data_19930 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 19930 _Entry.Title ; Human p38 alpha ILVM methyl resonance assignments in non-phosphorylated apo state ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2014-04-23 _Entry.Accession_date 2014-04-23 _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 Yuji Tokunaga . . . 19930 2 Koh Takeuchi . . . 19930 3 Hideo Takahashi . . . 19930 4 Ichio Shimada . . . 19930 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 19930 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 154 19930 '1H chemical shifts' 462 19930 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 . . 2014-09-26 2014-04-23 update BMRB 'update entry citation' 19930 1 . . 2014-08-05 2014-04-23 original author 'original release' 19930 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 19934 'Dual-phosphorylated human p38 alpha apo' 19930 BMRB 19935 'Dual-phosphorylated human p38 alpha ADP-bound' 19930 BMRB 19936 'Dual-phosphorylated human p38 alpha MK2 334/D peptide bound' 19930 BMRB 19937 'Dual-phosphorylated human p38 alpha ADP and MK2 334/D peptide bound' 19930 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 19930 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI 10.1038/nsmb.2861 _Citation.PubMed_ID 25038803 _Citation.Full_citation . _Citation.Title 'Allosteric enhancement of MAP kinase p38a's activity and substrate selectivity by docking interactions.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Struct. Mol. Biol.' _Citation.Journal_name_full 'Nature structural & molecular biology' _Citation.Journal_volume 21 _Citation.Journal_issue 8 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1545-9985 _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 704 _Citation.Page_last 711 _Citation.Year 2014 _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 Yuji Tokunaga Y. . . 19930 1 2 Koh Takeuchi K. . . 19930 1 3 Hideo Takahashi H. . . 19930 1 4 Ichio Shimada I. . . 19930 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly_2 _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly_2 _Assembly.Entry_ID 19930 _Assembly.ID 1 _Assembly.Name 'p38-0P apo' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'non-phosphorylated human p38 alpha (apo)' 1 $Non-phosphorylated_human_p38_alpha_(apo) A . yes native no no . . . 19930 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Non-phosphorylated_human_p38_alpha_(apo) _Entity.Sf_category entity _Entity.Sf_framecode Non-phosphorylated_human_p38_alpha_(apo) _Entity.Entry_ID 19930 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Non-phosphorylated_human_p38_alpha_(apo) _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 ; MAHHHHHHSQERPTFYRQEL NKTIWEVPERYQNLSPVGSG AYGSVCAAFDTKTGLRVAVK KLSRPFQSIIHAKRTYRELR LLKHMKHENVIGLLDVFTPA RSLEEFNDVYLVTHLMGADL NNIVKCQKLTDDHVQFLIYQ ILRGLKYIHSADIIHRDLKP SNLAVNEDCELKILDFGLAR HTDDEMTGYVATRWYRAPEI MLNWMHYNQTVDIWSVGCIM AELLTGRTLFPGTDHIDQLK LILRLVGTPGAELLKKISSE SARNYIQSLTQMPKMNFANV FIGANPLAVDLLEKMLVLDS DKRITAAQALAHAYFAQYHD PDDEPVADPYDQSFESRDLL IDEWKSLTYDEVISFVPPPL DQEEMES ; _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 367 _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 . . . . . 95.64 352 99.43 99.43 0.00e+00 . . . . 19930 1 2 no BMRB 17940 . p38alpha . . . . . 95.10 349 99.14 99.43 0.00e+00 . . . . 19930 1 3 no BMRB 19934 . Dual-phosphorylated_human_p38_alpha_(apo) . . . . . 100.00 367 99.46 99.46 0.00e+00 . . . . 19930 1 4 no BMRB 19935 . Dual-phosphorylated_human_p38_alpha . . . . . 100.00 367 99.46 99.46 0.00e+00 . . . . 19930 1 5 no BMRB 19936 . dual-phosphorylated_human_p38_alpha_(apo) . . . . . 100.00 367 99.46 99.46 0.00e+00 . . . . 19930 1 6 no BMRB 19937 . dual-phosphorylated_human_p38_alpha_(apo) . . . . . 100.00 367 99.46 99.46 0.00e+00 . . . . 19930 1 7 no PDB 1DI9 . "The Structure Of P38 Mitogen-Activated Protein Kinase In Complex With 4-[3-Methylsulfanylanilino]-6,7- Dimethoxyquinazoline" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 8 no PDB 1IAN . "Human P38 Map Kinase Inhibitor Complex" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 9 no PDB 1KV1 . "P38 Map Kinase In Complex With Inhibitor 1" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 10 no PDB 1KV2 . "Human P38 Map Kinase In Complex With Birb 796" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 11 no PDB 1LEW . "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Nuclear Substrate Mef2a" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19930 1 12 no PDB 1LEZ . "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Activator Mkk3b" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19930 1 13 no PDB 1M7Q . "Crystal Structure Of P38 Map Kinase In Complex With A Dihydroquinazolinone Inhibitor" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 14 no PDB 1OUK . "The Structure Of P38 Alpha In Complex With A Pyridinylimidazole Inhibitor" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 15 no PDB 1OUY . "The Structure Of P38 Alpha In Complex With A Dihydropyrido- Pyrimidine Inhibitor" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 16 no PDB 1OVE . "The Structure Of P38 Alpha In Complex With A Dihydroquinolinone" . . . . . 99.18 366 98.63 98.63 0.00e+00 . . . . 19930 1 17 no PDB 1OZ1 . "P38 Mitogen-Activated Kinase In Complex With 4-Azaindole Inhibitor" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 18 no PDB 1R39 . "The Structure Of P38alpha" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 19 no PDB 1R3C . "The Structure Of P38alpha C162s Mutant" . . . . . 99.18 366 98.63 98.63 0.00e+00 . . . . 19930 1 20 no PDB 1W7H . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 21 no PDB 1W82 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 22 no PDB 1W83 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 23 no PDB 1W84 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 24 no PDB 1WBN . "Fragment Based P38 Inhibitors" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 25 no PDB 1WBO . "Fragment Based P38 Inhibitors" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 26 no PDB 1WBS . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 27 no PDB 1WBT . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-based Lead Generation." . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 28 no PDB 1WBV . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 29 no PDB 1WBW . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 30 no PDB 1WFC . "Structure Of Apo, Unphosphorylated, P38 Mitogen Activated Protein Kinase P38 (P38 Map Kinase) The Mammalian Homologue Of The Ye" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 31 no PDB 1YQJ . "Crystal Structure Of P38 Alpha In Complex With A Selective Pyridazine Inhibitor" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 32 no PDB 1YW2 . "Mutated Mus Musculus P38 Kinase (Mp38)" . . . . . 97.82 360 98.89 99.16 0.00e+00 . . . . 19930 1 33 no PDB 1YWR . "Crystal Structure Analysis Of Inactive P38 Kinase Domain In Complex With A Monocyclic Pyrazolone Inhibitor" . . . . . 97.82 360 99.16 99.44 0.00e+00 . . . . 19930 1 34 no PDB 1ZYJ . "Human P38 Map Kinase In Complex With Inhibitor 1a" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 35 no PDB 1ZZ2 . "Two Classes Of P38alpha Map Kinase Inhibitors Having A Common Diphenylether Core But Exhibiting Divergent Binding Modes" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 36 no PDB 1ZZL . "Crystal Structure Of P38 With Triazolopyridine" . . . . . 95.64 351 100.00 100.00 0.00e+00 . . . . 19930 1 37 no PDB 2BAJ . "P38alpha Bound To Pyrazolourea" . . . . . 99.46 365 100.00 100.00 0.00e+00 . . . . 19930 1 38 no PDB 2BAK . "P38alpha Map Kinase Bound To Mpaq" . . . . . 99.46 365 100.00 100.00 0.00e+00 . . . . 19930 1 39 no PDB 2BAL . "P38alpha Map Kinase Bound To Pyrazoloamine" . . . . . 99.46 365 99.73 99.73 0.00e+00 . . . . 19930 1 40 no PDB 2BAQ . "P38alpha Bound To Ro3201195" . . . . . 99.46 365 99.45 99.73 0.00e+00 . . . . 19930 1 41 no PDB 2FSL . "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-A" . . . . . 100.00 367 99.46 99.46 0.00e+00 . . . . 19930 1 42 no PDB 2FSM . "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-B" . . . . . 100.00 367 99.46 99.46 0.00e+00 . . . . 19930 1 43 no PDB 2FSO . "Mitogen Activated Protein Kinase P38alpha (D176a) Activating Mutant" . . . . . 100.00 367 99.73 99.73 0.00e+00 . . . . 19930 1 44 no PDB 2FST . "Mitogen Activated Protein Kinase P38alpha (d176a+f327l) Activating Mutant" . . . . . 100.00 367 99.46 99.46 0.00e+00 . . . . 19930 1 45 no PDB 2GFS . "P38 Kinase Crystal Structure In Complex With Ro3201195" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 46 no PDB 2GHL . "Mutant Mus Musculus P38 Kinase Domain In Complex With Inhibitor Pg-874743" . . . . . 94.82 348 98.85 99.14 0.00e+00 . . . . 19930 1 47 no PDB 2GHM . "Mutated Map Kinase P38 (Mus Musculus) In Complex With Inhbitor Pg-895449" . . . . . 94.82 348 98.85 99.14 0.00e+00 . . . . 19930 1 48 no PDB 2GTM . "Mutated Mouse P38 Map Kinase Domain In Complex With Inhibitor Pg-892579" . . . . . 94.82 348 99.43 99.43 0.00e+00 . . . . 19930 1 49 no PDB 2GTN . "Mutated Map Kinase P38 (mus Musculus) In Complex With Inhbitor Pg-951717" . . . . . 94.82 348 99.43 99.43 0.00e+00 . . . . 19930 1 50 no PDB 2I0H . "The Structure Of P38alpha In Complex With An Arylpyridazinone" . . . . . 99.18 366 98.63 98.63 0.00e+00 . . . . 19930 1 51 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" . . . . . 97.55 359 98.88 98.88 0.00e+00 . . . . 19930 1 52 no PDB 2NPQ . "A Novel Lipid Binding Site In The P38 Alpha Map Kinase" . . . . . 100.00 367 100.00 100.00 0.00e+00 . . . . 19930 1 53 no PDB 2OKR . "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 54 no PDB 2ONL . "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 55 no PDB 2OZA . "Structure Of P38alpha Complex" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19930 1 56 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" . . . . . 94.82 348 98.85 98.85 0.00e+00 . . . . 19930 1 57 no PDB 2QD9 . "P38 Alpha Map Kinase Inhibitor Based On Heterobicyclic Scaffolds" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 58 no PDB 2RG5 . "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11b" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 59 no PDB 2RG6 . "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11j" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 60 no PDB 2Y8O . "Crystal Structure Of Human P38alpha Complexed With A Mapk Docking Peptide" . . . . . 97.82 362 99.72 99.72 0.00e+00 . . . . 19930 1 61 no PDB 2YIS . "Triazolopyridine Inhibitors Of P38 Kinase." . . . . . 97.82 359 100.00 100.00 0.00e+00 . . . . 19930 1 62 no PDB 2YIW . "Triazolopyridine Inhibitors Of P38 Kinase" . . . . . 97.82 359 100.00 100.00 0.00e+00 . . . . 19930 1 63 no PDB 2YIX . "Triazolopyridine Inhibitors Of P38" . . . . . 95.64 351 100.00 100.00 0.00e+00 . . . . 19930 1 64 no PDB 2ZAZ . "Crystal Structure Of P38 In Complex With 4-Anilino Quinoline Inhibitor" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 65 no PDB 2ZB0 . "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 66 no PDB 2ZB1 . "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 67 no PDB 3BV2 . "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 30" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 68 no PDB 3BV3 . "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 2" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 69 no PDB 3BX5 . "P38 Alpha Map Kinase Complexed With Bms-640994" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 70 no PDB 3C5U . "P38 Alpha Map Kinase Complexed With A Benzothiazole Based Inhibitor" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 71 no PDB 3CTQ . "Structure Of Map Kinase P38 In Complex With A 1-O-Tolyl-1,2, 3-Triazole-4-Carboxamide" . . . . . 94.82 348 98.85 98.85 0.00e+00 . . . . 19930 1 72 no PDB 3D7Z . "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 73 no PDB 3D83 . "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19930 1 74 no PDB 3DS6 . "P38 Complex With A Phthalazine Inhibitor" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 75 no PDB 3E92 . "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" . . . . . 100.27 371 98.64 98.64 0.00e+00 . . . . 19930 1 76 no PDB 3E93 . "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" . . . . . 100.27 371 98.64 98.64 0.00e+00 . . . . 