data_19937 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 19937 _Entry.Title ; Dual-phosphorylated human p38 alpha ILVM methyl resonance assignments in ADP and substrate-peptide-bound state ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2014-04-24 _Entry.Accession_date 2014-04-24 _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 . . . 19937 2 Koh Takeuchi . . . 19937 3 Hideo Takahashi . . . 19937 4 Ichio Shimada . . . 19937 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 19937 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 378 19937 '13C chemical shifts' 126 19937 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 2014-04-24 update BMRB 'update entry citation' 19937 1 . . 2014-08-05 2014-04-24 original author 'original release' 19937 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 19930 'non-phosphorylated (apo)' 19937 BMRB 19934 'Dual-phosphorylated human p38 alpha apo' 19937 BMRB 19935 'Dual-phosphorylated human p38 alpha ADP-bound' 19937 BMRB 19936 'Dual-phosphorylated human p38 alpha MK2 334/D peptide bound' 19937 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 19937 _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. . . 19937 1 2 Koh Takeuchi K. . . 19937 1 3 Hideo Takahashi H. . . 19937 1 4 Ichio Shimada I. . . 19937 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 19937 _Assembly.ID 1 _Assembly.Name 'Dual-phosphorylated human p38 alpha ADP and MK2 334/D peptide bound' _Assembly.BMRB_code . _Assembly.Number_of_components 3 _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 'dual-phosphorylated human p38 alpha (apo)' 1 $dual-phosphorylated_human_p38_alpha_(apo) A . yes native yes no . . . 19937 1 2 'MK2 334/D peptide' 2 $MK2_334-D_peptide A . no native no no . . . 19937 1 3 ADP 3 $entity_ADP A . no native no no . . . 19937 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_dual-phosphorylated_human_p38_alpha_(apo) _Entity.Sf_category entity _Entity.Sf_framecode dual-phosphorylated_human_p38_alpha_(apo) _Entity.Entry_ID 19937 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name dual-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 HTDDEMXGXVATRWYRAPEI 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 98.86 98.86 0.00e+00 . . . . 19937 1 2 no BMRB 17940 . p38alpha . . . . . 95.10 349 98.57 98.85 0.00e+00 . . . . 19937 1 3 no BMRB 19930 . Non-phosphorylated_human_p38_alpha_(apo) . . . . . 100.00 367 99.46 99.46 0.00e+00 . . . . 19937 1 4 no BMRB 19934 . Dual-phosphorylated_human_p38_alpha_(apo) . . . . . 100.00 367 100.00 100.00 0.00e+00 . . . . 19937 1 5 no BMRB 19935 . Dual-phosphorylated_human_p38_alpha . . . . . 100.00 367 100.00 100.00 0.00e+00 . . . . 19937 1 6 no BMRB 19936 . dual-phosphorylated_human_p38_alpha_(apo) . . . . . 100.00 367 100.00 100.00 0.00e+00 . . . . 19937 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 99.44 99.44 0.00e+00 . . . . 19937 1 8 no PDB 1IAN . "Human P38 Map Kinase Inhibitor Complex" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 9 no PDB 1KV1 . "P38 Map Kinase In Complex With Inhibitor 1" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 10 no PDB 1KV2 . "Human P38 Map Kinase In Complex With Birb 796" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 11 no PDB 1LEW . "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Nuclear Substrate Mef2a" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19937 1 12 no PDB 1LEZ . "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Activator Mkk3b" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19937 1 13 no PDB 1M7Q . "Crystal Structure Of P38 Map Kinase In Complex With A Dihydroquinazolinone Inhibitor" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 14 no PDB 1OUK . "The Structure Of P38 Alpha In Complex With A Pyridinylimidazole Inhibitor" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 15 no PDB 1OUY . "The Structure Of P38 Alpha In Complex With A Dihydropyrido- Pyrimidine Inhibitor" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 16 no PDB 1OVE . "The Structure Of P38 Alpha In Complex With A Dihydroquinolinone" . . . . . 