 13 62.634 0.1 . 1 . . . . 346 ILE CA . 17940 1 952 . 1 1 346 346 ILE CB C 13 36.019 0.1 . 1 . . . . 346 ILE CB . 17940 1 953 . 1 1 346 346 ILE N N 15 114.601 0.1 . 1 . . . . 346 ILE N . 17940 1 954 . 1 1 347 347 SER H H 1 7.434 0.02 . 1 . . . . 347 SER H . 17940 1 955 . 1 1 347 347 SER C C 13 174.57 0.1 . 1 . . . . 347 SER C . 17940 1 956 . 1 1 347 347 SER CA C 13 57.583 0.1 . 1 . . . . 347 SER CA . 17940 1 957 . 1 1 347 347 SER CB C 13 63.18 0.1 . 1 . . . . 347 SER CB . 17940 1 958 . 1 1 347 347 SER N N 15 113.416 0.1 . 1 . . . . 347 SER N . 17940 1 959 . 1 1 348 348 PHE H H 1 7.321 0.02 . 1 . . . . 348 PHE H . 17940 1 960 . 1 1 348 348 PHE C C 13 173.956 0.1 . 1 . . . . 348 PHE C . 17940 1 961 . 1 1 348 348 PHE CA C 13 59.744 0.1 . 1 . . . . 348 PHE CA . 17940 1 962 . 1 1 348 348 PHE CB C 13 38.852 0.1 . 1 . . . . 348 PHE CB . 17940 1 963 . 1 1 348 348 PHE N N 15 124.96 0.1 . 1 . . . . 348 PHE N . 17940 1 964 . 1 1 349 349 VAL H H 1 6.933 0.02 . 1 . . . . 349 VAL H . 17940 1 965 . 1 1 349 349 VAL CA C 13 63.116 0.1 . 1 . . . . 349 VAL CA . 17940 1 966 . 1 1 349 349 VAL CB C 13 32.888 0.1 . 1 . . . . 349 VAL CB . 17940 1 967 . 1 1 349 349 VAL N N 15 130.008 0.1 . 1 . . . . 349 VAL N . 17940 1 stop_ save_