19930 1 77 no PDB 3FC1 . "Crystal Structure Of P38 Kinase Bound To Pyrimido-Pyridazinone Inhibitor" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 78 no PDB 3FI4 . "P38 Kinase Crystal Structure In Complex With Ro4499" . . . . . 100.54 372 98.64 99.19 0.00e+00 . . . . 19930 1 79 no PDB 3FKL . "P38 Kinase Crystal Structure In Complex With Ro9552" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 80 no PDB 3FKN . "P38 Kinase Crystal Structure In Complex With Ro7125" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 81 no PDB 3FKO . "P38 Kinase Crystal Structure In Complex With Ro3668" . . . . . 100.54 372 98.64 99.19 0.00e+00 . . . . 19930 1 82 no PDB 3FL4 . "P38 Kinase Crystal Structure In Complex With Ro5634" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 83 no PDB 3FLN . "P38 Kinase Crystal Structure In Complex With R1487" . . . . . 100.54 372 98.64 99.19 0.00e+00 . . . . 19930 1 84 no PDB 3FLQ . "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-((S)-2-Methanesulfonyl-1-Methyl- Ethylamino)-8-Methyl-" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 85 no PDB 3FLS . "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-((R)-2-Methanesulfonyl-1-Methyl- Ethylamino)-8-Methyl-" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 86 no PDB 3FLW . "P38 Kinase Crystal Structure In Complex With Pamapimod" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 87 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" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 88 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" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 89 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-" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 90 no PDB 3FMJ . "P38 Kinase Crystal Structure In Complex With 4-(5-Methyl-3-Phenyl- Isoxazol-4-Yl)-Pyrimidin-2-Ylamine" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 91 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-" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 92 no PDB 3FML . "P38 Kinase Crystal Structure In Complex With Ro6224" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 93 no PDB 3FMM . "P38 Kinase Crystal Structure In Complex With Ro6226" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 94 no PDB 3FMN . "P38 Kinase Crystal Structure In Complex With Ro2530" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 95 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" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 96 no PDB 3FSK . "P38 Kinase Crystal Structure In Complex With Ro6257" . . . . . 100.54 372 98.92 99.19 0.00e+00 . . . . 19930 1 97 no PDB 3GC7 . "The Structure Of P38alpha In Complex With A Dihydroquinazolinone" . . . . . 99.18 366 98.63 98.63 0.00e+00 . . . . 19930 1 98 no PDB 3GCP . "Human P38 Map Kinase In Complex With Sb203580" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 99 no PDB 3GCQ . "Human P38 Map Kinase In Complex With Rl45" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 100 no PDB 3GCS . "Human P38 Map Kinase In Complex With Sorafenib" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 101 no PDB 3GCU . "Human P38 Map Kinase In Complex With Rl48" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 102 no PDB 3GCV . "Human P38 Map Kinase In Complex With Rl62" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 103 no PDB 3GFE . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 104 no PDB 3GI3 . "Crystal Structure Of A N-Phenyl-N'-Naphthylurea Analog In Complex With P38 Map Kinase" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19930 1 105 no PDB 3HEC . "P38 In Complex With Imatinib" . . . . . 94.82 348 100.00 100.00 0.00e+00 . . . . 19930 1 106 no PDB 3HEG . "P38 In Complex With Sorafenib" . . . . . 94.82 348 100.00 100.00 0.00e+00 . . . . 19930 1 107 no PDB 3HL7 . "Crystal Structure Of Human P38alpha Complexed With Sd-0006" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 108 no PDB 3HLL . "Crystal Structure Of Human P38alpha Complexed With Ph-797804" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 109 no PDB 3HP2 . "Crystal Structure Of Human P38alpha Complexed With A Pyridinone Compound" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 110 no PDB 3HP5 . "Crystal Structure Of Human P38alpha Complexed With A Pyrimidopyridazinone Compound" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 111 no PDB 3HRB . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 359 100.00 100.00 0.00e+00 . . . . 19930 1 112 no PDB 3HUB . "Human P38 Map Kinase In Complex With Scios-469" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 113 no PDB 3HUC . "Human P38 Map Kinase In Complex With Rl40" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 114 no PDB 3HV3 . "Human P38 Map Kinase In Complex With Rl49" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 115 no PDB 3HV4 . "Human P38 Map Kinase In Complex With Rl51" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 116 no PDB 3HV5 . "Human P38 Map Kinase In Complex With Rl24" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 117 no PDB 3HV6 . "Human P38 Map Kinase In Complex With Rl39" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 118 no PDB 3HV7 . "Human P38 Map Kinase In Complex With Rl38" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 119 no PDB 3HVC . "Crystal Structure Of Human P38alpha Map Kinase" . . . . . 97.82 362 100.00 100.00 0.00e+00 . . . . 19930 1 120 no PDB 3IPH . "Crystal Structure Of P38 In Complex With A Biphenylamide Inhibitor" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19930 1 121 no PDB 3ITZ . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridazine Inhibitor" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 122 no PDB 3IW5 . "Human P38 Map Kinase In Complex With An Indole Derivative" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 123 no PDB 3IW6 . "Human P38 Map Kinase In Complex With A Benzylpiperazin- Pyrrol" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 124 no PDB 3IW7 . "Human P38 Map Kinase In Complex With An Imidazo-Pyridine" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 125 no PDB 3IW8 . "Structure Of Inactive Human P38 Map Kinase In Complex With A Thiazole-Urea" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 126 no PDB 3K3I . "P38alpha Bound To Novel Dgf-Out Compound Pf-00215955" . . . . . 94.82 350 100.00 100.00 0.00e+00 . . . . 19930 1 127 no PDB 3K3J . "P38alpha Bound To Novel Dfg-Out Compound Pf-00416121" . . . . . 97.82 362 100.00 100.00 0.00e+00 . . . . 19930 1 128 no PDB 3KF7 . "Crystal Structure Of Human P38alpha Complexed With A Triazolopyrimidine Compound" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 129 no PDB 3L8S . "Human P38 Map Kinase In Complex With Cp-547632" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 130 no PDB 3L8X . "P38 Alpha Kinase Complexed With A Pyrazolo-Pyrimidine Based Inhibitor" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 131 no PDB 3LFA . "Human P38 Map Kinase In Complex With Dasatinib" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 132 no PDB 3LFB . "Human P38 Map Kinase In Complex With Rl98" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 133 no PDB 3LFC . "Human P38 Map Kinase In Complex With Rl99" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 134 no PDB 3LFD . "Human P38 Map Kinase In Complex With Rl113" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 135 no PDB 3LFE . "Human P38 Map Kinase In Complex With Rl116" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 136 no PDB 3LFF . "Human P38 Map Kinase In Complex With Rl166" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 137 no PDB 3LHJ . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor." . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 138 no PDB 3MGY . "Mutagenesis Of P38 Map Kinase Eshtablishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out " . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 139 no PDB 3MH0 . "Mutagenesis Of P38 Map Kinase Eshtablishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out " . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 140 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" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 141 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" . . . . . 97.82 360 99.72 100.00 0.00e+00 . . . . 19930 1 142 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" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 143 no PDB 3MPA . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 144 no PDB 3MPT . "Crystal Structure Of P38 Kinase In Complex With A Pyrrole-2- Carboxamide Inhibitor" . . . . . 100.27 371 98.91 98.91 0.00e+00 . . . . 19930 1 145 no PDB 3MVL . "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7k" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 146 no PDB 3MVM . "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7v" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 147 no PDB 3MW1 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 359 100.00 100.00 0.00e+00 . . . . 19930 1 148 no PDB 3NEW . "P38-Alpha Complexed With Compound 10" . . . . . 99.18 366 98.63 98.63 0.00e+00 . . . . 19930 1 149 no PDB 3NNU . "Crystal Structure Of P38 Alpha In Complex With Dp1376" . . . . . 96.19 354 100.00 100.00 0.00e+00 . . . . 19930 1 150 no PDB 3NNV . "Crystal Structure Of P38 Alpha In Complex With Dp437" . . . . . 96.19 354 100.00 100.00 0.00e+00 . . . . 19930 1 151 no PDB 3NNW . "Crystal Structure Of P38 Alpha In Complex With Dp802" . . . . . 96.19 354 100.00 100.00 0.00e+00 . . . . 19930 1 152 no PDB 3NNX . "Crystal Structure Of Phosphorylated P38 Alpha In Complex With Dp802" . . . . . 96.19 354 99.72 99.72 0.00e+00 . . . . 19930 1 153 no PDB 3NWW . "P38 Alpha Kinase Complexed With A 2-aminothiazol-5-yl-pyrimidine Based Inhibitor" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 154 no PDB 3O8P . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 155 no PDB 3O8T . "Conformational Plasticity Of P38 Map Kinase Dfg-Motif Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 156 no PDB 3O8U . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.72 100.00 0.00e+00 . . . . 19930 1 157 no PDB 3OBG . "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 158 no PDB 3OBJ . "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 159 no PDB 3OC1 . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 160 no PDB 3OCG . "P38 Alpha Kinase Complexed With A 5-Amino-Pyrazole Based Inhibitor" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 161 no PDB 3OD6 . "Crystal Structure Of P38alpha Y323t Active Mutant" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 162 no PDB 3ODY . "Crystal Structure Of P38alpha Y323q Active Mutant" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 163 no PDB 3ODZ . "Crystal Structure Of P38alpha Y323r Active Mutant" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 164 no PDB 3OEF . "Crystal Structure Of Y323f Inactive Mutant Of P38alpha Map Kinase" . . . . . 97.82 360 99.72 100.00 0.00e+00 . . . . 19930 1 165 no PDB 3P4K . "The Third Conformation Of P38a Map Kinase Observed In Phosphorylated P38a And In Solution" . . . . . 100.82 370 98.38 98.65 0.00e+00 . . . . 19930 1 166 no PDB 3P5K . "P38 Inhibitor-Bound" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19930 1 167 no PDB 3P78 . "P38 Inhibitor-Bound" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19930 1 168 no PDB 3P79 . "P38 Inhibitor-Bound" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19930 1 169 no PDB 3P7A . "P38 Inhibitor-Bound" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19930 1 170 no PDB 3P7B . "P38 Inhibitor-Bound" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19930 1 171 no PDB 3P7C . "P38 Inhibitor-Bound" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19930 1 172 no PDB 3PG3 . "Human P38 Map Kinase In Complex With Rl182" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19930 1 173 no PDB 3QUD . "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino-Benzophenone" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 174 no PDB 3QUE . "Human P38 Map Kinase In Complex With Skepinone-l" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 175 no PDB 3RIN . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 176 no PDB 3ROC . "Crystal Structure Of Human P38 Alpha Complexed With A Pyrimidinone Compound" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 177 no PDB 3S3I . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 95.10 349 100.00 100.00 0.00e+00 . . . . 