99.18 366 98.08 98.08 0.00e+00 . . . . 19937 1 17 no PDB 1OZ1 . "P38 Mitogen-Activated Kinase In Complex With 4-Azaindole Inhibitor" . . . . . 100.54 372 98.37 98.64 0.00e+00 . . . . 19937 1 18 no PDB 1R39 . "The Structure Of P38alpha" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 19 no PDB 1R3C . "The Structure Of P38alpha C162s Mutant" . . . . . 99.18 366 98.08 98.08 0.00e+00 . . . . 19937 1 20 no PDB 1W7H . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 21 no PDB 1W82 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 22 no PDB 1W83 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 23 no PDB 1W84 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 24 no PDB 1WBN . "Fragment Based P38 Inhibitors" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 25 no PDB 1WBO . "Fragment Based P38 Inhibitors" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 26 no PDB 1WBS . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 27 no PDB 1WBT . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-based Lead Generation." . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 28 no PDB 1WBV . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 29 no PDB 1WBW . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 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 98.35 98.35 0.00e+00 . . . . 19937 1 31 no PDB 1YQJ . "Crystal Structure Of P38 Alpha In Complex With A Selective Pyridazine Inhibitor" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 32 no PDB 1YW2 . "Mutated Mus Musculus P38 Kinase (Mp38)" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19937 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 99.16 0.00e+00 . . . . 19937 1 34 no PDB 1ZYJ . "Human P38 Map Kinase In Complex With Inhibitor 1a" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 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 99.44 99.44 0.00e+00 . . . . 19937 1 36 no PDB 1ZZL . "Crystal Structure Of P38 With Triazolopyridine" . . . . . 95.64 351 99.43 99.43 0.00e+00 . . . . 19937 1 37 no PDB 2BAJ . "P38alpha Bound To Pyrazolourea" . . . . . 99.46 365 99.45 99.45 0.00e+00 . . . . 19937 1 38 no PDB 2BAK . "P38alpha Map Kinase Bound To Mpaq" . . . . . 99.46 365 99.45 99.45 0.00e+00 . . . . 19937 1 39 no PDB 2BAL . "P38alpha Map Kinase Bound To Pyrazoloamine" . . . . . 99.46 365 99.18 99.18 0.00e+00 . . . . 19937 1 40 no PDB 2BAQ . "P38alpha Bound To Ro3201195" . . . . . 99.46 365 98.90 99.18 0.00e+00 . . . . 19937 1 41 no PDB 2FSL . "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-A" . . . . . 100.00 367 98.91 98.91 0.00e+00 . . . . 19937 1 42 no PDB 2FSM . "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-B" . . . . . 100.00 367 98.91 98.91 0.00e+00 . . . . 19937 1 43 no PDB 2FSO . "Mitogen Activated Protein Kinase P38alpha (D176a) Activating Mutant" . . . . . 100.00 367 99.18 99.18 0.00e+00 . . . . 19937 1 44 no PDB 2FST . "Mitogen Activated Protein Kinase P38alpha (d176a+f327l) Activating Mutant" . . . . . 100.00 367 98.91 98.91 0.00e+00 . . . . 19937 1 45 no PDB 2GFS . "P38 Kinase Crystal Structure In Complex With Ro3201195" . . . . . 100.54 372 98.37 98.64 0.00e+00 . . . . 19937 1 46 no PDB 2GHL . "Mutant Mus Musculus P38 Kinase Domain In Complex With Inhibitor Pg-874743" . . . . . 94.82 348 98.85 98.85 0.00e+00 . . . . 19937 1 47 no PDB 2GHM . "Mutated Map Kinase P38 (Mus Musculus) In Complex With Inhbitor Pg-895449" . . . . . 94.82 348 98.85 98.85 0.00e+00 . . . . 19937 1 48 no PDB 2GTM . "Mutated Mouse P38 Map Kinase Domain In Complex With Inhibitor Pg-892579" . . . . . 94.82 348 98.85 98.85 0.00e+00 . . . . 19937 1 49 no PDB 2GTN . "Mutated Map Kinase P38 (mus Musculus) In Complex With Inhbitor Pg-951717" . . . . . 94.82 348 98.85 98.85 0.00e+00 . . . . 19937 1 50 no PDB 2I0H . "The Structure Of P38alpha In Complex With An Arylpyridazinone" . . . . . 99.18 366 98.08 98.08 0.00e+00 . . . . 