19930 1 178 no PDB 3S4Q . "P38 Alpha Kinase Complexed With A Pyrazolo-Triazine Based Inhibitor" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 179 no PDB 3U8W . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Triazolopyridazinone Inhibitor" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 180 no PDB 3UVP . "Human P38 Map Kinase In Complex With A Benzamide Substituted Benzosuberone" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 181 no PDB 3UVQ . "Human P38 Map Kinase In Complex With A Dibenzosuberone Derivative" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 182 no PDB 3UVR . "Human P38 Map Kinase In Complex With Km064" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 183 no PDB 3ZS5 . "Structural Basis For Kinase Selectivity Of Three Clinical P38alpha Inhibitors" . . . . . 98.09 362 100.00 100.00 0.00e+00 . . . . 19930 1 184 no PDB 3ZSG . "X-Ray Structure Of P38alpha Bound To Tak-715" . . . . . 98.09 362 100.00 100.00 0.00e+00 . . . . 19930 1 185 no PDB 3ZSH . "X-Ray Structure Of P38alpha Bound To Scio-469" . . . . . 98.09 362 100.00 100.00 0.00e+00 . . . . 19930 1 186 no PDB 3ZSI . "X-Ray Structure Of P38alpha Bound To Vx-745" . . . . . 98.09 362 100.00 100.00 0.00e+00 . . . . 19930 1 187 no PDB 3ZYA . "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino- Dibenzosuberone" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19930 1 188 no PDB 4A9Y . "P38alpha Map Kinase Bound To Cmpd 8" . . . . . 99.46 365 100.00 100.00 0.00e+00 . . . . 19930 1 189 no PDB 4AA0 . "P38alpha Map Kinase Bound To Cmpd 2" . . . . . 99.46 365 100.00 100.00 0.00e+00 . . . . 19930 1 190 no PDB 4AA4 . "P38alpha Map Kinase Bound To Cmpd 22" . . . . . 99.46 365 100.00 100.00 0.00e+00 . . . . 19930 1 191 no PDB 4AA5 . "P38alpha Map Kinase Bound To Cmpd 33" . . . . . 99.46 365 99.73 99.73 0.00e+00 . . . . 19930 1 192 no PDB 4AAC . "P38alpha Map Kinase Bound To Cmpd 29" . . . . . 99.46 365 100.00 100.00 0.00e+00 . . . . 19930 1 193 no PDB 4DLI . "Human P38 Map Kinase In Complex With Rl87" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 194 no PDB 4DLJ . "Human P38 Map Kinase In Complex With Rl163" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 195 no PDB 4E5A . "The W197a Mutant Of P38a Map Kinase" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 196 no PDB 4E5B . "Structure Of P38a Map Kinase Without Bog" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 197 no PDB 4E6A . "P38a-pia23 Complex" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 198 no PDB 4E6C . "P38a-perifosine Complex" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 199 no PDB 4E8A . "The Crystal Structure Of P38a Map Kinase In Complex With Pia24" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 200 no PDB 4EH2 . "Human P38 Map Kinase In Complex With Np-F1 And Rl87" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 201 no PDB 4EH3 . "Human P38 Map Kinase In Complex With Np-F2 And Rl87" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 202 no PDB 4EH4 . "Human P38 Map Kinase In Complex With Np-F3 And Rl87" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 203 no PDB 4EH5 . "Human P38 Map Kinase In Complex With Np-F4 And Rl87" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 204 no PDB 4EH6 . "Human P38 Map Kinase In Complex With Np-F5 And Rl87" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 205 no PDB 4EH7 . "Human P38 Map Kinase In Complex With Np-F6 And Rl87" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 206 no PDB 4EH8 . "Human P38 Map Kinase In Complex With Np-F7 And Rl87" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 207 no PDB 4EH9 . "Human P38 Map Kinase In Complex With Np-F11 And Rl87" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 208 no PDB 4EHV . "Human P38 Map Kinase In Complex With Np-F10 And Rl87" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 209 no PDB 4GEO . "P38a Map Kinase Def-pocket Penta Mutant (m194a, L195a, H228a, I229a, Y258a)" . . . . . 100.00 367 98.09 98.09 0.00e+00 . . . . 19930 1 210 no PDB 4KA3 . "Structure Of Map Kinase In Complex With A Docking Peptide" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19930 1 211 no PDB 4KIN . "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 5-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 212 no PDB 4KIP . "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 2-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 213 no PDB 4KIQ . "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With Ethyl 6-((5-(cyclopropylcarbamoyl)-2-methylpheny" . . . . . 99.18 366 100.00 100.00 0.00e+00 . . . . 19930 1 214 no PDB 4L8M . "Human P38 Map Kinase In Complex With A Dibenzoxepinone" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 215 no PDB 4LOO . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (monoclinic Crystal Form)" . . . . . 97.82 361 99.44 99.44 0.00e+00 . . . . 19930 1 216 no PDB 4LOP . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form)" . . . . . 97.82 361 99.44 99.44 0.00e+00 . . . . 19930 1 217 no PDB 4LOQ . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form With Bound Sulphate)" . . . . . 97.82 361 99.44 99.44 0.00e+00 . . . . 19930 1 218 no PDB 4TYH . "Ternary Complex Of P38 And Mk2 With A P38 Inhibitor" . . . . . 94.82 348 99.43 99.43 0.00e+00 . . . . 19930 1 219 no DBJ BAB85654 . "Alternative spliced variant of p38alpha EXIP [Homo sapiens]" . . . . . 68.94 307 100.00 100.00 0.00e+00 . . . . 19930 1 220 no DBJ BAE21782 . "unnamed protein product [Mus musculus]" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19930 1 221 no DBJ BAE30324 . "unnamed protein product [Mus musculus]" . . . . . 77.11 283 99.65 99.65 0.00e+00 . . . . 19930 1 222 no DBJ BAE31659 . "unnamed protein product [Mus musculus]" . . . . . 77.11 283 99.65 99.65 0.00e+00 . . . . 19930 1 223 no DBJ BAF84398 . "unnamed protein product [Homo sapiens]" . . . . . 97.82 360 99.72 99.72 0.00e+00 . . . . 19930 1 224 no EMBL CAG38743 . "MAPK14 [Homo sapiens]" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 225 no GB AAA20888 . "MAP kinase [Mus musculus]" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19930 1 226 no GB AAA57456 . "CSaids binding protein [Homo sapiens]" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 227 no GB AAA74301 . "MAP kinase [Homo sapiens]" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 228 no GB AAB51285 . "p38 mitogen activated protein kinase [Rattus norvegicus]" . . . . . 97.82 360 98.05 98.89 0.00e+00 . . . . 19930 1 229 no GB AAC36131 . "p38 mitogen activated protein kinase [Canis lupus familiaris]" . . . . . 97.82 360 99.44 100.00 0.00e+00 . . . . 19930 1 230 no PRF 2111247A . "p38 mitogen-activated protein kinase" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 231 no PRF 2124426A . "Mxi2 protein" . . . . . 76.29 297 99.64 99.64 0.00e+00 . . . . 19930 1 232 no REF NP_001003206 . "mitogen-activated protein kinase 14 [Canis lupus familiaris]" . . . . . 97.82 360 99.44 100.00 0.00e+00 . . . . 19930 1 233 no REF NP_001136366 . "mitogen-activated protein kinase 14 [Ovis aries]" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 1 234 no REF NP_001161985 . "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" . . . . . 77.11 283 99.65 99.65 0.00e+00 . . . . 19930 1 235 no REF NP_001161986 . "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" . . . . . 77.11 283 99.65 99.65 0.00e+00 . . . . 19930 1 236 no REF NP_036081 . "mitogen-activated protein kinase 14 isoform 1 [Mus musculus]" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19930 1 237 no SP O02812 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Mitogen-activated protein " . . . . . 97.82 360 99.44 100.00 0.00e+00 . . . . 19930 1 238 no SP P47811 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=CRK1; AltName: Full=Mitoge" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19930 1 239 no SP P70618 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=CRK1; AltName: Full=Mitoge" . . . . . 97.82 360 98.61 99.16 0.00e+00 . . . . 19930 1 240 no SP Q16539 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Cytokine suppressive anti-" . . . . . 97.82 360 100.00 100.00 0.00e+00 . . . . 19930 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 -6 MET . 19930 1 2 -5 ALA . 19930 1 3 -4 HIS . 19930 1 4 -3 HIS . 19930 1 5 -2 HIS . 19930 1 6 -1 HIS . 19930 1 7 0 HIS . 19930 1 8 1 HIS . 19930 1 9 2 SER . 19930 1 10 3 GLN . 19930 1 11 4 GLU . 19930 1 12 5 ARG . 19930 1 13 6 PRO . 19930 1 14 7 THR . 19930 1 15 8 PHE . 19930 1 16 9 TYR . 19930 1 17 10 ARG . 19930 1 18 11 GLN . 19930 1 19 12 GLU . 19930 1 20 13 LEU . 19930 1 21 14 ASN . 19930 1 22 15 LYS . 19930 1 23 16 THR . 19930 1 24 17 ILE . 19930 1 25 18 TRP . 19930 1 26 19 GLU . 19930 1 27 20 VAL . 19930 1 28 21 PRO . 19930 1 29 22 GLU . 19930 1 30 23 ARG . 19930 1 31 24 TYR . 19930 1 32 25 GLN . 19930 1 33 26 ASN . 19930 1 34 27 LEU . 19930 1 35 28 SER . 19930 1 36 29 PRO . 19930 1 37 30 VAL . 19930 1 38 31 GLY . 19930 1 39 32 SER . 19930 1 40 33 GLY . 19930 1 41 34 ALA . 19930 1 42 35 TYR . 19930 1 43 36 GLY . 19930 1 44 37 SER . 19930 1 45 38 VAL . 19930 1 46 39 CYS . 19930 1 47 40 ALA . 19930 1 48 41 ALA . 19930 1 49 42 PHE . 19930 1 50 43 ASP . 19930 1 51 44 THR . 19930 1 52 45 LYS . 19930 1 53 46 THR . 19930 1 54 47 GLY . 19930 1 55 48 LEU . 19930 1 56 49 ARG . 19930 1 57 50 VAL . 19930 1 58 51 ALA . 19930 1 59 52 VAL . 19930 1 60 53 LYS . 19930 1 61 54 LYS . 19930 1 62 55 LEU . 19930 1 63 56 SER . 19930 1 64 57 ARG . 19930 1 65 58 PRO . 19930 1 66 59 PHE . 19930 1 67 60 GLN . 19930 1 68 61 SER . 19930 1 69 62 ILE . 19930 1 70 63 ILE . 19930 1 71 64 HIS . 19930 1 72 65 ALA . 19930 1 73 66 LYS . 19930 1 74 67 ARG . 19930 1 75 68 THR . 19930 1 76 69 TYR . 19930 1 77 70 ARG . 19930 1 78 71 GLU . 19930 1 79 72 LEU . 19930 1 80 73 ARG . 19930 1 81 74 LEU . 19930 1 82 75 LEU . 19930 1 83 76 LYS . 19930 1 84 77 HIS . 19930 1 85 78 MET . 19930 1 86 79 LYS . 19930 1 87 80 HIS . 19930 1 88 81 GLU . 19930 1 89 82 ASN . 19930 1 90 83 VAL . 19930 1 91 84 ILE . 19930 1 92 85 GLY . 19930 1 93 86 LEU . 19930 1 94 87 LEU . 19930 1 95 88 ASP . 19930 1 96 89 VAL . 19930 1 97 90 PHE . 19930 1 98 91 THR . 19930 1 99 92 PRO . 19930 1 100 93 ALA . 19930 1 101 94 ARG . 19930 1 102 95 SER . 19930 1 103 96 LEU . 19930 1 104 97 GLU . 19930 1 105 98 GLU . 19930 1 106 99 PHE . 19930 1 107 100 ASN . 19930 1 108 101 ASP . 19930 1 109 102 VAL . 19930 1 110 103 TYR . 19930 1 111 104 LEU . 19930 1 112 105 VAL . 19930 1 113 106 THR . 19930 1 114 107 HIS . 19930 1 115 108 LEU . 19930 1 116 109 MET . 19930 1 117 110 GLY . 19930 1 118 111 ALA . 19930 1 119 112 ASP . 19930 1 120 113 LEU . 19930 1 121 114 ASN . 19930 1 122 115 ASN . 19930 1 123 116 ILE . 19930 1 124 117 VAL . 19930 1 125 118 LYS . 19930 1 126 119 CYS . 19930 1 127 120 GLN . 19930 1 128 121 LYS . 19930 1 129 122 LEU . 19930 1 130 123 THR . 19930 1 131 124 ASP . 19930 1 132 125 ASP . 19930 1 133 126 HIS . 19930 1 134 127 VAL . 19930 1 135 128 GLN . 19930 1 136 129 PHE . 19930 1 137 130 LEU . 19930 1 138 131 ILE . 19930 1 139 132 TYR . 19930 1 140 133 GLN . 19930 1 141 134 ILE . 19930 1 142 135 LEU . 19930 1 143 136 ARG . 19930 1 144 137 GLY . 19930 1 145 138 LEU . 19930 1 146 139 LYS . 19930 1 147 140 TYR . 19930 1 148 141 ILE . 19930 1 149 142 HIS . 19930 1 150 143 SER . 19930 1 151 144 ALA . 19930 1 152 145 ASP . 19930 1 153 146 ILE . 19930 1 154 147 ILE . 19930 1 155 148 HIS . 19930 1 156 149 ARG . 19930 1 157 150 ASP . 19930 1 158 151 LEU . 19930 1 159 152 LYS . 19930 1 160 153 PRO . 19930 1 161 154 SER . 19930 1 162 155 ASN . 19930 1 163 156 LEU . 19930 1 164 157 ALA . 19930 1 165 158 VAL . 19930 1 166 159 ASN . 19930 1 167 160 GLU . 19930 1 168 161 ASP . 19930 1 169 162 CYS . 19930 1 170 163 GLU . 19930 1 171 164 LEU . 19930 1 172 165 LYS . 19930 1 173 166 ILE . 19930 1 174 167 LEU . 19930 1 175 168 ASP . 19930 1 176 169 PHE . 19930 1 177 170 GLY . 19930 1 178 171 LEU . 19930 1 179 172 ALA . 19930 1 180 173 ARG . 19930 1 181 174 HIS . 19930 1 182 175 THR . 19930 1 183 176 ASP . 19930 1 184 177 ASP . 19930 1 185 178 GLU . 19930 1 186 179 MET . 19930 1 187 180 THR . 19930 1 188 181 GLY . 19930 1 189 182 TYR . 19930 1 190 183 VAL . 19930 1 191 184 ALA . 19930 1 192 185 THR . 19930 1 193 186 ARG . 19930 1 194 187 TRP . 19930 1 195 188 TYR . 19930 1 196 189 ARG . 19930 1 197 190 ALA . 19930 1 198 191 PRO . 19930 1 199 192 GLU . 19930 1 200 193 ILE . 19930 1 201 194 MET . 19930 1 202 195 LEU . 19930 1 203 196 ASN . 19930 1 204 197 TRP . 19930 1 205 198 MET . 19930 1 206 199 HIS . 19930 1 207 200 TYR . 19930 1 208 201 ASN . 19930 1 209 202 GLN . 19930 1 210 203 THR . 19930 1 211 204 VAL . 19930 1 212 205 ASP . 19930 1 213 206 ILE . 19930 1 214 207 TRP . 19930 1 215 208 SER . 19930 1 216 209 VAL . 19930 1 217 210 GLY . 19930 1 218 211 CYS . 19930 1 219 212 ILE . 19930 1 220 213 MET . 19930 1 221 214 ALA . 19930 1 222 215 GLU . 19930 1 223 216 LEU . 19930 1 224 217 LEU . 19930 1 225 218 THR . 19930 1 226 219 GLY . 19930 1 227 220 ARG . 19930 1 228 221 THR . 19930 1 229 222 LEU . 19930 1 230 223 PHE . 19930 1 231 224 PRO . 19930 1 232 225 GLY . 19930 1 233 226 THR . 19930 1 234 227 ASP . 19930 1 235 228 HIS . 19930 1 236 229 ILE . 19930 1 237 230 ASP . 19930 1 238 231 GLN . 19930 1 239 232 LEU . 19930 1 240 233 LYS . 19930 1 241 234 LEU . 19930 1 242 235 ILE . 19930 1 243 236 LEU . 19930 1 244 237 ARG . 19930 1 245 238 LEU . 19930 1 246 239 VAL . 19930 1 247 240 GLY . 19930 1 248 241 THR . 19930 1 249 242 PRO . 19930 1 250 243 GLY . 19930 1 251 244 ALA . 19930 1 252 245 GLU . 19930 1 253 246 LEU . 19930 1 254 247 LEU . 19930 1 255 248 LYS . 19930 1 256 249 LYS . 19930 1 257 250 ILE . 19930 1 258 251 SER . 19930 1 259 252 SER . 19930 1 260 253 GLU . 19930 1 261 254 SER . 19930 1 262 255 ALA . 19930 1 263 256 ARG . 19930 1 264 257 ASN . 19930 1 265 258 TYR . 19930 1 266 259 ILE . 19930 1 267 260 GLN . 19930 1 268 261 SER . 19930 1 269 262 LEU . 19930 1 270 263 THR . 19930 1 271 264 GLN . 19930 1 272 265 MET . 19930 1 273 266 PRO . 19930 1 274 267 LYS . 19930 1 275 268 MET . 19930 1 276 269 ASN . 19930 1 277 270 PHE . 19930 1 278 271 ALA . 19930 1 279 272 ASN . 19930 1 280 273 VAL . 19930 1 281 274 PHE . 19930 1 282 275 ILE . 19930 1 283 276 GLY . 19930 1 284 277 ALA . 19930 1 285 278 ASN . 19930 1 286 279 PRO . 19930 1 287 280 LEU . 19930 1 288 281 ALA . 19930 1 289 282 VAL . 19930 1 290 283 ASP . 19930 1 291 284 LEU . 19930 1 292 285 LEU . 19930 1 293 286 GLU . 19930 1 294 287 LYS . 19930 1 295 288 MET . 19930 1 296 289 LEU . 19930 1 297 290 VAL . 19930 1 298 291 LEU . 19930 1 299 292 ASP . 19930 1 300 293 SER . 19930 1 301 294 ASP . 19930 1 302 295 LYS . 19930 1 303 296 ARG . 19930 1 304 297 ILE . 19930 1 305 298 THR . 19930 1 306 299 ALA . 19930 1 307 300 ALA . 19930 1 308 301 GLN . 19930 1 309 302 ALA . 19930 1 310 303 LEU . 19930 1 311 304 ALA . 19930 1 312 305 HIS . 19930 1 313 306 ALA . 19930 1 314 307 TYR . 19930 1 315 308 PHE . 19930 1 316 309 ALA . 19930 1 317 310 GLN . 19930 1 318 311 TYR . 19930 1 319 312 HIS . 19930 1 320 313 ASP . 19930 1 321 314 PRO . 19930 1 322 315 ASP . 19930 1 323 316 ASP . 19930 1 324 317 GLU . 19930 1 325 318 PRO . 19930 1 326 319 VAL . 19930 1 327 320 ALA . 19930 1 328 321 ASP . 19930 1 329 322 PRO . 19930 1 330 323 TYR . 19930 1 331 324 ASP . 19930 1 332 325 GLN . 19930 1 333 326 SER . 19930 1 334 327 PHE . 19930 1 335 328 GLU . 19930 1 336 329 SER . 19930 1 337 330 ARG . 19930 1 338 331 ASP . 19930 1 339 332 LEU . 19930 1 340 333 LEU . 19930 1 341 334 ILE . 19930 1 342 335 ASP . 19930 1 343 336 GLU . 19930 1 344 337 TRP . 19930 1 345 338 LYS . 19930 1 346 339 SER . 19930 1 347 340 LEU . 19930 1 348 341 THR . 19930 1 349 342 TYR . 19930 1 350 343 ASP . 19930 1 351 344 GLU . 19930 1 352 345 VAL . 19930 1 353 346 ILE . 19930 1 354 347 SER . 19930 1 355 348 PHE . 19930 1 356 349 VAL . 19930 1 357 350 PRO . 19930 1 358 351 PRO . 19930 1 359 352 PRO . 19930 1 360 353 LEU . 19930 1 361 354 ASP . 19930 1 362 355 GLN . 19930 1 363 356 GLU . 19930 1 364 357 GLU . 19930 1 365 358 MET . 19930 1 366 359 GLU . 19930 1 367 360 SER . 19930 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 19930 1 . ALA 2 2 19930 1 . HIS 3 3 19930 1 . HIS 4 4 19930 1 . HIS 5 5 19930 1 . HIS 6 6 19930 1 . HIS 7 7 19930 1 . HIS 8 8 19930 1 . SER 9 9 19930 1 . GLN 10 10 19930 1 . GLU 11 11 19930 1 . ARG 12 12 19930 1 . PRO 13 13 19930 1 . THR 14 14 19930 1 . PHE 15 15 19930 1 . TYR 16 16 19930 1 . ARG 17 17 19930 1 . GLN 18 18 19930 1 . GLU 19 19 19930 1 . LEU 20 20 19930 1 . ASN 21 21 19930 1 . LYS 22 22 19930 1 . THR 23 23 19930 1 . ILE 24 24 19930 1 . TRP 25 25 19930 1 . GLU 26 26 19930 1 . VAL 27 27 19930 1 . PRO 28 28 19930 1 . GLU 29 29 19930 1 . ARG 30 30 19930 1 . TYR 31 31 19930 1 . GLN 32 32 19930 1 . ASN 33 33 19930 1 . LEU 34 34 19930 1 . SER 35 35 19930 1 . PRO 36 36 19930 1 . VAL 37 37 19930 1 . GLY 38 38 19930 1 . SER 39 39 19930 1 . GLY 40 40 19930 1 . ALA 41 41 19930 1 . TYR 42 42 19930 1 . GLY 43 43 19930 1 . SER 44 44 19930 1 . VAL 45 45 19930 1 . CYS 46 46 19930 1 . ALA 47 47 19930 1 . ALA 48 48 19930 1 . PHE 49 49 19930 1 . ASP 50 50 19930 1 . THR 51 51 19930 1 . LYS 52 52 19930 1 . THR 53 53 19930 1 . GLY 54 54 19930 1 . LEU 55 55 19930 1 . ARG 56 56 19930 1 . VAL 57 57 19930 1 . ALA 58 58 19930 1 . VAL 59 59 19930 1 . LYS 60 60 19930 1 . LYS 61 61 19930 1 . LEU 62 62 19930 1 . SER 63 63 19930 1 . ARG 64 64 19930 1 . PRO 65 65 19930 1 . PHE 66 66 19930 1 . GLN 67 67 19930 1 . SER 68 68 19930 1 . ILE 69 69 19930 1 . ILE 70 70 19930 1 . HIS 71 71 19930 1 . ALA 72 72 19930 1 . LYS 73 73 19930 1 . ARG 74 74 19930 1 . THR 75 75 19930 1 . TYR 76 76 19930 1 . ARG 77 77 19930 1 . GLU 78 78 19930 1 . LEU 79 79 19930 1 . ARG 80 80 19930 1 . LEU 81 81 19930 1 . LEU 82 82 19930 1 . LYS 83 83 19930 1 . HIS 84 84 19930 1 . MET 85 85 19930 1 . LYS 86 86 19930 1 . HIS 87 87 19930 1 . GLU 88 88 19930 1 . ASN 89 89 19930 1 . VAL 90 90 19930 1 . ILE 91 91 19930 1 . GLY 92 92 19930 1 . LEU 93 93 19930 1 . LEU 94 94 19930 1 . ASP 95 95 19930 1 . VAL 96 96 19930 1 . PHE 97 97 19930 1 . THR 98 98 19930 1 . PRO 99 99 19930 1 . ALA 100 100 19930 1 . ARG 101 101 19930 1 . SER 102 102 19930 1 . LEU 103 103 19930 1 . GLU 104 104 19930 1 . GLU 105 105 19930 1 . PHE 106 106 19930 1 . ASN 107 107 19930 1 . ASP 108 108 19930 1 . VAL 109 109 19930 1 . TYR 110 110 19930 1 . LEU 111 111 19930 1 . VAL 112 112 19930 1 . THR 113 113 19930 1 . HIS 114 114 19930 1 . LEU 115 115 19930 1 . MET 116 116 19930 1 . GLY 117 117 19930 1 . ALA 118 118 19930 1 . ASP 119 119 19930 1 . LEU 120 120 19930 1 . ASN 121 121 19930 1 . ASN 122 122 19930 1 . ILE 123 123 19930 1 . VAL 124 124 19930 1 . LYS 125 125 19930 1 . CYS 126 126 19930 1 . GLN 127 127 19930 1 . LYS 128 128 19930 1 . LEU 129 129 19930 1 . THR 130 130 19930 1 . ASP 131 131 19930 1 . ASP 132 132 19930 1 . HIS 133 133 19930 1 . VAL 134 134 19930 1 . GLN 135 135 19930 1 . PHE 136 136 19930 1 . LEU 137 137 19930 1 . ILE 138 138 19930 1 . TYR 139 139 19930 1 . GLN 140 140 19930 1 . ILE 141 141 19930 1 . LEU 142 142 19930 1 . ARG 143 143 19930 1 . GLY 144 144 19930 1 . LEU 145 145 19930 1 . LYS 146 146 19930 1 . TYR 147 147 19930 1 . ILE 148 148 19930 1 . HIS 149 149 19930 1 . SER 150 150 19930 1 . ALA 151 151 19930 1 . ASP 152 152 19930 1 . ILE 153 153 19930 1 . ILE 154 154 19930 1 . HIS 155 155 19930 1 . ARG 156 156 19930 1 . ASP 157 157 19930 1 . LEU 158 158 19930 1 . LYS 159 159 19930 1 . PRO 160 160 19930 1 . SER 161 161 19930 1 . ASN 162 162 19930 1 . LEU 163 163 19930 1 . ALA 164 164 19930 1 . VAL 165 165 19930 1 . ASN 166 166 19930 1 . GLU 167 167 19930 1 . ASP 168 168 19930 1 . CYS 169 169 19930 1 . GLU 170 170 19930 1 . LEU 171 171 19930 1 . LYS 172 172 19930 1 . ILE 173 173 19930 1 . LEU 174 174 19930 1 . ASP 175 175 19930 1 . PHE 176 176 19930 1 . GLY 177 177 19930 1 . LEU 178 178 19930 1 . ALA 179 179 19930 1 . ARG 180 180 19930 1 . HIS 181 181 19930 1 . THR 182 182 19930 1 . ASP 183 183 19930 1 . ASP 184 184 19930 1 . GLU 185 185 19930 1 . MET 186 186 19930 1 . THR 187 187 19930 1 . GLY 188 188 19930 1 . TYR 189 189 19930 1 . VAL 190 190 19930 1 . ALA 191 191 19930 1 . THR 192 192 19930 1 . ARG 193 193 19930 1 . TRP 194 194 19930 1 . TYR 195 195 19930 1 . ARG 196 196 19930 1 . ALA 197 197 19930 1 . PRO 198 198 19930 1 . GLU 199 199 19930 1 . ILE 200 200 19930 1 . MET 201 201 19930 1 . LEU 202 202 19930 1 . ASN 203 203 19930 1 . TRP 204 204 19930 1 . MET 205 205 19930 1 . HIS 206 206 19930 1 . TYR 207 207 19930 1 . ASN 208 208 19930 1 . GLN 209 209 19930 1 . THR 210 210 19930 1 . VAL 211 211 19930 1 . ASP 212 212 19930 1 . ILE 213 213 19930 1 . TRP 214 214 19930 1 . SER 215 215 19930 1 . VAL 216 216 19930 1 . GLY 217 217 19930 1 . CYS 218 218 19930 1 . ILE 219 219 19930 1 . MET 220 220 19930 1 . ALA 221 221 19930 1 . GLU 222 222 19930 1 . LEU 223 223 19930 1 . LEU 224 224 19930 1 . THR 225 225 19930 1 . GLY 226 226 19930 1 . ARG 227 227 19930 1 . THR 228 228 19930 1 . LEU 229 229 19930 1 . PHE 230 230 19930 1 . PRO 231 231 19930 1 . GLY 232 232 19930 1 . THR 233 233 19930 1 . ASP 234 234 19930 1 . HIS 235 235 19930 1 . ILE 236 236 19930 1 . ASP 237 237 19930 1 . GLN 238 238 19930 1 . LEU 239 239 19930 1 . LYS 240 240 19930 1 . LEU 241 241 19930 1 . ILE 242 242 19930 1 . LEU 243 243 19930 1 . ARG 244 244 19930 1 . LEU 245 245 19930 1 . VAL 246 246 19930 1 . GLY 247 247 19930 1 . THR 248 248 19930 1 . PRO 249 249 19930 1 . GLY 250 250 19930 1 . ALA 251 251 19930 1 . GLU 252 252 19930 1 . LEU 253 253 19930 1 . LEU 254 254 19930 1 . LYS 255 255 19930 1 . LYS 256 256 19930 1 . ILE 257 257 19930 1 . SER 258 258 19930 1 . SER 259 259 19930 1 . GLU 260 260 19930 1 . SER 261 261 19930 1 . ALA 262 262 19930 1 . ARG 263 263 19930 1 . ASN 264 264 19930 1 . TYR 265 265 19930 1 . ILE 266 266 19930 1 . GLN 267 267 19930 1 . SER 268 268 19930 1 . LEU 269 269 19930 1 . THR 270 270 19930 1 . GLN 271 271 19930 1 . MET 272 272 19930 1 . PRO 273 273 19930 1 . LYS 274 274 19930 1 . MET 275 275 19930 1 . ASN 276 276 19930 1 . PHE 277 277 19930 1 . ALA 278 278 19930 1 . ASN 279 279 19930 1 . VAL 280 280 19930 1 . PHE 281 281 19930 1 . ILE 282 282 19930 1 . GLY 283 283 19930 1 . ALA 284 284 19930 1 . ASN 285 285 19930 1 . PRO 286 286 19930 1 . LEU 287 287 19930 1 . ALA 288 288 19930 1 . VAL 289 289 19930 1 . ASP 290 290 19930 1 . LEU 291 291 19930 1 . LEU 292 292 19930 1 . GLU 293 293 19930 1 . LYS 294 294 19930 1 . MET 295 295 19930 1 . LEU 296 296 19930 1 . VAL 297 297 19930 1 . LEU 298 298 19930 1 . ASP 299 299 19930 1 . SER 300 300 19930 1 . ASP 301 301 19930 1 . LYS 302 302 19930 1 . ARG 303 303 19930 1 . ILE 304 304 19930 1 . THR 305 305 19930 1 . ALA 306 306 19930 1 . ALA 307 307 19930 1 . GLN 308 308 19930 1 . ALA 309 309 19930 1 . LEU 310 310 19930 1 . ALA 311 311 19930 1 . HIS 312 312 19930 1 . ALA 313 313 19930 1 . TYR 314 314 19930 1 . PHE 315 315 19930 1 . ALA 316 316 19930 1 . GLN 317 317 19930 1 . TYR 318 318 19930 1 . HIS 319 319 19930 1 . ASP 320 320 19930 1 . PRO 321 321 19930 1 . ASP 322 322 19930 1 . ASP 323 323 19930 1 . GLU 324 324 19930 1 . PRO 325 325 19930 1 . VAL 326 326 19930 1 . ALA 327 327 19930 1 . ASP 328 328 19930 1 . PRO 329 329 19930 1 . TYR 330 330 19930 1 . ASP 331 331 19930 1 . GLN 332 332 19930 1 . SER 333 333 19930 1 . PHE 334 334 19930 1 . GLU 335 335 19930 1 . SER 336 336 19930 1 . ARG 337 337 19930 1 . ASP 338 338 19930 1 . LEU 339 339 19930 1 . LEU 340 340 19930 1 . ILE 341 341 19930 1 . ASP 342 342 19930 1 . GLU 343 343 19930 1 . TRP 344 344 19930 1 . LYS 345 345 19930 1 . SER 346 346 19930 1 . LEU 347 347 19930 1 . THR 348 348 19930 1 . TYR 349 349 19930 1 . ASP 350 350 19930 1 . GLU 351 351 19930 1 . VAL 352 352 19930 1 . ILE 353 353 19930 1 . SER 354 354 19930 1 . PHE 355 355 19930 1 . VAL 356 356 19930 1 . PRO 357 357 19930 1 . PRO 358 358 19930 1 . PRO 359 359 19930 1 . LEU 360 360 19930 1 . ASP 361 361 19930 1 . GLN 362 362 19930 1 . GLU 363 363 19930 1 . GLU 364 364 19930 1 . MET 365 365 19930 1 . GLU 366 366 19930 1 . SER 367 367 19930 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 19930 _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 $Non-phosphorylated_human_p38_alpha_(apo) . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 19930 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 19930 _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 $Non-phosphorylated_human_p38_alpha_(apo) . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET15b . . . . . . 19930 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 19930 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _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 'Non-phosphorylated human p38 alpha (apo)' 'U-2H15N13C, ILVM-methyl-1H13C]' . . 1 $Non-phosphorylated_human_p38_alpha_(apo) . . 0.2 . . mM . . . . 19930 1 2 TRIS '[U-100% 2H]' . . . . . . 25 . . mM . . . . 19930 1 3 'potassium chloride' 'natural abundance' . . . . . . 150 . . mM . . . . 19930 1 4 DTT [U-2H] . . . . . . 5 . . mM . . . . 