19937 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 98.32 98.32 0.00e+00 . . . . 19937 1 52 no PDB 2NPQ . "A Novel Lipid Binding Site In The P38 Alpha Map Kinase" . . . . . 100.00 367 99.46 99.46 0.00e+00 . . . . 19937 1 53 no PDB 2OKR . "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 54 no PDB 2ONL . "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 55 no PDB 2OZA . "Structure Of P38alpha Complex" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19937 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 98.28 98.28 0.00e+00 . . . . 19937 1 57 no PDB 2QD9 . "P38 Alpha Map Kinase Inhibitor Based On Heterobicyclic Scaffolds" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 58 no PDB 2RG5 . "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11b" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 59 no PDB 2RG6 . "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11j" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 60 no PDB 2Y8O . "Crystal Structure Of Human P38alpha Complexed With A Mapk Docking Peptide" . . . . . 97.82 362 99.16 99.16 0.00e+00 . . . . 19937 1 61 no PDB 2YIS . "Triazolopyridine Inhibitors Of P38 Kinase." . . . . . 97.82 359 99.44 99.44 0.00e+00 . . . . 19937 1 62 no PDB 2YIW . "Triazolopyridine Inhibitors Of P38 Kinase" . . . . . 97.82 359 99.44 99.44 0.00e+00 . . . . 19937 1 63 no PDB 2YIX . "Triazolopyridine Inhibitors Of P38" . . . . . 95.64 351 99.43 99.43 0.00e+00 . . . . 19937 1 64 no PDB 2ZAZ . "Crystal Structure Of P38 In Complex With 4-Anilino Quinoline Inhibitor" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 65 no PDB 2ZB0 . "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 66 no PDB 2ZB1 . "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 67 no PDB 3BV2 . "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 30" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 68 no PDB 3BV3 . "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 2" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 69 no PDB 3BX5 . "P38 Alpha Map Kinase Complexed With Bms-640994" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 70 no PDB 3C5U . "P38 Alpha Map Kinase Complexed With A Benzothiazole Based Inhibitor" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 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 98.28 98.28 0.00e+00 . . . . 19937 1 72 no PDB 3D7Z . "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 73 no PDB 3D83 . "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19937 1 74 no PDB 3DS6 . "P38 Complex With A Phthalazine Inhibitor" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 75 no PDB 3E92 . "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" . . . . . 100.27 371 98.10 98.10 0.00e+00 . . . . 19937 1 76 no PDB 3E93 . "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" . . . . . 100.27 371 98.10 98.10 0.00e+00 . . . . 19937 1 77 no PDB 3FC1 . "Crystal Structure Of P38 Kinase Bound To Pyrimido-Pyridazinone Inhibitor" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 78 no PDB 3FI4 . "P38 Kinase Crystal Structure In Complex With Ro4499" . . . . . 100.54 372 98.10 98.64 0.00e+00 . . . . 19937 1 79 no PDB 3FKL . "P38 Kinase Crystal Structure In Complex With Ro9552" . . . . . 100.54 372 98.37 98.64 0.00e+00 . . . . 19937 1 80 no PDB 3FKN . "P38 Kinase Crystal Structure In Complex With Ro7125" . . . . . 100.54 372 98.37 98.64 0.00e+00 . . . . 19937 1 81 no PDB 3FKO . "P38 Kinase Crystal Structure In Complex With Ro3668" . . . . . 100.54 372 98.10 98.64 0.00e+00 . . . . 19937 1 82 no PDB 3FL4 . "P38 Kinase Crystal Structure In Complex With Ro5634" . . . . . 100.54 372 98.37 98.64 0.00e+00 . . . . 19937 1 83 no PDB 3FLN . "P38 Kinase Crystal Structure In Complex With R1487" . . . . . 100.54 372 98.10 98.64 0.00e+00 . . . . 19937 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 98.37 98.64 0.00e+00 . . . . 19937 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 98.37 98.64 0.00e+00 . . . . 19937 1 86 no PDB 3FLW . "P38 Kinase Crystal Structure In Complex With Pamapimod" . . . . . 