19930 1 5 H2O 'natural abundance' . . . . . . 90 . . % . . . . 19930 1 6 D2O '[U-100% 2H]' . . . . . . 10 . . % . . . . 19930 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 19930 _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' 150 . mM 19930 1 pH 7.5 . pH 19930 1 pressure 1 . atm 19930 1 temperature 298 . K 19930 1 stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 19930 _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 Biospin' . . 19930 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 19930 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 19930 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 19930 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 19930 2 stop_ save_ save_CARA _Software.Sf_category software _Software.Sf_framecode CARA _Software.Entry_ID 19930 _Software.ID 3 _Software.Name CARA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Keller, R.' . . 19930 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 19930 3 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 19930 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 19930 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_3 _NMR_spectrometer.Entry_ID 19930 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 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 19930 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 600 . . . 19930 1 2 spectrometer_2 Bruker Avance . 700 . . . 19930 1 3 spectrometer_3 Bruker Avance . 800 . . . 19930 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 19930 _Experiment_list.ID 1 _Experiment_list.Details ; Assignments of the ILVM-methyl resonances in p38 were performed by combining a mutational analysis, J-coupling-based triple resonance experiments ((H)CC(CO)NH, H(CCCO)NH, and HCCH-TOCSY experiments), and an analysis of the inter-methyl 1H-1H NOE network based on the crystal structures. ; 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 (H)CC(CO)NH no . . . . . . . . . . 1 $sample_2 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19930 1 2 H(CCCO)NH no . . . . . . . . . . 1 $sample_2 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19930 1 3 HCCH-TOCSY no . . . . . . . . . . 1 $sample_2 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19930 1 4 '3D 1H-13C NOESY aliphatic' no . . . . . . . . . . 1 $sample_2 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19930 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 19930 _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 . . . . . . . . . 19930 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 19930 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_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_2 _Assigned_chem_shift_list.Entry_ID 19930 _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 (H)CC(CO)NH . . . 19930 1 2 H(CCCO)NH . . . 19930 1 3 HCCH-TOCSY . . . 19930 1 4 '3D 1H-13C NOESY aliphatic' . . . 19930 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 20 20 LEU HD11 H 1 0.274 0.014 . 2 . . . . 13 LEU HD1 . 19930 1 2 . 1 1 20 20 LEU HD12 H 1 0.274 0.014 . 2 . . . . 13 LEU HD1 . 19930 1 3 . 1 1 20 20 LEU HD13 H 1 0.274 0.014 . 2 . . . . 13 LEU HD1 . 19930 1 4 . 1 1 20 20 LEU HD21 H 1 0.702 0.014 . 2 . . . . 13 LEU HD2 . 19930 1 5 . 1 1 20 20 LEU HD22 H 1 0.702 0.014 . 2 . . . . 13 LEU HD2 . 19930 1 6 . 1 1 20 20 LEU HD23 H 1 0.702 0.014 . 2 . . . . 13 LEU HD2 . 19930 1 7 . 1 1 20 20 LEU CD1 C 13 25.876 0.045 . 1 . . . . 13 LEU CD1 . 19930 1 8 . 1 1 20 20 LEU CD2 C 13 24.081 0.045 . 1 . . . . 13 LEU CD2 . 19930 1 9 . 1 1 24 24 ILE HD11 H 1 0.746 0.014 . 1 . . . . 17 ILE HD1 . 19930 1 10 . 1 1 24 24 ILE HD12 H 1 0.746 0.014 . 1 . . . . 17 ILE HD1 . 19930 1 11 . 1 1 24 24 ILE HD13 H 1 0.746 0.014 . 1 . . . . 17 ILE HD1 . 19930 1 12 . 1 1 24 24 ILE CD1 C 13 10.645 0.045 . 1 . . . . 17 ILE CD1 . 19930 1 13 . 1 1 27 27 VAL HG11 H 1 0.931 0.014 . 2 . . . . 20 VAL HG1 . 19930 1 14 . 1 1 27 27 VAL HG12 H 1 0.931 0.014 . 2 . . . . 20 VAL HG1 . 19930 1 15 . 1 1 27 27 VAL HG13 H 1 0.931 0.014 . 2 . . . . 20 VAL HG1 . 19930 1 16 . 1 1 27 27 VAL HG21 H 1 0.693 0.014 . 2 . . . . 20 VAL HG2 . 19930 1 17 . 1 1 27 27 VAL HG22 H 1 0.693 0.014 . 2 . . . . 20 VAL HG2 . 19930 1 18 . 1 1 27 27 VAL HG23 H 1 0.693 0.014 . 2 . . . . 20 VAL HG2 . 19930 1 19 . 1 1 27 27 VAL CG1 C 13 21.746 0.045 . 1 . . . . 20 VAL CG1 . 19930 1 20 . 1 1 27 27 VAL CG2 C 13 19.452 0.045 . 1 . . . . 20 VAL CG2 . 19930 1 21 . 1 1 34 34 LEU HD11 H 1 0.719 0.014 . 2 . . . . 27 LEU HD1 . 19930 1 22 . 1 1 34 34 LEU HD12 H 1 0.719 0.014 . 2 . . . . 27 LEU HD1 . 19930 1 23 . 1 1 34 34 LEU HD13 H 1 0.719 0.014 . 2 . . . . 27 LEU HD1 . 19930 1 24 . 1 1 34 34 LEU HD21 H 1 0.575 0.014 . 2 . . . . 27 LEU HD2 . 19930 1 25 . 1 1 34 34 LEU HD22 H 1 0.575 0.014 . 2 . . . . 27 LEU HD2 . 19930 1 26 . 1 1 34 34 LEU HD23 H 1 0.575 0.014 . 2 . . . . 27 LEU HD2 . 19930 1 27 . 1 1 34 34 LEU CD1 C 13 24.589 0.045 . 1 . . . . 27 LEU CD1 . 19930 1 28 . 1 1 34 34 LEU CD2 C 13 24.471 0.045 . 1 . . . . 27 LEU CD2 . 19930 1 29 . 1 1 37 37 VAL HG11 H 1 0.935 0.014 . 2 . . . . 30 VAL HG1 . 19930 1 30 . 1 1 37 37 VAL HG12 H 1 0.935 0.014 . 2 . . . . 30 VAL HG1 . 19930 1 31 . 1 1 37 37 VAL HG13 H 1 0.935 0.014 . 2 . . . . 30 VAL HG1 . 19930 1 32 . 1 1 37 37 VAL HG21 H 1 0.86 0.014 . 2 . . . . 30 VAL HG2 . 19930 1 33 . 1 1 37 37 VAL HG22 H 1 0.86 0.014 . 2 . . . . 30 VAL HG2 . 19930 1 34 . 1 1 37 37 VAL HG23 H 1 0.86 0.014 . 2 . . . . 30 VAL HG2 . 19930 1 35 . 1 1 37 37 VAL CG1 C 13 21.25 0.045 . 1 . . . . 30 VAL CG1 . 19930 1 36 . 1 1 37 37 VAL CG2 C 13 20.713 0.045 . 1 . . . . 30 VAL CG2 . 19930 1 37 . 1 1 45 45 VAL HG11 H 1 0.816 0.014 . 2 . . . . 38 VAL HG1 . 19930 1 38 . 1 1 45 45 VAL HG12 H 1 0.816 0.014 . 2 . . . . 38 VAL HG1 . 19930 1 39 . 1 1 45 45 VAL HG13 H 1 0.816 0.014 . 2 . . . . 38 VAL HG1 . 19930 1 40 . 1 1 45 45 VAL HG21 H 1 0.881 0.014 . 2 . . . . 38 VAL HG2 . 19930 1 41 . 1 1 45 45 VAL HG22 H 1 0.881 0.014 . 2 . . . . 38 VAL HG2 . 19930 1 42 . 1 1 45 45 VAL HG23 H 1 0.881 0.014 . 2 . . . . 38 VAL HG2 . 19930 1 43 . 1 1 45 45 VAL CG1 C 13 21.276 0.045 . 1 . . . . 38 VAL CG1 . 19930 1 44 . 1 1 45 45 VAL CG2 C 13 21.455 0.045 . 1 . . . . 38 VAL CG2 . 19930 1 45 . 1 1 55 55 LEU HD11 H 1 0.874 0.014 . 2 . . . . 48 LEU HD1 . 19930 1 46 . 1 1 55 55 LEU HD12 H 1 0.874 0.014 . 2 . . . . 48 LEU HD1 . 19930 1 47 . 1 1 55 55 LEU HD13 H 1 0.874 0.014 . 2 . . . . 48 LEU HD1 . 19930 1 48 . 1 1 55 55 LEU HD21 H 1 0.911 0.014 . 2 . . . . 48 LEU HD2 . 19930 1 49 . 1 1 55 55 LEU HD22 H 1 0.911 0.014 . 2 . . . . 48 LEU HD2 . 19930 1 50 . 1 1 55 55 LEU HD23 H 1 0.911 0.014 . 2 . . . . 48 LEU HD2 . 19930 1 51 . 1 1 55 55 LEU CD1 C 13 24.781 0.045 . 1 . . . . 48 LEU CD1 . 19930 1 52 . 1 1 55 55 LEU CD2 C 13 22.421 0.045 . 1 . . . . 48 LEU CD2 . 19930 1 53 . 1 1 57 57 VAL HG11 H 1 0.745 0.014 . 2 . . . . 50 VAL HG1 . 19930 1 54 . 1 1 57 57 VAL HG12 H 1 0.745 0.014 . 2 . . . . 50 VAL HG1 . 19930 1 55 . 1 1 57 57 VAL HG13 H 1 0.745 0.014 . 2 . . . . 50 VAL HG1 . 19930 1 56 . 1 1 57 57 VAL HG21 H 1 0.63 0.014 . 2 . . . . 50 VAL HG2 . 19930 1 57 . 1 1 57 57 VAL HG22 H 1 0.63 0.014 . 2 . . . . 50 VAL HG2 . 19930 1 58 . 1 1 57 57 VAL HG23 H 1 0.63 0.014 . 2 . . . . 50 VAL HG2 . 19930 1 59 . 1 1 57 57 VAL CG1 C 13 22.191 0.045 . 1 . . . . 50 VAL CG1 . 19930 1 60 . 1 1 57 57 VAL CG2 C 13 18.433 0.045 . 1 . . . . 50 VAL CG2 . 19930 1 61 . 1 1 59 59 VAL HG11 H 1 1.082 0.014 . 2 . . . . 52 VAL HG1 . 19930 1 62 . 1 1 59 59 VAL HG12 H 1 1.082 0.014 . 2 . . . . 52 VAL HG1 . 19930 1 63 . 1 1 59 59 VAL HG13 H 1 1.082 0.014 . 2 . . . . 52 VAL HG1 . 19930 1 64 . 1 1 59 59 VAL HG21 H 1 0.543 0.014 . 2 . . . . 52 VAL HG2 . 19930 1 65 . 1 1 59 59 VAL HG22 H 1 0.543 0.014 . 2 . . . . 52 VAL HG2 . 19930 1 66 . 1 1 59 59 VAL HG23 H 1 0.543 0.014 . 2 . . . . 52 VAL HG2 . 19930 1 67 . 1 1 59 59 VAL CG1 C 13 22.297 0.045 . 1 . . . . 52 VAL CG1 . 19930 1 68 . 1 1 59 59 VAL CG2 C 13 20.234 0.045 . 1 . . . . 52 VAL CG2 . 19930 1 69 . 1 1 62 62 LEU HD11 H 1 0.789 0.014 . 2 . . . . 55 LEU HD1 . 19930 1 70 . 1 1 62 62 LEU HD12 H 1 0.789 0.014 . 2 . . . . 55 LEU HD1 . 19930 1 71 . 1 1 62 62 LEU HD13 H 1 0.789 0.014 . 2 . . . . 55 LEU HD1 . 19930 1 72 . 1 1 62 62 LEU HD21 H 1 0.76 0.014 . 2 . . . . 55 LEU HD2 . 19930 1 73 . 1 1 62 62 LEU HD22 H 1 0.76 0.014 . 2 . . . . 55 LEU HD2 . 19930 1 74 . 1 1 62 62 LEU HD23 H 1 0.76 0.014 . 2 . . . . 55 LEU HD2 . 19930 1 75 . 1 1 62 62 LEU CD1 C 13 25.585 0.045 . 1 . . . . 55 LEU CD1 . 19930 1 76 . 1 1 62 62 LEU CD2 C 13 22.922 0.045 . 1 . . . . 55 LEU CD2 . 19930 1 77 . 1 1 69 69 ILE HD11 H 1 0.948 0.014 . 1 . . . . 62 ILE HD1 . 19930 1 78 . 1 1 69 69 ILE HD12 H 1 0.948 0.014 . 1 . . . . 62 ILE HD1 . 19930 1 79 . 1 1 69 69 ILE HD13 H 1 0.948 0.014 . 1 . . . . 62 ILE HD1 . 19930 1 80 . 1 1 69 69 ILE CD1 C 13 13.75 0.045 . 1 . . . . 62 ILE CD1 . 19930 1 81 . 1 1 70 70 ILE HD11 H 1 0.845 0.014 . 1 . . . . 63 ILE HD1 . 19930 1 82 . 1 1 70 70 ILE HD12 H 1 0.845 0.014 . 1 . . . . 63 ILE HD1 . 19930 1 83 . 1 1 70 70 ILE HD13 H 1 0.845 0.014 . 1 . . . . 63 ILE HD1 . 19930 1 84 . 1 1 70 70 ILE CD1 C 13 12.22 0.045 . 1 . . . . 63 ILE CD1 . 19930 1 85 . 1 1 79 79 LEU HD11 H 1 0.932 0.014 . 2 . . . . 72 LEU HD1 . 19930 1 86 . 1 1 79 79 LEU HD12 H 1 0.932 0.014 . 2 . . . . 72 LEU HD1 . 19930 1 87 . 1 1 79 79 LEU HD13 H 1 0.932 0.014 . 2 . . . . 72 LEU HD1 . 19930 1 88 . 1 1 79 79 LEU HD21 H 1 0.9 0.014 . 2 . . . . 72 LEU HD2 . 19930 1 89 . 1 1 79 79 LEU HD22 H 1 0.9 0.014 . 2 . . . . 72 LEU HD2 . 19930 1 90 . 1 1 79 79 LEU HD23 H 1 0.9 0.014 . 2 . . . . 72 LEU HD2 . 19930 1 91 . 1 1 79 79 LEU CD1 C 13 24.711 0.045 . 1 . . . . 72 LEU CD1 . 19930 1 92 . 1 1 79 79 LEU CD2 C 13 27.789 0.045 . 1 . . . . 72 LEU CD2 . 19930 1 93 . 1 1 81 81 LEU HD11 H 1 0.568 0.014 . 2 . . . . 74 LEU HD1 . 19930 1 94 . 1 1 81 81 LEU HD12 H 1 0.568 0.014 . 2 . . . . 74 LEU HD1 . 19930 1 95 . 1 1 81 81 LEU HD13 H 1 0.568 0.014 . 2 . . . . 74 LEU HD1 . 19930 1 96 . 1 1 81 81 LEU HD21 H 1 0.36 0.014 . 2 . . . . 74 LEU HD2 . 19930 1 97 . 1 1 81 81 LEU HD22 H 1 0.36 0.014 . 2 . . . . 74 LEU HD2 . 19930 1 98 . 1 1 81 81 LEU HD23 H 1 0.36 0.014 . 2 . . . . 74 LEU HD2 . 19930 1 99 . 1 1 81 81 LEU CD1 C 13 25.211 0.045 . 1 . . . . 74 LEU CD1 . 19930 1 100 . 1 1 81 81 LEU CD2 C 13 24.492 0.045 . 1 . . . . 74 LEU CD2 . 19930 1 101 . 1 1 82 82 LEU HD11 H 1 0.871 0.014 . 2 . . . . 75 LEU HD1 . 19930 1 102 . 1 1 82 82 LEU HD12 H 1 0.871 0.014 . 2 . . . . 75 LEU HD1 . 19930 1 103 . 1 1 82 82 LEU HD13 H 1 0.871 0.014 . 2 . . . . 75 LEU HD1 . 19930 1 104 . 1 1 82 82 LEU HD21 H 1 0.861 0.014 . 2 . . . . 75 LEU HD2 . 19930 1 105 . 1 1 82 82 LEU HD22 H 1 0.861 0.014 . 2 . . . . 75 LEU HD2 . 19930 1 106 . 1 1 82 82 LEU HD23 H 1 0.861 0.014 . 2 . . . . 75 LEU HD2 . 19930 1 107 . 1 1 82 82 LEU CD1 C 13 26.465 0.045 . 1 . . . . 75 LEU CD1 . 19930 1 108 . 1 1 82 82 LEU CD2 C 13 22.994 0.045 . 1 . . . . 75 LEU CD2 . 19930 1 109 . 1 1 85 85 MET HE1 H 1 1.778 0.014 . 1 . . . . 78 MET HE . 19930 1 110 . 1 1 85 85 MET HE2 H 1 1.778 0.014 . 1 . . . . 78 MET HE . 19930 1 111 . 1 1 85 85 MET HE3 H 1 1.778 0.014 . 1 . . . . 78 MET HE . 19930 1 112 . 1 1 85 85 MET CE C 13 19.094 0.045 . 1 . . . . 78 MET CE . 19930 1 113 . 1 1 90 90 VAL HG11 H 1 1.191 0.014 . 2 . . . . 83 VAL HG1 . 19930 1 114 . 1 1 90 90 VAL HG12 H 1 1.191 0.014 . 2 . . . . 83 VAL HG1 . 19930 1 115 . 1 1 90 90 VAL HG13 H 1 1.191 0.014 . 2 . . . . 83 VAL HG1 . 19930 1 116 . 1 1 90 90 VAL HG21 H 1 0.773 0.014 . 2 . . . . 83 VAL HG2 . 19930 1 117 . 1 1 90 90 VAL HG22 H 1 0.773 0.014 . 2 . . . . 83 VAL HG2 . 19930 1 118 . 1 1 90 90 VAL HG23 H 1 0.773 0.014 . 2 . . . . 83 VAL HG2 . 19930 1 119 . 1 1 90 90 VAL CG1 C 13 22.316 0.045 . 1 . . . . 83 VAL CG1 . 19930 1 120 . 1 1 90 90 VAL CG2 C 13 21.651 0.045 . 1 . . . . 83 VAL CG2 . 19930 1 121 . 1 1 91 91 ILE HD11 H 1 1.13 0.014 . 1 . . . . 84 ILE HD1 . 19930 1 122 . 1 1 91 91 ILE HD12 H 1 1.13 0.014 . 1 . . . . 84 ILE HD1 . 19930 1 123 . 1 1 91 91 ILE HD13 H 1 1.13 0.014 . 1 . . . . 84 ILE HD1 . 19930 1 124 . 1 1 91 91 ILE CD1 C 13 14.432 0.045 . 1 . . . . 84 ILE CD1 . 19930 1 125 . 1 1 93 93 LEU HD11 H 1 0.878 0.014 . 2 . . . . 86 LEU HD1 . 19930 1 126 . 1 1 93 93 LEU HD12 H 1 0.878 0.014 . 2 . . . . 86 LEU HD1 . 19930 1 127 . 1 1 93 93 LEU HD13 H 1 0.878 0.014 . 2 . . . . 86 LEU HD1 . 19930 1 128 . 1 1 93 93 LEU HD21 H 1 0.614 0.014 . 2 . . . . 86 LEU HD2 . 19930 1 129 . 1 1 93 93 LEU HD22 H 1 0.614 0.014 . 2 . . . . 86 LEU HD2 . 19930 1 130 . 1 1 93 93 LEU HD23 H 1 0.614 0.014 . 2 . . . . 86 LEU HD2 . 19930 1 131 . 1 1 93 93 LEU CD1 C 13 24.484 0.045 . 1 . . . . 86 LEU CD1 . 19930 1 132 . 1 1 93 93 LEU CD2 C 13 25.578 0.045 . 1 . . . . 86 LEU CD2 . 19930 1 133 . 1 1 94 94 LEU HD11 H 1 0.454 0.014 . 2 . . . . 87 LEU HD1 . 19930 1 134 . 1 1 94 94 LEU HD12 H 1 0.454 0.014 . 2 . . . . 87 LEU HD1 . 19930 1 135 . 1 1 94 94 LEU HD13 H 1 0.454 0.014 . 2 . . . . 87 LEU HD1 . 19930 1 136 . 1 1 94 94 LEU HD21 H 1 0.688 0.014 . 2 . . . . 87 LEU HD2 . 19930 1 137 . 1 1 94 94 LEU HD22 H 1 0.688 0.014 . 2 . . . . 87 LEU HD2 . 19930 1 138 . 1 1 94 94 LEU HD23 H 1 0.688 0.014 . 2 . . . . 87 LEU HD2 . 19930 1 139 . 1 1 94 94 LEU CD1 C 13 25.086 0.045 . 1 . . . . 87 LEU CD1 . 19930 1 140 . 1 1 94 94 LEU CD2 C 13 22.731 0.045 . 1 . . . . 87 LEU CD2 . 19930 1 141 . 1 1 96 96 VAL HG11 H 1 0.59 0.014 . 2 . . . . 89 VAL HG1 . 19930 1 142 . 1 1 96 96 VAL HG12 H 1 0.59 0.014 . 2 . . . . 89 VAL HG1 . 19930 1 143 . 1 1 96 96 VAL HG13 H 1 0.59 0.014 . 2 . . . . 89 VAL HG1 . 19930 1 144 . 1 1 96 96 VAL HG21 H 1 0.91 0.014 . 2 . . . . 89 VAL HG2 . 19930 1 145 . 1 1 96 96 VAL HG22 H 1 0.91 0.014 . 2 . . . . 89 VAL HG2 . 19930 1 146 . 1 1 96 96 VAL HG23 H 1 0.91 0.014 . 2 . . . . 89 VAL HG2 . 19930 1 147 . 1 1 96 96 VAL CG1 C 13 19.71 0.045 . 1 . . . . 89 VAL CG1 . 19930 1 148 . 1 1 96 96 VAL CG2 C 13 23.145 0.045 . 1 . . . . 89 VAL CG2 . 19930 1 149 . 1 1 109 109 VAL HG11 H 1 0.769 0.014 . 2 . . . . 102 VAL HG1 . 19930 1 150 . 1 1 109 109 VAL HG12 H 1 0.769 0.014 . 2 . . . . 102 VAL HG1 . 19930 1 151 . 1 1 109 109 VAL HG13 H 1 0.769 0.014 . 2 . . . . 102 VAL HG1 . 19930 1 152 . 1 1 109 109 VAL HG21 H 1 0.943 0.014 . 2 . . . . 102 VAL HG2 . 19930 1 153 . 1 1 109 109 VAL HG22 H 1 0.943 0.014 . 2 . . . . 102 VAL HG2 . 19930 1 154 . 1 1 109 109 VAL HG23 H 1 0.943 0.014 . 2 . . . . 102 VAL HG2 . 19930 1 155 . 1 1 109 109 VAL CG1 C 13 20.903 0.045 . 1 . . . . 102 VAL CG1 . 19930 1 156 . 1 1 109 109 VAL CG2 C 13 22.332 0.045 . 1 . . . . 102 VAL CG2 . 19930 1 157 . 1 1 111 111 LEU HD11 H 1 0.747 0.014 . 2 . . . . 104 LEU HD1 . 19930 1 158 . 1 1 111 111 LEU HD12 H 1 0.747 0.014 . 2 . . . . 104 LEU HD1 . 19930 1 159 . 1 1 111 111 LEU HD13 H 1 0.747 0.014 . 2 . . . . 104 LEU HD1 . 19930 1 160 . 1 1 111 111 LEU HD21 H 1 0.751 0.014 . 2 . . . . 104 LEU HD2 . 19930 1 161 . 1 1 111 111 LEU HD22 H 1 0.751 0.014 . 2 . . . . 104 LEU HD2 . 19930 1 162 . 1 1 111 111 LEU HD23 H 1 0.751 0.014 . 2 . . . . 104 LEU HD2 . 19930 1 163 . 1 1 111 111 LEU CD1 C 13 25.738 0.045 . 1 . . . . 104 LEU CD1 . 19930 1 164 . 1 1 111 111 LEU CD2 C 13 24.356 0.045 . 1 . . . . 104 LEU CD2 . 19930 1 165 . 1 1 112 112 VAL HG11 H 1 0.868 0.014 . 2 . . . . 105 VAL HG1 . 19930 1 166 . 1 1 112 112 VAL HG12 H 1 0.868 0.014 . 2 . . . . 105 VAL HG1 . 19930 1 167 . 1 1 112 112 VAL HG13 H 1 0.868 0.014 . 2 . . . . 105 VAL HG1 . 19930 1 168 . 1 1 112 112 VAL HG21 H 1 0.726 0.014 . 2 . . . . 105 VAL HG2 . 19930 1 169 . 1 1 112 112 VAL HG22 H 1 0.726 0.014 . 2 . . . . 105 VAL HG2 . 19930 1 170 . 1 1 112 112 VAL HG23 H 1 0.726 0.014 . 2 . . . . 105 VAL HG2 . 19930 1 171 . 1 1 112 112 VAL CG1 C 13 20.579 0.045 . 1 . . . . 105 VAL CG1 . 19930 1 172 . 1 1 112 112 VAL CG2 C 13 21.078 0.045 . 1 . . . . 105 VAL CG2 . 19930 1 173 . 1 1 116 116 MET HE1 H 1 1.895 0.014 . 1 . . . . 109 MET HE . 19930 1 174 . 1 1 116 116 MET HE2 H 1 1.895 0.014 . 1 . . . . 109 MET HE . 19930 1 175 . 1 1 116 116 MET HE3 H 1 1.895 0.014 . 1 . . . . 109 MET HE . 19930 1 176 . 1 1 116 116 MET CE C 13 17.627 0.045 . 1 . . . . 109 MET CE . 19930 1 177 . 1 1 120 120 LEU HD11 H 1 0.822 0.014 . 2 . . . . 113 LEU HD1 . 19930 1 178 . 1 1 120 120 LEU HD12 H 1 0.822 0.014 . 2 . . . . 113 LEU HD1 . 19930 1 179 . 1 1 120 120 LEU HD13 H 1 0.822 0.014 . 2 . . . . 113 LEU HD1 . 19930 1 180 . 1 1 120 120 LEU HD21 H 1 0.713 0.014 . 2 . . . . 113 LEU HD2 . 19930 1 181 . 1 1 120 120 LEU HD22 H 1 0.713 0.014 . 2 . . . . 113 LEU HD2 . 19930 1 182 . 1 1 120 120 LEU HD23 H 1 0.713 0.014 . 2 . . . . 113 LEU HD2 . 19930 1 183 . 1 1 120 120 LEU CD1 C 13 24.6 0.045 . 1 . . . . 113 LEU CD1 . 19930 1 184 . 1 1 120 120 LEU CD2 C 13 25.614 0.045 . 1 . . . . 113 LEU CD2 . 19930 1 185 . 1 1 123 123 ILE HD11 H 1 0.698 0.014 . 1 . . . . 116 ILE HD1 . 19930 1 186 . 1 1 123 123 ILE HD12 H 1 0.698 0.014 . 1 . . . . 116 ILE HD1 . 19930 1 187 . 1 1 123 123 ILE HD13 H 1 0.698 0.014 . 1 . . . . 116 ILE HD1 . 19930 1 188 . 1 1 123 123 ILE CD1 C 13 11.621 0.045 . 1 . . . . 116 ILE CD1 . 19930 1 189 . 1 1 124 124 VAL HG11 H 1 0.997 0.014 . 2 . . . . 117 VAL HG1 . 19930 1 190 . 1 1 124 124 VAL HG12 H 1 0.997 0.014 . 2 . . . . 117 VAL HG1 . 19930 1 191 . 1 1 124 124 VAL HG13 H 1 0.997 0.014 . 2 . . . . 117 VAL HG1 . 19930 1 192 . 1 1 124 124 VAL HG21 H 1 1.019 0.014 . 2 . . . . 117 VAL HG2 . 19930 1 193 . 1 1 124 124 VAL HG22 H 1 1.019 0.014 . 2 . . . . 117 VAL HG2 . 19930 1 194 . 1 1 124 124 VAL HG23 H 1 1.019 0.014 . 2 . . . . 117 VAL HG2 . 19930 1 195 . 1 1 124 124 VAL CG1 C 13 21.221 0.045 . 1 . . . . 117 VAL CG1 . 19930 1 196 . 1 1 124 124 VAL CG2 C 13 21.987 0.045 . 1 . . . . 117 VAL CG2 . 19930 1 197 . 1 1 129 129 LEU HD11 H 1 0.828 0.014 . 2 . . . . 122 LEU HD1 . 19930 1 198 . 1 1 129 129 LEU HD12 H 1 0.828 0.014 . 2 . . . . 122 LEU HD1 . 19930 1 199 . 1 1 129 129 LEU HD13 H 1 0.828 0.014 . 2 . . . . 122 LEU HD1 . 19930 1 200 . 1 1 129 129 LEU HD21 H 1 0.609 0.014 . 2 . . . . 122 LEU HD2 . 19930 1 201 . 1 1 129 129 LEU HD22 H 1 0.609 0.014 . 2 . . . . 122 LEU HD2 . 19930 1 202 . 1 1 129 129 LEU HD23 H 1 0.609 0.014 . 2 . . . . 122 LEU HD2 . 19930 1 203 . 1 1 129 129 LEU CD1 C 13 26.609 0.045 . 1 . . . . 122 LEU CD1 . 19930 1 204 . 1 1 129 129 LEU CD2 C 13 22.785 0.045 . 1 . . . . 122 LEU CD2 . 19930 1 205 . 1 1 134 134 VAL HG11 H 1 1.13 0.014 . 2 . . . . 127 VAL HG1 . 19930 1 206 . 1 1 134 134 VAL HG12 H 1 1.13 0.014 . 2 . . . . 127 VAL HG1 . 19930 1 207 . 1 1 134 134 VAL HG13 H 1 1.13 0.014 . 2 . . . . 127 VAL HG1 . 19930 1 208 . 1 1 134 134 VAL HG21 H 1 1.055 0.014 . 2 . . . . 127 VAL HG2 . 19930 1 209 . 1 1 134 134 VAL HG22 H 1 1.055 0.014 . 2 . . . . 127 VAL HG2 . 19930 1 210 . 1 1 134 134 VAL HG23 H 1 1.055 0.014 . 2 . . . . 127 VAL HG2 . 19930 1 211 . 1 1 134 134 VAL CG1 C 13 22.404 0.045 . 1 . . . . 127 VAL CG1 . 19930 1 212 . 1 1 134 134 VAL CG2 C 13 23.544 0.045 . 1 . . . . 127 VAL CG2 . 19930 1 213 . 1 1 137 137 LEU HD11 H 1 0.797 0.014 . 2 . . . . 130 LEU HD1 . 19930 1 214 . 1 1 137 137 LEU HD12 H 1 0.797 0.014 . 2 . . . . 130 LEU HD1 . 19930 1 215 . 1 1 137 137 LEU HD13 H 1 0.797 0.014 . 2 . . . . 130 LEU HD1 . 19930 1 216 . 1 1 137 137 LEU HD21 H 1 0.738 0.014 . 2 . . . . 130 LEU HD2 . 19930 1 217 . 1 1 137 137 LEU HD22 H 1 0.738 0.014 . 2 . . . . 130 LEU HD2 . 19930 1 218 . 1 1 137 137 LEU HD23 H 1 0.738 0.014 . 2 . . . . 130 LEU HD2 . 19930 1 219 . 1 1 137 137 LEU CD1 C 13 26.594 0.045 . 1 . . . . 130 LEU CD1 . 19930 1 220 . 1 1 137 137 LEU CD2 C 13 24.231 0.045 . 1 . . . . 130 LEU CD2 . 19930 1 221 . 1 1 138 138 ILE HD11 H 1 0.57 0.014 . 1 . . . . 131 ILE HD1 . 19930 1 222 . 1 1 138 138 ILE HD12 H 1 0.57 0.014 . 1 . . . . 131 ILE HD1 . 19930 1 223 . 1 1 138 138 ILE HD13 H 1 0.57 0.014 . 1 . . . . 131 ILE HD1 . 19930 1 224 . 1 1 138 138 ILE CD1 C 13 8.381 0.045 . 1 . . . . 131 ILE CD1 . 19930 1 225 . 1 1 141 141 ILE HD11 H 1 0.636 0.014 . 1 . . . . 134 ILE HD1 . 19930 1 226 . 1 1 141 141 ILE HD12 H 1 0.636 0.014 . 1 . . . . 134 ILE HD1 . 19930 1 227 . 1 1 141 141 ILE HD13 H 1 0.636 0.014 . 1 . . . . 134 ILE HD1 . 19930 1 228 . 1 1 141 141 ILE CD1 C 13 14.398 0.045 . 1 . . . . 134 ILE CD1 . 19930 1 229 . 1 1 142 142 LEU HD11 H 1 0.658 0.014 . 2 . . . . 135 LEU HD1 . 19930 1 230 . 1 1 142 142 LEU HD12 H 1 0.658 0.014 . 2 . . . . 135 LEU HD1 . 19930 1 231 . 1 1 142 142 LEU HD13 H 1 0.658 0.014 . 2 . . . . 135 LEU HD1 . 19930 1 232 . 1 1 142 142 LEU HD21 H 1 0.754 0.014 . 2 . . . . 135 LEU HD2 . 19930 1 233 . 1 1 142 142 LEU HD22 H 1 0.754 0.014 . 2 . . . . 135 LEU HD2 . 19930 1 234 . 1 1 142 142 LEU HD23 H 1 0.754 0.014 . 2 . . . . 135 LEU HD2 . 19930 1 235 . 1 1 142 142 LEU CD1 C 13 28.692 0.045 . 1 . . . . 135 LEU CD1 . 19930 1 236 . 1 1 142 142 LEU CD2 C 13 22.702 0.045 . 1 . . . . 135 LEU CD2 . 19930 1 237 . 1 1 145 145 LEU HD11 H 1 0.627 0.014 . 2 . . . . 138 LEU HD1 . 19930 1 238 . 1 1 145 145 LEU HD12 H 1 0.627 0.014 . 2 . . . . 138 LEU HD1 . 19930 1 239 . 1 1 145 145 LEU HD13 H 1 0.627 0.014 . 2 . . . . 138 LEU HD1 . 19930 1 240 . 1 1 145 145 LEU HD21 H 1 0.65 0.014 . 2 . . . . 138 LEU HD2 . 19930 1 241 . 1 1 145 145 LEU HD22 H 1 0.65 0.014 . 2 . . . . 138 LEU HD2 . 19930 1 242 . 1 1 145 145 LEU HD23 H 1 0.65 0.014 . 2 . . . . 138 LEU HD2 . 19930 1 243 . 1 1 145 145 LEU CD1 C 13 26.827 0.045 . 1 . . . . 138 LEU CD1 . 19930 1 244 . 1 1 145 145 LEU CD2 C 13 21.818 0.045 . 1 . . . . 138 LEU CD2 . 19930 1 245 . 1 1 148 148 ILE HD11 H 1 0.749 0.014 . 1 . . . . 141 ILE HD1 . 19930 1 246 . 1 1 148 148 ILE HD12 H 1 0.749 0.014 . 1 . . . . 141 ILE HD1 . 19930 1 247 . 1 1 148 148 ILE HD13 H 1 0.749 0.014 . 1 . . . . 141 ILE HD1 . 19930 1 248 . 1 1 148 148 ILE CD1 C 13 14.357 0.045 . 1 . . . . 141 ILE CD1 . 19930 1 249 . 1 1 153 153 ILE HD11 H 1 0.49 0.014 . 1 . . . . 146 ILE HD1 . 19930 1 250 . 1 1 153 153 ILE HD12 H 1 0.49 0.014 . 1 . . . . 146 ILE HD1 . 19930 1 251 . 1 1 153 153 ILE HD13 H 1 0.49 0.014 . 1 . . . . 146 ILE HD1 . 19930 1 252 . 1 1 153 153 ILE CD1 C 13 12.811 0.045 . 1 . . . . 146 ILE CD1 . 19930 1 253 . 1 1 154 154 ILE HD11 H 1 0.842 0.014 . 1 . . . . 147 ILE HD1 . 19930 1 254 . 1 1 154 154 ILE HD12 H 1 0.842 0.014 . 1 . . . . 147 ILE HD1 . 19930 1 255 . 1 1 154 154 ILE HD13 H 1 0.842 0.014 . 1 . . . . 147 ILE HD1 . 19930 1 256 . 1 1 154 154 ILE CD1 C 13 13.268 0.045 . 1 . . . . 147 ILE CD1 . 19930 1 257 . 1 1 158 158 LEU HD11 H 1 0.551 0.014 . 2 . . . . 151 LEU HD1 . 19930 1 258 . 1 1 158 158 LEU HD12 H 1 0.551 0.014 . 2 . . . . 151 LEU HD1 . 19930 1 259 . 1 1 158 158 LEU HD13 H 1 0.551 0.014 . 2 . . . . 151 LEU HD1 . 19930 1 260 . 1 1 158 158 LEU HD21 H 1 0.422 0.014 . 2 . . . . 151 LEU HD2 . 19930 1 261 . 1 1 158 158 LEU HD22 H 1 0.422 0.014 . 2 . . . . 151 LEU HD2 . 19930 1 262 . 1 1 158 158 LEU HD23 H 1 0.422 0.014 . 2 . . . . 151 LEU HD2 . 19930 1 263 . 1 1 158 158 LEU CD1 C 13 25.122 0.045 . 1 . . . . 151 LEU CD1 . 19930 1 264 . 1 1 158 158 LEU CD2 C 13 25.422 0.045 . 1 . . . . 151 LEU CD2 . 19930 1 265 . 1 1 163 163 LEU HD11 H 1 0.668 0.014 . 2 . . . . 156 LEU HD1 . 19930 1 266 . 1 1 163 163 LEU HD12 H 1 0.668 0.014 . 2 . . . . 156 LEU HD1 . 19930 1 267 . 1 1 163 163 LEU HD13 H 1 0.668 0.014 . 2 . . . . 156 LEU HD1 . 19930 1 268 . 1 1 163 163 LEU HD21 H 1 0.797 0.014 . 2 . . . . 156 LEU HD2 . 19930 1 269 . 1 1 163 163 LEU HD22 H 1 0.797 0.014 . 2 . . . . 156 LEU HD2 . 19930 1 270 . 1 1 163 163 LEU HD23 H 1 0.797 0.014 . 2 . . . . 156 LEU HD2 . 19930 1 271 . 1 1 163 163 LEU CD1 C 13 27.92 0.045 . 1 . . . . 156 LEU CD1 . 19930 1 272 . 1 1 163 163 LEU CD2 C 13 26.034 0.045 . 1 . . . . 156 LEU CD2 . 19930 1 273 . 1 1 165 165 VAL HG11 H 1 0.815 0.014 . 2 . . . . 158 VAL HG1 . 19930 1 274 . 1 1 165 165 VAL HG12 H 1 0.815 0.014 . 2 . . . . 158 VAL HG1 . 19930 1 275 . 1 1 165 165 VAL HG13 H 1 0.815 0.014 . 2 . . . . 158 VAL HG1 . 19930 1 276 . 1 1 165 165 VAL HG21 H 1 0.659 0.014 . 2 . . . . 158 VAL HG2 . 19930 1 277 . 1 1 165 165 VAL HG22 H 1 0.659 0.014 . 2 . . . . 158 VAL HG2 . 19930 1 278 . 1 1 165 165 VAL HG23 H 1 0.659 0.014 . 2 . . . . 158 VAL HG2 . 19930 1 279 . 1 1 165 165 VAL CG1 C 13 22.111 0.045 . 1 . . . . 158 VAL CG1 . 19930 1 280 . 1 1 165 165 VAL CG2 C 13 20.621 0.045 . 1 . . . . 158 VAL CG2 . 19930 1 281 . 1 1 171 171 LEU HD11 H 1 0.707 0.014 . 2 . . . . 164 LEU HD1 . 19930 1 282 . 1 1 171 171 LEU HD12 H 1 0.707 0.014 . 2 . . . . 164 LEU HD1 . 19930 1 283 . 1 1 171 171 LEU HD13 H 1 0.707 0.014 . 2 . . . . 164 LEU HD1 . 19930 1 284 . 1 1 171 171 LEU HD21 H 1 0.505 0.014 . 2 . . . . 164 LEU HD2 . 19930 1 285 . 1 1 171 171 LEU HD22 H 1 0.505 0.014 . 2 . . . . 164 LEU HD2 . 19930 1 286 . 1 1 171 171 LEU HD23 H 1 0.505 0.014 . 2 . . . . 164 LEU HD2 . 19930 1 287 . 1 1 171 171 LEU CD1 C 13 27.05 0.045 . 1 . . . . 164 LEU CD1 . 19930 1 288 . 1 1 171 171 LEU CD2 C 13 24.291 0.045 . 1 . . . . 164 LEU CD2 . 19930 1 289 . 1 1 173 173 ILE HD11 H 1 0.812 0.014 . 1 . . . . 166 ILE HD1 . 19930 1 290 . 1 1 173 173 ILE HD12 H 1 0.812 0.014 . 1 . . . . 166 ILE HD1 . 19930 1 291 . 1 1 173 173 ILE HD13 H 1 0.812 0.014 . 1 . . . . 166 ILE HD1 . 19930 1 292 . 1 1 173 173 ILE CD1 C 13 14.026 0.045 . 1 . . . . 166 ILE CD1 . 19930 1 293 . 1 1 174 174 LEU HD11 H 1 0.87 0.014 . 