100.54 372 98.37 98.64 0.00e+00 . . . . 19937 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 98.37 98.64 0.00e+00 . . . . 19937 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 98.37 98.64 0.00e+00 . . . . 19937 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 98.37 98.64 0.00e+00 . . . . 19937 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 98.37 98.64 0.00e+00 . . . . 19937 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 98.37 98.64 0.00e+00 . . . . 19937 1 92 no PDB 3FML . "P38 Kinase Crystal Structure In Complex With Ro6224" . . . . . 100.54 372 98.37 98.64 0.00e+00 . . . . 19937 1 93 no PDB 3FMM . "P38 Kinase Crystal Structure In Complex With Ro6226" . . . . . 100.54 372 98.37 98.64 0.00e+00 . . . . 19937 1 94 no PDB 3FMN . "P38 Kinase Crystal Structure In Complex With Ro2530" . . . . . 100.54 372 98.37 98.64 0.00e+00 . . . . 19937 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 98.37 98.64 0.00e+00 . . . . 19937 1 96 no PDB 3FSK . "P38 Kinase Crystal Structure In Complex With Ro6257" . . . . . 100.54 372 98.37 98.64 0.00e+00 . . . . 19937 1 97 no PDB 3GC7 . "The Structure Of P38alpha In Complex With A Dihydroquinazolinone" . . . . . 99.18 366 98.08 98.08 0.00e+00 . . . . 19937 1 98 no PDB 3GCP . "Human P38 Map Kinase In Complex With Sb203580" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 99 no PDB 3GCQ . "Human P38 Map Kinase In Complex With Rl45" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 100 no PDB 3GCS . "Human P38 Map Kinase In Complex With Sorafenib" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 101 no PDB 3GCU . "Human P38 Map Kinase In Complex With Rl48" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 102 no PDB 3GCV . "Human P38 Map Kinase In Complex With Rl62" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 103 no PDB 3GFE . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 104 no PDB 3GI3 . "Crystal Structure Of A N-Phenyl-N'-Naphthylurea Analog In Complex With P38 Map Kinase" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19937 1 105 no PDB 3HEC . "P38 In Complex With Imatinib" . . . . . 94.82 348 99.43 99.43 0.00e+00 . . . . 19937 1 106 no PDB 3HEG . "P38 In Complex With Sorafenib" . . . . . 94.82 348 99.43 99.43 0.00e+00 . . . . 19937 1 107 no PDB 3HL7 . "Crystal Structure Of Human P38alpha Complexed With Sd-0006" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 108 no PDB 3HLL . "Crystal Structure Of Human P38alpha Complexed With Ph-797804" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 109 no PDB 3HP2 . "Crystal Structure Of Human P38alpha Complexed With A Pyridinone Compound" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 110 no PDB 3HP5 . "Crystal Structure Of Human P38alpha Complexed With A Pyrimidopyridazinone Compound" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 111 no PDB 3HRB . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 359 99.44 99.44 0.00e+00 . . . . 19937 1 112 no PDB 3HUB . "Human P38 Map Kinase In Complex With Scios-469" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 113 no PDB 3HUC . "Human P38 Map Kinase In Complex With Rl40" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 114 no PDB 3HV3 . "Human P38 Map Kinase In Complex With Rl49" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 115 no PDB 3HV4 . "Human P38 Map Kinase In Complex With Rl51" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 116 no PDB 3HV5 . "Human P38 Map Kinase In Complex With Rl24" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 117 no PDB 3HV6 . "Human P38 Map Kinase In Complex With Rl39" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 118 no PDB 3HV7 . "Human P38 Map Kinase In Complex With Rl38" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 119 no PDB 3HVC . "Crystal Structure Of Human P38alpha Map Kinase" . . . . . 97.82 362 99.44 99.44 0.00e+00 . . . . 19937 1 120 no PDB 3IPH . "Crystal Structure Of P38 In Complex With A Biphenylamide Inhibitor" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19937 1 121 no PDB 3ITZ . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridazine Inhibitor" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 122 no PDB 3IW5 . "Human P38 Map Kinase In Complex With An Indole Derivative" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 123 no PDB 3IW6 . "Human P38 Map Kinase In Complex With A Benzylpiperazin- Pyrrol" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 124 no PDB 3IW7 . "Human P38 Map Kinase In Complex With An Imidazo-Pyridine" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 125 no PDB 3IW8 . "Structure Of Inactive Human P38 Map Kinase In Complex With A Thiazole-Urea" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 126 no PDB 3K3I . "P38alpha Bound To Novel Dgf-Out Compound Pf-00215955" . . . . . 94.82 350 99.43 99.43 0.00e+00 . . . . 19937 1 127 no PDB 3K3J . "P38alpha Bound To Novel Dfg-Out Compound Pf-00416121" . . . . . 97.82 362 99.44 99.44 0.00e+00 . . . . 19937 1 128 no PDB 3KF7 . "Crystal Structure Of Human P38alpha Complexed With A Triazolopyrimidine Compound" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 129 no PDB 3L8S . "Human P38 Map Kinase In Complex With Cp-547632" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 130 no PDB 3L8X . "P38 Alpha Kinase Complexed With A Pyrazolo-Pyrimidine Based Inhibitor" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 131 no PDB 3LFA . "Human P38 Map Kinase In Complex With Dasatinib" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 132 no PDB 3LFB . "Human P38 Map Kinase In Complex With Rl98" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 133 no PDB 3LFC . "Human P38 Map Kinase In Complex With Rl99" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 134 no PDB 3LFD . "Human P38 Map Kinase In Complex With Rl113" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 135 no PDB 3LFE . "Human P38 Map Kinase In Complex With Rl116" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 136 no PDB 3LFF . "Human P38 Map Kinase In Complex With Rl166" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 137 no PDB 3LHJ . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor." . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 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 99.44 99.44 0.00e+00 . . . . 19937 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 99.16 99.16 0.00e+00 . . . . 19937 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 99.16 99.16 0.00e+00 . . . . 19937 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 99.16 99.44 0.00e+00 . . . . 19937 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 99.16 99.16 0.00e+00 . . . . 19937 1 143 no PDB 3MPA . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 144 no PDB 3MPT . "Crystal Structure Of P38 Kinase In Complex With A Pyrrole-2- Carboxamide Inhibitor" . . . . . 100.27 371 98.37 98.37 0.00e+00 . . . . 19937 1 145 no PDB 3MVL . "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7k" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 146 no PDB 3MVM . "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7v" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 147 no PDB 3MW1 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 359 99.44 99.44 0.00e+00 . . . . 19937 1 148 no PDB 3NEW . "P38-Alpha Complexed With Compound 10" . . . . . 99.18 366 98.08 98.08 0.00e+00 . . . . 19937 1 149 no PDB 3NNU . "Crystal Structure Of P38 Alpha In Complex With Dp1376" . . . . . 96.19 354 99.43 99.43 0.00e+00 . . . . 19937 1 150 no PDB 3NNV . "Crystal Structure Of P38 Alpha In Complex With Dp437" . . . . . 96.19 354 99.43 99.43 0.00e+00 . . . . 19937 1 151 no PDB 3NNW . "Crystal Structure Of P38 Alpha In Complex With Dp802" . . . . . 96.19 354 99.43 99.43 0.00e+00 . . . . 19937 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 . . . . 19937 1 153 no PDB 3NWW . "P38 Alpha Kinase Complexed With A 2-aminothiazol-5-yl-pyrimidine Based Inhibitor" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 154 no PDB 3O8P . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 155 no PDB 3O8T . "Conformational Plasticity Of P38 Map Kinase Dfg-Motif Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 156 no PDB 3O8U . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.16 99.44 0.00e+00 . . . . 19937 1 157 no PDB 3OBG . "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 158 no PDB 3OBJ . "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 159 no PDB 3OC1 . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 160 no PDB 3OCG . "P38 Alpha Kinase Complexed With A 5-Amino-Pyrazole Based Inhibitor" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 161 no PDB 3OD6 . "Crystal Structure Of P38alpha Y323t Active Mutant" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 162 no PDB 3ODY . "Crystal Structure Of P38alpha Y323q Active Mutant" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 163 no PDB 3ODZ . "Crystal Structure Of P38alpha Y323r Active Mutant" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 164 no PDB 3OEF . "Crystal Structure Of Y323f Inactive Mutant Of P38alpha Map Kinase" . . . . . 97.82 360 99.16 99.44 0.00e+00 . . . . 19937 1 165 no PDB 3P4K . "The Third Conformation Of P38a Map Kinase Observed In Phosphorylated P38a And In Solution" . . . . . 100.82 370 97.84 98.11 0.00e+00 . . . . 19937 1 166 no PDB 3P5K . "P38 Inhibitor-Bound" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19937 1 167 no PDB 3P78 . "P38 Inhibitor-Bound" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19937 1 168 no PDB 3P79 . "P38 Inhibitor-Bound" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19937 1 169 no PDB 3P7A . "P38 Inhibitor-Bound" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19937 1 170 no PDB 3P7B . "P38 Inhibitor-Bound" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19937 1 171 no PDB 3P7C . "P38 Inhibitor-Bound" . . . . . 99.18 366 98.90 98.90 0.00e+00 . . . . 19937 1 172 no PDB 3PG3 . "Human P38 Map Kinase In Complex With Rl182" . . . . . 97.82 360 98.33 98.33 0.00e+00 . . . . 19937 1 173 no PDB 3QUD . "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino-Benzophenone" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 174 no PDB 3QUE . "Human P38 Map Kinase In Complex With Skepinone-l" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 175 no PDB 3RIN . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 176 no PDB 3ROC . "Crystal Structure Of Human P38 Alpha Complexed With A Pyrimidinone Compound" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 177 no PDB 3S3I . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 95.10 349 99.43 99.43 0.00e+00 . . . . 19937 1 178 no PDB 3S4Q . "P38 Alpha Kinase Complexed With A Pyrazolo-Triazine Based Inhibitor" . . . . . 99.18 366 99.45 99.45 0.00e+00 . . . . 19937 1 179 no PDB 3U8W . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Triazolopyridazinone Inhibitor" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 180 no PDB 3UVP . "Human P38 Map Kinase In Complex With A Benzamide Substituted Benzosuberone" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 181 no PDB 3UVQ . "Human P38 Map Kinase In Complex With A Dibenzosuberone Derivative" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 182 no PDB 3UVR . "Human P38 Map Kinase In Complex With Km064" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 183 no PDB 3ZS5 . "Structural Basis For Kinase Selectivity Of Three Clinical P38alpha Inhibitors" . . . . . 98.09 362 99.44 99.44 0.00e+00 . . . . 19937 1 184 no PDB 3ZSG . "X-Ray Structure Of P38alpha Bound To Tak-715" . . . . . 98.09 362 99.44 99.44 0.00e+00 . . . . 19937 1 185 no PDB 3ZSH . "X-Ray Structure Of P38alpha Bound To Scio-469" . . . . . 98.09 362 99.44 99.44 0.00e+00 . . . . 19937 1 186 no PDB 3ZSI . "X-Ray Structure Of P38alpha Bound To Vx-745" . . . . . 98.09 362 99.44 99.44 0.00e+00 . . . . 19937 1 187 no PDB 3ZYA . "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino- Dibenzosuberone" . . . . . 