2 . . . . 167 LEU HD1 . 19930 1 294 . 1 1 174 174 LEU HD12 H 1 0.87 0.014 . 2 . . . . 167 LEU HD1 . 19930 1 295 . 1 1 174 174 LEU HD13 H 1 0.87 0.014 . 2 . . . . 167 LEU HD1 . 19930 1 296 . 1 1 174 174 LEU HD21 H 1 0.829 0.014 . 2 . . . . 167 LEU HD2 . 19930 1 297 . 1 1 174 174 LEU HD22 H 1 0.829 0.014 . 2 . . . . 167 LEU HD2 . 19930 1 298 . 1 1 174 174 LEU HD23 H 1 0.829 0.014 . 2 . . . . 167 LEU HD2 . 19930 1 299 . 1 1 174 174 LEU CD1 C 13 25.522 0.045 . 1 . . . . 167 LEU CD1 . 19930 1 300 . 1 1 174 174 LEU CD2 C 13 24.18 0.045 . 1 . . . . 167 LEU CD2 . 19930 1 301 . 1 1 178 178 LEU HD11 H 1 0.693 0.014 . 2 . . . . 171 LEU HD1 . 19930 1 302 . 1 1 178 178 LEU HD12 H 1 0.693 0.014 . 2 . . . . 171 LEU HD1 . 19930 1 303 . 1 1 178 178 LEU HD13 H 1 0.693 0.014 . 2 . . . . 171 LEU HD1 . 19930 1 304 . 1 1 178 178 LEU HD21 H 1 0.622 0.014 . 2 . . . . 171 LEU HD2 . 19930 1 305 . 1 1 178 178 LEU HD22 H 1 0.622 0.014 . 2 . . . . 171 LEU HD2 . 19930 1 306 . 1 1 178 178 LEU HD23 H 1 0.622 0.014 . 2 . . . . 171 LEU HD2 . 19930 1 307 . 1 1 178 178 LEU CD1 C 13 25.11 0.045 . 1 . . . . 171 LEU CD1 . 19930 1 308 . 1 1 178 178 LEU CD2 C 13 22.663 0.045 . 1 . . . . 171 LEU CD2 . 19930 1 309 . 1 1 186 186 MET HE1 H 1 1.994 0.014 . 1 . . . . 179 MET HE . 19930 1 310 . 1 1 186 186 MET HE2 H 1 1.994 0.014 . 1 . . . . 179 MET HE . 19930 1 311 . 1 1 186 186 MET HE3 H 1 1.994 0.014 . 1 . . . . 179 MET HE . 19930 1 312 . 1 1 186 186 MET CE C 13 16.994 0.045 . 1 . . . . 179 MET CE . 19930 1 313 . 1 1 190 190 VAL HG11 H 1 0.827 0.014 . 2 . . . . 183 VAL HG1 . 19930 1 314 . 1 1 190 190 VAL HG12 H 1 0.827 0.014 . 2 . . . . 183 VAL HG1 . 19930 1 315 . 1 1 190 190 VAL HG13 H 1 0.827 0.014 . 2 . . . . 183 VAL HG1 . 19930 1 316 . 1 1 190 190 VAL HG21 H 1 0.854 0.014 . 2 . . . . 183 VAL HG2 . 19930 1 317 . 1 1 190 190 VAL HG22 H 1 0.854 0.014 . 2 . . . . 183 VAL HG2 . 19930 1 318 . 1 1 190 190 VAL HG23 H 1 0.854 0.014 . 2 . . . . 183 VAL HG2 . 19930 1 319 . 1 1 190 190 VAL CG1 C 13 20.98 0.045 . 1 . . . . 183 VAL CG1 . 19930 1 320 . 1 1 190 190 VAL CG2 C 13 20.378 0.045 . 1 . . . . 183 VAL CG2 . 19930 1 321 . 1 1 200 200 ILE HD11 H 1 0.481 0.014 . 1 . . . . 193 ILE HD1 . 19930 1 322 . 1 1 200 200 ILE HD12 H 1 0.481 0.014 . 1 . . . . 193 ILE HD1 . 19930 1 323 . 1 1 200 200 ILE HD13 H 1 0.481 0.014 . 1 . . . . 193 ILE HD1 . 19930 1 324 . 1 1 200 200 ILE CD1 C 13 11.478 0.045 . 1 . . . . 193 ILE CD1 . 19930 1 325 . 1 1 201 201 MET HE1 H 1 1.788 0.014 . 1 . . . . 194 MET HE . 19930 1 326 . 1 1 201 201 MET HE2 H 1 1.788 0.014 . 1 . . . . 194 MET HE . 19930 1 327 . 1 1 201 201 MET HE3 H 1 1.788 0.014 . 1 . . . . 194 MET HE . 19930 1 328 . 1 1 201 201 MET CE C 13 16.502 0.045 . 1 . . . . 194 MET CE . 19930 1 329 . 1 1 202 202 LEU HD11 H 1 0.845 0.014 . 2 . . . . 195 LEU HD1 . 19930 1 330 . 1 1 202 202 LEU HD12 H 1 0.845 0.014 . 2 . . . . 195 LEU HD1 . 19930 1 331 . 1 1 202 202 LEU HD13 H 1 0.845 0.014 . 2 . . . . 195 LEU HD1 . 19930 1 332 . 1 1 202 202 LEU HD21 H 1 0.957 0.014 . 2 . . . . 195 LEU HD2 . 19930 1 333 . 1 1 202 202 LEU HD22 H 1 0.957 0.014 . 2 . . . . 195 LEU HD2 . 19930 1 334 . 1 1 202 202 LEU HD23 H 1 0.957 0.014 . 2 . . . . 195 LEU HD2 . 19930 1 335 . 1 1 202 202 LEU CD1 C 13 22.839 0.045 . 1 . . . . 195 LEU CD1 . 19930 1 336 . 1 1 202 202 LEU CD2 C 13 24.863 0.045 . 1 . . . . 195 LEU CD2 . 19930 1 337 . 1 1 205 205 MET HE1 H 1 2.011 0.014 . 1 . . . . 198 MET HE . 19930 1 338 . 1 1 205 205 MET HE2 H 1 2.011 0.014 . 1 . . . . 198 MET HE . 19930 1 339 . 1 1 205 205 MET HE3 H 1 2.011 0.014 . 1 . . . . 198 MET HE . 19930 1 340 . 1 1 205 205 MET CE C 13 17.078 0.045 . 1 . . . . 198 MET CE . 19930 1 341 . 1 1 211 211 VAL HG11 H 1 1.298 0.014 . 2 . . . . 204 VAL HG1 . 19930 1 342 . 1 1 211 211 VAL HG12 H 1 1.298 0.014 . 2 . . . . 204 VAL HG1 . 19930 1 343 . 1 1 211 211 VAL HG13 H 1 1.298 0.014 . 2 . . . . 204 VAL HG1 . 19930 1 344 . 1 1 211 211 VAL HG21 H 1 1.2 0.014 . 2 . . . . 204 VAL HG2 . 19930 1 345 . 1 1 211 211 VAL HG22 H 1 1.2 0.014 . 2 . . . . 204 VAL HG2 . 19930 1 346 . 1 1 211 211 VAL HG23 H 1 1.2 0.014 . 2 . . . . 204 VAL HG2 . 19930 1 347 . 1 1 211 211 VAL CG1 C 13 22.515 0.045 . 1 . . . . 204 VAL CG1 . 19930 1 348 . 1 1 211 211 VAL CG2 C 13 19.797 0.045 . 1 . . . . 204 VAL CG2 . 19930 1 349 . 1 1 213 213 ILE HD11 H 1 0.628 0.014 . 1 . . . . 206 ILE HD1 . 19930 1 350 . 1 1 213 213 ILE HD12 H 1 0.628 0.014 . 1 . . . . 206 ILE HD1 . 19930 1 351 . 1 1 213 213 ILE HD13 H 1 0.628 0.014 . 1 . . . . 206 ILE HD1 . 19930 1 352 . 1 1 213 213 ILE CD1 C 13 8.09 0.045 . 1 . . . . 206 ILE CD1 . 19930 1 353 . 1 1 216 216 VAL HG11 H 1 0.861 0.014 . 2 . . . . 209 VAL HG1 . 19930 1 354 . 1 1 216 216 VAL HG12 H 1 0.861 0.014 . 2 . . . . 209 VAL HG1 . 19930 1 355 . 1 1 216 216 VAL HG13 H 1 0.861 0.014 . 2 . . . . 209 VAL HG1 . 19930 1 356 . 1 1 216 216 VAL HG21 H 1 1.009 0.014 . 2 . . . . 209 VAL HG2 . 19930 1 357 . 1 1 216 216 VAL HG22 H 1 1.009 0.014 . 2 . . . . 209 VAL HG2 . 19930 1 358 . 1 1 216 216 VAL HG23 H 1 1.009 0.014 . 2 . . . . 209 VAL HG2 . 19930 1 359 . 1 1 216 216 VAL CG1 C 13 22.859 0.045 . 1 . . . . 209 VAL CG1 . 19930 1 360 . 1 1 216 216 VAL CG2 C 13 24.904 0.045 . 1 . . . . 209 VAL CG2 . 19930 1 361 . 1 1 219 219 ILE HD11 H 1 0.302 0.014 . 1 . . . . 212 ILE HD1 . 19930 1 362 . 1 1 219 219 ILE HD12 H 1 0.302 0.014 . 1 . . . . 212 ILE HD1 . 19930 1 363 . 1 1 219 219 ILE HD13 H 1 0.302 0.014 . 1 . . . . 212 ILE HD1 . 19930 1 364 . 1 1 219 219 ILE CD1 C 13 12.962 0.045 . 1 . . . . 212 ILE CD1 . 19930 1 365 . 1 1 220 220 MET HE1 H 1 1.728 0.014 . 1 . . . . 213 MET HE . 19930 1 366 . 1 1 220 220 MET HE2 H 1 1.728 0.014 . 1 . . . . 213 MET HE . 19930 1 367 . 1 1 220 220 MET HE3 H 1 1.728 0.014 . 1 . . . . 213 MET HE . 19930 1 368 . 1 1 220 220 MET CE C 13 19.947 0.045 . 1 . . . . 213 MET CE . 19930 1 369 . 1 1 223 223 LEU HD11 H 1 0.836 0.014 . 2 . . . . 216 LEU HD1 . 19930 1 370 . 1 1 223 223 LEU HD12 H 1 0.836 0.014 . 2 . . . . 216 LEU HD1 . 19930 1 371 . 1 1 223 223 LEU HD13 H 1 0.836 0.014 . 2 . . . . 216 LEU HD1 . 19930 1 372 . 1 1 223 223 LEU HD21 H 1 0.745 0.014 . 2 . . . . 216 LEU HD2 . 19930 1 373 . 1 1 223 223 LEU HD22 H 1 0.745 0.014 . 2 . . . . 216 LEU HD2 . 19930 1 374 . 1 1 223 223 LEU HD23 H 1 0.745 0.014 . 2 . . . . 216 LEU HD2 . 19930 1 375 . 1 1 223 223 LEU CD1 C 13 26.267 0.045 . 1 . . . . 216 LEU CD1 . 19930 1 376 . 1 1 223 223 LEU CD2 C 13 22.143 0.045 . 1 . . . . 216 LEU CD2 . 19930 1 377 . 1 1 224 224 LEU HD11 H 1 0.541 0.014 . 2 . . . . 217 LEU HD1 . 19930 1 378 . 1 1 224 224 LEU HD12 H 1 0.541 0.014 . 2 . . . . 217 LEU HD1 . 19930 1 379 . 1 1 224 224 LEU HD13 H 1 0.541 0.014 . 2 . . . . 217 LEU HD1 . 19930 1 380 . 1 1 224 224 LEU HD21 H 1 0.966 0.014 . 2 . . . . 217 LEU HD2 . 19930 1 381 . 1 1 224 224 LEU HD22 H 1 0.966 0.014 . 2 . . . . 217 LEU HD2 . 19930 1 382 . 1 1 224 224 LEU HD23 H 1 0.966 0.014 . 2 . . . . 217 LEU HD2 . 19930 1 383 . 1 1 224 224 LEU CD1 C 13 26.342 0.045 . 1 . . . . 217 LEU CD1 . 19930 1 384 . 1 1 224 224 LEU CD2 C 13 22.696 0.045 . 1 . . . . 217 LEU CD2 . 19930 1 385 . 1 1 229 229 LEU HD11 H 1 0.46 0.014 . 2 . . . . 222 LEU HD1 . 19930 1 386 . 1 1 229 229 LEU HD12 H 1 0.46 0.014 . 2 . . . . 222 LEU HD1 . 19930 1 387 . 1 1 229 229 LEU HD13 H 1 0.46 0.014 . 2 . . . . 222 LEU HD1 . 19930 1 388 . 1 1 229 229 LEU HD21 H 1 0.259 0.014 . 2 . . . . 222 LEU HD2 . 19930 1 389 . 1 1 229 229 LEU HD22 H 1 0.259 0.014 . 2 . . . . 222 LEU HD2 . 19930 1 390 . 1 1 229 229 LEU HD23 H 1 0.259 0.014 . 2 . . . . 222 LEU HD2 . 19930 1 391 . 1 1 229 229 LEU CD1 C 13 21.708 0.045 . 1 . . . . 222 LEU CD1 . 19930 1 392 . 1 1 229 229 LEU CD2 C 13 28.38 0.045 . 1 . . . . 222 LEU CD2 . 19930 1 393 . 1 1 236 236 ILE HD11 H 1 0.546 0.014 . 1 . . . . 229 ILE HD1 . 19930 1 394 . 1 1 236 236 ILE HD12 H 1 0.546 0.014 . 1 . . . . 229 ILE HD1 . 19930 1 395 . 1 1 236 236 ILE HD13 H 1 0.546 0.014 . 1 . . . . 229 ILE HD1 . 19930 1 396 . 1 1 236 236 ILE CD1 C 13 10.376 0.045 . 1 . . . . 229 ILE CD1 . 19930 1 397 . 1 1 239 239 LEU HD11 H 1 0.515 0.014 . 2 . . . . 232 LEU HD1 . 19930 1 398 . 1 1 239 239 LEU HD12 H 1 0.515 0.014 . 2 . . . . 232 LEU HD1 . 19930 1 399 . 1 1 239 239 LEU HD13 H 1 0.515 0.014 . 2 . . . . 232 LEU HD1 . 19930 1 400 . 1 1 239 239 LEU HD21 H 1 0.769 0.014 . 2 . . . . 232 LEU HD2 . 19930 1 401 . 1 1 239 239 LEU HD22 H 1 0.769 0.014 . 2 . . . . 232 LEU HD2 . 19930 1 402 . 1 1 239 239 LEU HD23 H 1 0.769 0.014 . 2 . . . . 232 LEU HD2 . 19930 1 403 . 1 1 239 239 LEU CD1 C 13 25.537 0.045 . 1 . . . . 232 LEU CD1 . 19930 1 404 . 1 1 239 239 LEU CD2 C 13 22.731 0.045 . 1 . . . . 232 LEU CD2 . 19930 1 405 . 1 1 242 242 ILE HD11 H 1 0.613 0.014 . 1 . . . . 235 ILE HD1 . 19930 1 406 . 1 1 242 242 ILE HD12 H 1 0.613 0.014 . 1 . . . . 235 ILE HD1 . 19930 1 407 . 1 1 242 242 ILE HD13 H 1 0.613 0.014 . 1 . . . . 235 ILE HD1 . 19930 1 408 . 1 1 242 242 ILE CD1 C 13 13.822 0.045 . 1 . . . . 235 ILE CD1 . 19930 1 409 . 1 1 243 243 LEU HD11 H 1 0.86 0.014 . 2 . . . . 236 LEU HD1 . 19930 1 410 . 1 1 243 243 LEU HD12 H 1 0.86 0.014 . 2 . . . . 236 LEU HD1 . 19930 1 411 . 1 1 243 243 LEU HD13 H 1 0.86 0.014 . 2 . . . . 236 LEU HD1 . 19930 1 412 . 1 1 243 243 LEU HD21 H 1 0.874 0.014 . 2 . . . . 236 LEU HD2 . 19930 1 413 . 1 1 243 243 LEU HD22 H 1 0.874 0.014 . 2 . . . . 236 LEU HD2 . 19930 1 414 . 1 1 243 243 LEU HD23 H 1 0.874 0.014 . 2 . . . . 236 LEU HD2 . 19930 1 415 . 1 1 243 243 LEU CD1 C 13 26.319 0.045 . 1 . . . . 236 LEU CD1 . 19930 1 416 . 1 1 243 243 LEU CD2 C 13 22.877 0.045 . 1 . . . . 236 LEU CD2 . 19930 1 417 . 1 1 245 245 LEU HD11 H 1 0.632 0.014 . 2 . . . . 238 LEU HD1 . 19930 1 418 . 1 1 245 245 LEU HD12 H 1 0.632 0.014 . 2 . . . . 238 LEU HD1 . 19930 1 419 . 1 1 245 245 LEU HD13 H 1 0.632 0.014 . 2 . . . . 238 LEU HD1 . 19930 1 420 . 1 1 245 245 LEU HD21 H 1 0.768 0.014 . 2 . . . . 238 LEU HD2 . 19930 1 421 . 1 1 245 245 LEU HD22 H 1 0.768 0.014 . 2 . . . . 238 LEU HD2 . 19930 1 422 . 1 1 245 245 LEU HD23 H 1 0.768 0.014 . 2 . . . . 238 LEU HD2 . 19930 1 423 . 1 1 245 245 LEU CD1 C 13 23.86 0.045 . 1 . . . . 238 LEU CD1 . 19930 1 424 . 1 1 245 245 LEU CD2 C 13 26.472 0.045 . 1 . . . . 238 LEU CD2 . 19930 1 425 . 1 1 246 246 VAL HG11 H 1 1.449 0.014 . 2 . . . . 239 VAL HG1 . 19930 1 426 . 1 1 246 246 VAL HG12 H 1 1.449 0.014 . 2 . . . . 239 VAL HG1 . 19930 1 427 . 1 1 246 246 VAL HG13 H 1 1.449 0.014 . 2 . . . . 239 VAL HG1 . 19930 1 428 . 1 1 246 246 VAL HG21 H 1 1.307 0.014 . 2 . . . . 239 VAL HG2 . 19930 1 429 . 1 1 246 246 VAL HG22 H 1 1.307 0.014 . 2 . . . . 239 VAL HG2 . 19930 1 430 . 1 1 246 246 VAL HG23 H 1 1.307 0.014 . 2 . . . . 239 VAL HG2 . 19930 1 431 . 1 1 246 246 VAL CG1 C 13 22.308 0.045 . 1 . . . . 239 VAL CG1 . 19930 1 432 . 1 1 246 246 VAL CG2 C 13 19.584 0.045 . 1 . . . . 239 VAL CG2 . 19930 1 433 . 1 1 254 254 LEU HD11 H 1 0.915 0.014 . 2 . . . . 247 LEU HD1 . 19930 1 434 . 1 1 254 254 LEU HD12 H 1 0.915 0.014 . 2 . . . . 247 LEU HD1 . 19930 1 435 . 1 1 254 254 LEU HD13 H 1 0.915 0.014 . 2 . . . . 247 LEU HD1 . 19930 1 436 . 1 1 254 254 LEU HD21 H 1 0.848 0.014 . 2 . . . . 247 LEU HD2 . 19930 1 437 . 1 1 254 254 LEU HD22 H 1 0.848 0.014 . 2 . . . . 247 LEU HD2 . 19930 1 438 . 1 1 254 254 LEU HD23 H 1 0.848 0.014 . 2 . . . . 247 LEU HD2 . 19930 1 439 . 1 1 254 254 LEU CD1 C 13 23.625 0.045 . 1 . . . . 247 LEU CD1 . 19930 1 440 . 1 1 254 254 LEU CD2 C 13 25.487 0.045 . 1 . . . . 247 LEU CD2 . 19930 1 441 . 1 1 257 257 ILE HD11 H 1 0.057 0.014 . 1 . . . . 250 ILE HD1 . 19930 1 442 . 1 1 257 257 ILE HD12 H 1 0.057 0.014 . 1 . . . . 250 ILE HD1 . 19930 1 443 . 1 1 257 257 ILE HD13 H 1 0.057 0.014 . 1 . . . . 250 ILE HD1 . 19930 1 444 . 1 1 257 257 ILE CD1 C 13 12.684 0.045 . 1 . . . . 250 ILE CD1 . 19930 1 445 . 1 1 266 266 ILE HD11 H 1 0.805 0.014 . 1 . . . . 259 ILE HD1 . 19930 1 446 . 1 1 266 266 ILE HD12 H 1 0.805 0.014 . 1 . . . . 259 ILE HD1 . 19930 1 447 . 1 1 266 266 ILE HD13 H 1 0.805 0.014 . 1 . . . . 259 ILE HD1 . 19930 1 448 . 1 1 266 266 ILE CD1 C 13 12.942 0.045 . 1 . . . . 259 ILE CD1 . 19930 1 449 . 1 1 269 269 LEU HD11 H 1 0.804 0.014 . 2 . . . . 262 LEU HD1 . 19930 1 450 . 1 1 269 269 LEU HD12 H 1 0.804 0.014 . 2 . . . . 262 LEU HD1 . 19930 1 451 . 1 1 269 269 LEU HD13 H 1 0.804 0.014 . 2 . . . . 262 LEU HD1 . 19930 1 452 . 1 1 269 269 LEU HD21 H 1 0.751 0.014 . 2 . . . . 262 LEU HD2 . 19930 1 453 . 1 1 269 269 LEU HD22 H 1 0.751 0.014 . 2 . . . . 262 LEU HD2 . 19930 1 454 . 1 1 269 269 LEU HD23 H 1 0.751 0.014 . 2 . . . . 262 LEU HD2 . 19930 1 455 . 1 1 269 269 LEU CD1 C 13 24.857 0.045 . 