99.18 366 98.35 98.35 0.00e+00 . . . . 19937 1 188 no PDB 4A9Y . "P38alpha Map Kinase Bound To Cmpd 8" . . . . . 99.46 365 99.45 99.45 0.00e+00 . . . . 19937 1 189 no PDB 4AA0 . "P38alpha Map Kinase Bound To Cmpd 2" . . . . . 99.46 365 99.45 99.45 0.00e+00 . . . . 19937 1 190 no PDB 4AA4 . "P38alpha Map Kinase Bound To Cmpd 22" . . . . . 99.46 365 99.45 99.45 0.00e+00 . . . . 19937 1 191 no PDB 4AA5 . "P38alpha Map Kinase Bound To Cmpd 33" . . . . . 99.46 365 99.18 99.18 0.00e+00 . . . . 19937 1 192 no PDB 4AAC . "P38alpha Map Kinase Bound To Cmpd 29" . . . . . 99.46 365 99.45 99.45 0.00e+00 . . . . 19937 1 193 no PDB 4DLI . "Human P38 Map Kinase In Complex With Rl87" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 194 no PDB 4DLJ . "Human P38 Map Kinase In Complex With Rl163" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 195 no PDB 4E5A . "The W197a Mutant Of P38a Map Kinase" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 196 no PDB 4E5B . "Structure Of P38a Map Kinase Without Bog" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 197 no PDB 4E6A . "P38a-pia23 Complex" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 198 no PDB 4E6C . "P38a-perifosine Complex" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 199 no PDB 4E8A . "The Crystal Structure Of P38a Map Kinase In Complex With Pia24" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 200 no PDB 4EH2 . "Human P38 Map Kinase In Complex With Np-F1 And Rl87" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 201 no PDB 4EH3 . "Human P38 Map Kinase In Complex With Np-F2 And Rl87" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 202 no PDB 4EH4 . "Human P38 Map Kinase In Complex With Np-F3 And Rl87" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 203 no PDB 4EH5 . "Human P38 Map Kinase In Complex With Np-F4 And Rl87" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 204 no PDB 4EH6 . "Human P38 Map Kinase In Complex With Np-F5 And Rl87" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 205 no PDB 4EH7 . "Human P38 Map Kinase In Complex With Np-F6 And Rl87" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 206 no PDB 4EH8 . "Human P38 Map Kinase In Complex With Np-F7 And Rl87" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 207 no PDB 4EH9 . "Human P38 Map Kinase In Complex With Np-F11 And Rl87" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 208 no PDB 4EHV . "Human P38 Map Kinase In Complex With Np-F10 And Rl87" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 209 no PDB 4GEO . "P38a Map Kinase Def-pocket Penta Mutant (m194a, L195a, H228a, I229a, Y258a)" . . . . . 100.00 367 97.55 97.55 0.00e+00 . . . . 19937 1 210 no PDB 4KA3 . "Structure Of Map Kinase In Complex With A Docking Peptide" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19937 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 99.45 99.45 0.00e+00 . . . . 19937 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 99.45 99.45 0.00e+00 . . . . 19937 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 99.45 99.45 0.00e+00 . . . . 19937 1 214 no PDB 4L8M . "Human P38 Map Kinase In Complex With A Dibenzoxepinone" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 215 no PDB 4LOO . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (monoclinic Crystal Form)" . . . . . 97.82 361 98.89 98.89 0.00e+00 . . . . 19937 1 216 no PDB 4LOP . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form)" . . . . . 97.82 361 98.89 98.89 0.00e+00 . . . . 19937 1 217 no PDB 4LOQ . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form With Bound Sulphate)" . . . . . 97.82 361 98.89 98.89 0.00e+00 . . . . 19937 1 218 no PDB 4TYH . "Ternary Complex Of P38 And Mk2 With A P38 Inhibitor" . . . . . 94.82 348 98.85 98.85 0.00e+00 . . . . 19937 1 219 no DBJ BAB85654 . "Alternative spliced variant of p38alpha EXIP [Homo sapiens]" . . . . . 68.94 307 99.21 99.21 0.00e+00 . . . . 19937 1 220 no DBJ BAE21782 . "unnamed protein product [Mus musculus]" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19937 1 221 no DBJ BAE30324 . "unnamed protein product [Mus musculus]" . . . . . 