1 . . . . 262 LEU CD1 . 19930 1 456 . 1 1 269 269 LEU CD2 C 13 23.658 0.045 . 1 . . . . 262 LEU CD2 . 19930 1 457 . 1 1 272 272 MET HE1 H 1 2.097 0.014 . 1 . . . . 265 MET HE . 19930 1 458 . 1 1 272 272 MET HE2 H 1 2.097 0.014 . 1 . . . . 265 MET HE . 19930 1 459 . 1 1 272 272 MET HE3 H 1 2.097 0.014 . 1 . . . . 265 MET HE . 19930 1 460 . 1 1 272 272 MET CE C 13 17.49 0.045 . 1 . . . . 265 MET CE . 19930 1 461 . 1 1 275 275 MET HE1 H 1 2.072 0.014 . 1 . . . . 268 MET HE . 19930 1 462 . 1 1 275 275 MET HE2 H 1 2.072 0.014 . 1 . . . . 268 MET HE . 19930 1 463 . 1 1 275 275 MET HE3 H 1 2.072 0.014 . 1 . . . . 268 MET HE . 19930 1 464 . 1 1 275 275 MET CE C 13 17.112 0.045 . 1 . . . . 268 MET CE . 19930 1 465 . 1 1 280 280 VAL HG11 H 1 -0.141 0.014 . 2 . . . . 273 VAL HG1 . 19930 1 466 . 1 1 280 280 VAL HG12 H 1 -0.141 0.014 . 2 . . . . 273 VAL HG1 . 19930 1 467 . 1 1 280 280 VAL HG13 H 1 -0.141 0.014 . 2 . . . . 273 VAL HG1 . 19930 1 468 . 1 1 280 280 VAL HG21 H 1 0.701 0.014 . 2 . . . . 273 VAL HG2 . 19930 1 469 . 1 1 280 280 VAL HG22 H 1 0.701 0.014 . 2 . . . . 273 VAL HG2 . 19930 1 470 . 1 1 280 280 VAL HG23 H 1 0.701 0.014 . 2 . . . . 273 VAL HG2 . 19930 1 471 . 1 1 280 280 VAL CG1 C 13 19.499 0.045 . 1 . . . . 273 VAL CG1 . 19930 1 472 . 1 1 280 280 VAL CG2 C 13 21.257 0.045 . 1 . . . . 273 VAL CG2 . 19930 1 473 . 1 1 282 282 ILE HD11 H 1 0.878 0.014 . 1 . . . . 275 ILE HD1 . 19930 1 474 . 1 1 282 282 ILE HD12 H 1 0.878 0.014 . 1 . . . . 275 ILE HD1 . 19930 1 475 . 1 1 282 282 ILE HD13 H 1 0.878 0.014 . 1 . . . . 275 ILE HD1 . 19930 1 476 . 1 1 282 282 ILE CD1 C 13 12.313 0.045 . 1 . . . . 275 ILE CD1 . 19930 1 477 . 1 1 287 287 LEU HD11 H 1 0.983 0.014 . 2 . . . . 280 LEU HD1 . 19930 1 478 . 1 1 287 287 LEU HD12 H 1 0.983 0.014 . 2 . . . . 280 LEU HD1 . 19930 1 479 . 1 1 287 287 LEU HD13 H 1 0.983 0.014 . 2 . . . . 280 LEU HD1 . 19930 1 480 . 1 1 287 287 LEU HD21 H 1 0.921 0.014 . 2 . . . . 280 LEU HD2 . 19930 1 481 . 1 1 287 287 LEU HD22 H 1 0.921 0.014 . 2 . . . . 280 LEU HD2 . 19930 1 482 . 1 1 287 287 LEU HD23 H 1 0.921 0.014 . 2 . . . . 280 LEU HD2 . 19930 1 483 . 1 1 287 287 LEU CD1 C 13 25.473 0.045 . 1 . . . . 280 LEU CD1 . 19930 1 484 . 1 1 287 287 LEU CD2 C 13 22.599 0.045 . 1 . . . . 280 LEU CD2 . 19930 1 485 . 1 1 289 289 VAL HG11 H 1 1.021 0.014 . 2 . . . . 282 VAL HG1 . 19930 1 486 . 1 1 289 289 VAL HG12 H 1 1.021 0.014 . 2 . . . . 282 VAL HG1 . 19930 1 487 . 1 1 289 289 VAL HG13 H 1 1.021 0.014 . 2 . . . . 282 VAL HG1 . 19930 1 488 . 1 1 289 289 VAL HG21 H 1 0.994 0.014 . 2 . . . . 282 VAL HG2 . 19930 1 489 . 1 1 289 289 VAL HG22 H 1 0.994 0.014 . 2 . . . . 282 VAL HG2 . 19930 1 490 . 1 1 289 289 VAL HG23 H 1 0.994 0.014 . 2 . . . . 282 VAL HG2 . 19930 1 491 . 1 1 289 289 VAL CG1 C 13 22.688 0.045 . 1 . . . . 282 VAL CG1 . 19930 1 492 . 1 1 289 289 VAL CG2 C 13 23.64 0.045 . 1 . . . . 282 VAL CG2 . 19930 1 493 . 1 1 291 291 LEU HD11 H 1 0.705 0.014 . 2 . . . . 284 LEU HD1 . 19930 1 494 . 1 1 291 291 LEU HD12 H 1 0.705 0.014 . 2 . . . . 284 LEU HD1 . 19930 1 495 . 1 1 291 291 LEU HD13 H 1 0.705 0.014 . 2 . . . . 284 LEU HD1 . 19930 1 496 . 1 1 291 291 LEU HD21 H 1 0.708 0.014 . 2 . . . . 284 LEU HD2 . 19930 1 497 . 1 1 291 291 LEU HD22 H 1 0.708 0.014 . 2 . . . . 284 LEU HD2 . 19930 1 498 . 1 1 291 291 LEU HD23 H 1 0.708 0.014 . 2 . . . . 284 LEU HD2 . 19930 1 499 . 1 1 291 291 LEU CD1 C 13 22.768 0.045 . 1 . . . . 284 LEU CD1 . 19930 1 500 . 1 1 291 291 LEU CD2 C 13 28.009 0.045 . 1 . . . . 284 LEU CD2 . 19930 1 501 . 1 1 292 292 LEU HD11 H 1 -0.058 0.014 . 2 . . . . 285 LEU HD1 . 19930 1 502 . 1 1 292 292 LEU HD12 H 1 -0.058 0.014 . 2 . . . . 285 LEU HD1 . 19930 1 503 . 1 1 292 292 LEU HD13 H 1 -0.058 0.014 . 2 . . . . 285 LEU HD1 . 19930 1 504 . 1 1 292 292 LEU HD21 H 1 0.559 0.014 . 2 . . . . 285 LEU HD2 . 19930 1 505 . 1 1 292 292 LEU HD22 H 1 0.559 0.014 . 2 . . . . 285 LEU HD2 . 19930 1 506 . 1 1 292 292 LEU HD23 H 1 0.559 0.014 . 2 . . . . 285 LEU HD2 . 19930 1 507 . 1 1 292 292 LEU CD1 C 13 24.429 0.045 . 1 . . . . 285 LEU CD1 . 19930 1 508 . 1 1 292 292 LEU CD2 C 13 24.732 0.045 . 1 . . . . 285 LEU CD2 . 19930 1 509 . 1 1 295 295 MET HE1 H 1 1.939 0.014 . 1 . . . . 288 MET HE . 19930 1 510 . 1 1 295 295 MET HE2 H 1 1.939 0.014 . 1 . . . . 288 MET HE . 19930 1 511 . 1 1 295 295 MET HE3 H 1 1.939 0.014 . 1 . . . . 288 MET HE . 19930 1 512 . 1 1 295 295 MET CE C 13 18.654 0.045 . 1 . . . . 288 MET CE . 19930 1 513 . 1 1 296 296 LEU HD11 H 1 0.527 0.014 . 2 . . . . 289 LEU HD1 . 19930 1 514 . 1 1 296 296 LEU HD12 H 1 0.527 0.014 . 2 . . . . 289 LEU HD1 . 19930 1 515 . 1 1 296 296 LEU HD13 H 1 0.527 0.014 . 2 . . . . 289 LEU HD1 . 19930 1 516 . 1 1 296 296 LEU HD21 H 1 -0.242 0.014 . 2 . . . . 289 LEU HD2 . 19930 1 517 . 1 1 296 296 LEU HD22 H 1 -0.242 0.014 . 2 . . . . 289 LEU HD2 . 19930 1 518 . 1 1 296 296 LEU HD23 H 1 -0.242 0.014 . 2 . . . . 289 LEU HD2 . 19930 1 519 . 1 1 296 296 LEU CD1 C 13 26.529 0.045 . 1 . . . . 289 LEU CD1 . 19930 1 520 . 1 1 296 296 LEU CD2 C 13 21.884 0.045 . 1 . . . . 289 LEU CD2 . 19930 1 521 . 1 1 297 297 VAL HG11 H 1 1.097 0.014 . 2 . . . . 290 VAL HG1 . 19930 1 522 . 1 1 297 297 VAL HG12 H 1 1.097 0.014 . 2 . . . . 290 VAL HG1 . 19930 1 523 . 1 1 297 297 VAL HG13 H 1 1.097 0.014 . 2 . . . . 290 VAL HG1 . 19930 1 524 . 1 1 297 297 VAL HG21 H 1 0.934 0.014 . 2 . . . . 290 VAL HG2 . 19930 1 525 . 1 1 297 297 VAL HG22 H 1 0.934 0.014 . 2 . . . . 290 VAL HG2 . 19930 1 526 . 1 1 297 297 VAL HG23 H 1 0.934 0.014 . 2 . . . . 290 VAL HG2 . 19930 1 527 . 1 1 297 297 VAL CG1 C 13 21.903 0.045 . 1 . . . . 290 VAL CG1 . 19930 1 528 . 1 1 297 297 VAL CG2 C 13 20.77 0.045 . 1 . . . . 290 VAL CG2 . 19930 1 529 . 1 1 298 298 LEU HD11 H 1 0.864 0.014 . 2 . . . . 291 LEU HD1 . 19930 1 530 . 1 1 298 298 LEU HD12 H 1 0.864 0.014 . 2 . . . . 291 LEU HD1 . 19930 1 531 . 1 1 298 298 LEU HD13 H 1 0.864 0.014 . 2 . . . . 291 LEU HD1 . 19930 1 532 . 1 1 298 298 LEU HD21 H 1 0.813 0.014 . 2 . . . . 291 LEU HD2 . 19930 1 533 . 1 1 298 298 LEU HD22 H 1 0.813 0.014 . 2 . . . . 291 LEU HD2 . 19930 1 534 . 1 1 298 298 LEU HD23 H 1 0.813 0.014 . 2 . . . . 291 LEU HD2 . 19930 1 535 . 1 1 298 298 LEU CD1 C 13 24.552 0.045 . 1 . . . . 291 LEU CD1 . 19930 1 536 . 1 1 298 298 LEU CD2 C 13 24.002 0.045 . 1 . . . . 291 LEU CD2 . 19930 1 537 . 1 1 304 304 ILE HD11 H 1 0.821 0.014 . 1 . . . . 297 ILE HD1 . 19930 1 538 . 1 1 304 304 ILE HD12 H 1 0.821 0.014 . 1 . . . . 297 ILE HD1 . 19930 1 539 . 1 1 304 304 ILE HD13 H 1 0.821 0.014 . 1 . . . . 297 ILE HD1 . 19930 1 540 . 1 1 304 304 ILE CD1 C 13 13.846 0.045 . 1 . . . . 297 ILE CD1 . 19930 1 541 . 1 1 310 310 LEU HD11 H 1 0.722 0.014 . 2 . . . . 303 LEU HD1 . 19930 1 542 . 1 1 310 310 LEU HD12 H 1 0.722 0.014 . 2 . . . . 303 LEU HD1 . 19930 1 543 . 1 1 310 310 LEU HD13 H 1 0.722 0.014 . 2 . . . . 303 LEU HD1 . 19930 1 544 . 1 1 310 310 LEU HD21 H 1 0.442 0.014 . 2 . . . . 303 LEU HD2 . 19930 1 545 . 1 1 310 310 LEU HD22 H 1 0.442 0.014 . 2 . . . . 303 LEU HD2 . 19930 1 546 . 1 1 310 310 LEU HD23 H 1 0.442 0.014 . 2 . . . . 303 LEU HD2 . 19930 1 547 . 1 1 310 310 LEU CD1 C 13 26.804 0.045 . 1 . . . . 303 LEU CD1 . 19930 1 548 . 1 1 310 310 LEU CD2 C 13 25.352 0.045 . 1 . . . . 303 LEU CD2 . 19930 1 549 . 1 1 326 326 VAL HG11 H 1 1.099 0.014 . 2 . . . . 319 VAL HG1 . 19930 1 550 . 1 1 326 326 VAL HG12 H 1 1.099 0.014 . 2 . . . . 319 VAL HG1 . 19930 1 551 . 1 1 326 326 VAL HG13 H 1 1.099 0.014 . 2 . . . . 319 VAL HG1 . 19930 1 552 . 1 1 326 326 VAL HG21 H 1 0.949 0.014 . 2 . . . . 319 VAL HG2 . 19930 1 553 . 1 1 326 326 VAL HG22 H 1 0.949 0.014 . 2 . . . . 319 VAL HG2 . 19930 1 554 . 1 1 326 326 VAL HG23 H 1 0.949 0.014 . 2 . . . . 319 VAL HG2 . 19930 1 555 . 1 1 326 326 VAL CG1 C 13 22.517 0.045 . 1 . . . . 319 VAL CG1 . 19930 1 556 . 1 1 326 326 VAL CG2 C 13 17.401 0.045 . 1 . . . . 319 VAL CG2 . 19930 1 557 . 1 1 339 339 LEU HD11 H 1 -0.697 0.014 . 2 . . . . 332 LEU HD1 . 19930 1 558 . 1 1 339 339 LEU HD12 H 1 -0.697 0.014 . 2 . . . . 332 LEU HD1 . 19930 1 559 . 1 1 339 339 LEU HD13 H 1 -0.697 0.014 . 2 . . . . 332 LEU HD1 . 19930 1 560 . 1 1 339 339 LEU HD21 H 1 0.464 0.014 . 2 . . . . 332 LEU HD2 . 19930 1 561 . 1 1 339 339 LEU HD22 H 1 0.464 0.014 . 2 . . . . 332 LEU HD2 . 19930 1 562 . 1 1 339 339 LEU HD23 H 1 0.464 0.014 . 2 . . . . 332 LEU HD2 . 19930 1 563 . 1 1 339 339 LEU CD1 C 13 24.003 0.045 . 1 . . . . 332 LEU CD1 . 19930 1 564 . 1 1 339 339 LEU CD2 C 13 21.979 0.045 . 1 . . . . 332 LEU CD2 . 19930 1 565 . 1 1 340 340 LEU HD11 H 1 0.945 0.014 . 2 . . . . 333 LEU HD1 . 19930 1 566 . 1 1 340 340 LEU HD12 H 1 0.945 0.014 . 2 . . . . 333 LEU HD1 . 19930 1 567 . 1 1 340 340 LEU HD13 H 1 0.945 0.014 . 2 . . . . 333 LEU HD1 . 19930 1 568 . 1 1 340 340 LEU HD21 H 1 0.953 0.014 . 2 . . . . 333 LEU HD2 . 19930 1 569 . 1 1 340 340 LEU HD22 H 1 0.953 0.014 . 2 . . . . 333 LEU HD2 . 19930 1 570 . 1 1 340 340 LEU HD23 H 1 0.953 0.014 . 2 . . . . 333 LEU HD2 . 19930 1 571 . 1 1 340 340 LEU CD1 C 13 25.209 0.045 . 1 . . . . 333 LEU CD1 . 19930 1 572 . 1 1 340 340 LEU CD2 C 13 22.023 0.045 . 1 . . . . 333 LEU CD2 . 19930 1 573 . 1 1 341 341 ILE HD11 H 1 1.255 0.014 . 1 . . . . 334 ILE HD1 . 19930 1 574 . 1 1 341 341 ILE HD12 H 1 1.255 0.014 . 1 . . . . 334 ILE HD1 . 19930 1 575 . 1 1 341 341 ILE HD13 H 1 1.255 0.014 . 1 . . . . 334 ILE HD1 . 19930 1 576 . 1 1 341 341 ILE CD1 C 13 13.581 0.045 . 1 . . . . 334 ILE CD1 . 19930 1 577 . 1 1 347 347 LEU HD11 H 1 0.245 0.014 . 2 . . . . 340 LEU HD1 . 19930 1 578 . 1 1 347 347 LEU HD12 H 1 0.245 0.014 . 2 . . . . 340 LEU HD1 . 19930 1 579 . 1 1 347 347 LEU HD13 H 1 0.245 0.014 . 2 . . . . 340 LEU HD1 . 19930 1 580 . 1 1 347 347 LEU HD21 H 1 0.693 0.014 . 2 . . . . 340 LEU HD2 . 19930 1 581 . 1 1 347 347 LEU HD22 H 1 0.693 0.014 . 2 . . . . 340 LEU HD2 . 19930 1 582 . 1 1 347 347 LEU HD23 H 1 0.693 0.014 . 2 . . . . 340 LEU HD2 . 19930 1 583 . 1 1 347 347 LEU CD1 C 13 25.522 0.045 . 1 . . . . 340 LEU CD1 . 19930 1 584 . 1 1 347 347 LEU CD2 C 13 22.852 0.045 . 1 . . . . 340 LEU CD2 . 19930 1 585 . 1 1 352 352 VAL HG11 H 1 0.895 0.014 . 2 . . . . 345 VAL HG1 . 19930 1 586 . 1 1 352 352 VAL HG12 H 1 0.895 0.014 . 2 . . . . 345 VAL HG1 . 19930 1 587 . 1 1 352 352 VAL HG13 H 1 0.895 0.014 . 2 . . . . 345 VAL HG1 . 19930 1 588 . 1 1 352 352 VAL HG21 H 1 1.115 0.014 . 2 . . . . 345 VAL HG2 . 19930 1 589 . 1 1 352 352 VAL HG22 H 1 1.115 0.014 . 2 . . . . 345 VAL HG2 . 19930 1 590 . 1 1 352 352 VAL HG23 H 1 1.115 0.014 . 2 . . . . 345 VAL HG2 . 19930 1 591 . 1 1 352 352 VAL CG1 C 13 21.171 0.045 . 1 . . . . 345 VAL CG1 . 19930 1 592 . 1 1 352 352 VAL CG2 C 13 22.876 0.045 . 1 . . . . 345 VAL CG2 . 19930 1 593 . 1 1 353 353 ILE HD11 H 1 0.509 0.014 . 1 . . . . 346 ILE HD1 . 19930 1 594 . 1 1 353 353 ILE HD12 H 1 0.509 0.014 . 1 . . . . 346 ILE HD1 . 19930 1 595 . 1 1 353 353 ILE HD13 H 1 0.509 0.014 . 1 . . . . 346 ILE HD1 . 19930 1 596 . 1 1 353 353 ILE CD1 C 13 11.919 0.045 . 1 . . . . 346 ILE CD1 . 19930 1 597 . 1 1 356 356 VAL HG11 H 1 0.876 0.014 . 2 . . . . 349 VAL HG1 . 19930 1 598 . 1 1 356 356 VAL HG12 H 1 0.876 0.014 . 2 . . . . 349 VAL HG1 . 19930 1 599 . 1 1 356 356 VAL HG13 H 1 0.876 0.014 . 2 . . . . 349 VAL HG1 . 19930 1 600 . 1 1 356 356 VAL HG21 H 1 0.83 0.014 . 2 . . . . 349 VAL HG2 . 19930 1 601 . 1 1 356 356 VAL HG22 H 1 0.83 0.014 . 2 . . . . 349 VAL HG2 . 19930 1 602 . 1 1 356 356 VAL HG23 H 1 0.83 0.014 . 2 . . . . 349 VAL HG2 . 19930 1 603 . 1 1 356 356 VAL CG1 C 13 20.436 0.045 . 1 . . . . 349 VAL CG1 . 19930 1 604 . 1 1 356 356 VAL CG2 C 13 20.458 0.045 . 1 . . . . 349 VAL CG2 . 19930 1 605 . 1 1 360 360 LEU HD11 H 1 0.919 0.014 . 2 . . . . 353 LEU HD1 . 19930 1 606 . 1 1 360 360 LEU HD12 H 1 0.919 0.014 . 2 . . . . 353 LEU HD1 . 19930 1 607 . 1 1 360 360 LEU HD13 H 1 0.919 0.014 . 2 . . . . 353 LEU HD1 . 19930 1 608 . 1 1 360 360 LEU HD21 H 1 0.872 0.014 . 2 . . . . 353 LEU HD2 . 19930 1 609 . 1 1 360 360 LEU HD22 H 1 0.872 0.014 . 2 . . . . 353 LEU HD2 . 19930 1 610 . 1 1 360 360 LEU HD23 H 1 0.872 0.014 . 2 . . . . 353 LEU HD2 . 19930 1 611 . 1 1 360 360 LEU CD1 C 13 25.079 0.045 . 1 . . . . 353 LEU CD1 . 19930 1 612 . 1 1 360 360 LEU CD2 C 13 23.453 0.045 . 1 . . . . 353 LEU CD2 . 19930 1 613 . 1 1 365 365 MET HE1 H 1 2.11 0.014 . 1 . . . . 358 MET HE . 19930 1 614 . 1 1 365 365 MET HE2 H 1 2.11 0.014 . 1 . . . . 358 MET HE . 19930 1 615 . 1 1 365 365 MET HE3 H 1 2.11 0.014 . 1 . . . . 358 MET HE . 19930 1 616 . 1 1 365 365 MET CE C 13 17.041 0.045 . 1 . . . . 358 MET CE . 19930 1 stop_ save_