77.11 283 98.94 98.94 0.00e+00 . . . . 19937 1 222 no DBJ BAE31659 . "unnamed protein product [Mus musculus]" . . . . . 77.11 283 98.94 98.94 0.00e+00 . . . . 19937 1 223 no DBJ BAF84398 . "unnamed protein product [Homo sapiens]" . . . . . 97.82 360 99.16 99.16 0.00e+00 . . . . 19937 1 224 no EMBL CAG38743 . "MAPK14 [Homo sapiens]" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 225 no GB AAA20888 . "MAP kinase [Mus musculus]" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19937 1 226 no GB AAA57456 . "CSaids binding protein [Homo sapiens]" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 227 no GB AAA74301 . "MAP kinase [Homo sapiens]" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 228 no GB AAB51285 . "p38 mitogen activated protein kinase [Rattus norvegicus]" . . . . . 97.82 360 97.49 98.33 0.00e+00 . . . . 19937 1 229 no GB AAC36131 . "p38 mitogen activated protein kinase [Canis lupus familiaris]" . . . . . 97.82 360 98.89 99.44 0.00e+00 . . . . 19937 1 230 no PRF 2111247A . "p38 mitogen-activated protein kinase" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 231 no PRF 2124426A . "Mxi2 protein" . . . . . 76.29 297 98.93 98.93 0.00e+00 . . . . 19937 1 232 no REF NP_001003206 . "mitogen-activated protein kinase 14 [Canis lupus familiaris]" . . . . . 97.82 360 98.89 99.44 0.00e+00 . . . . 19937 1 233 no REF NP_001136366 . "mitogen-activated protein kinase 14 [Ovis aries]" . . . . . 97.82 360 99.44 99.44 0.00e+00 . . . . 19937 1 234 no REF NP_001161985 . "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" . . . . . 77.11 283 98.94 98.94 0.00e+00 . . . . 19937 1 235 no REF NP_001161986 . "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" . . . . . 77.11 283 98.94 98.94 0.00e+00 . . . . 19937 1 236 no REF NP_036081 . "mitogen-activated protein kinase 14 isoform 1 [Mus musculus]" . . . . . 97.82 360 98.89 98.89 0.00e+00 . . . . 19937 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 98.89 99.44 0.00e+00 . . . . 19937 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 98.89 98.89 0.00e+00 . . . . 19937 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 98.05 98.61 0.00e+00 . . . . 19937 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 99.44 99.44 0.00e+00 . . . . 19937 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 . 19937 1 2 -5 ALA . 19937 1 3 -4 HIS . 19937 1 4 -3 HIS . 19937 1 5 -2 HIS . 19937 1 6 -1 HIS . 19937 1 7 0 HIS . 19937 1 8 1 HIS . 19937 1 9 2 SER . 19937 1 10 3 GLN . 19937 1 11 4 GLU . 19937 1 12 5 ARG . 19937 1 13 6 PRO . 19937 1 14 7 THR . 19937 1 15 8 PHE . 19937 1 16 9 TYR . 19937 1 17 10 ARG . 19937 1 18 11 GLN . 19937 1 19 12 GLU . 19937 1 20 13 LEU . 19937 1 21 14 ASN . 19937 1 22 15 LYS . 19937 1 23 16 THR . 19937 1 24 17 ILE . 19937 1 25 18 TRP . 19937 1 26 19 GLU . 19937 1 27 20 VAL . 19937 1 28 21 PRO . 19937 1 29 22 GLU . 19937 1 30 23 ARG . 19937 1 31 24 TYR . 19937 1 32 25 GLN . 19937 1 33 26 ASN . 19937 1 34 27 LEU . 19937 1 35 28 SER . 19937 1 36 29 PRO . 19937 1 37 30 VAL . 19937 1 38 31 GLY . 19937 1 39 32 SER . 19937 1 40 33 GLY . 19937 1 41 34 ALA . 19937 1 42 35 TYR . 19937 1 43 36 GLY . 19937 1 44 37 SER . 19937 1 45 38 VAL . 19937 1 46 39 CYS . 19937 1 47 40 ALA . 19937 1 48 41 ALA . 19937 1 49 42 PHE . 19937 1 50 43 ASP . 19937 1 51 44 THR . 19937 1 52 45 LYS . 19937 1 53 46 THR . 19937 1 54 47 GLY . 19937 1 55 48 LEU . 19937 1 56 49 ARG . 19937 1 57 50 VAL . 19937 1 58 51 ALA . 19937 1 59 52 VAL . 19937 1 60 53 LYS . 19937 1 61 54 LYS . 19937 1 62 55 LEU . 19937 1 63 56 SER . 19937 1 64 57 ARG . 19937 1 65 58 PRO . 19937 1 66 59 PHE . 19937 1 67 60 GLN . 19937 1 68 61 SER . 19937 1 69 62 ILE . 19937 1 70 63 ILE . 19937 1 71 64 HIS . 19937 1 72 65 ALA . 19937 1 73 66 LYS . 19937 1 74 67 ARG . 19937 1 75 68 THR . 19937 1 76 69 TYR . 19937 1 77 70 ARG . 19937 1 78 71 GLU . 19937 1 79 72 LEU . 19937 1 80 73 ARG . 19937 1 81 74 LEU . 19937 1 82 75 LEU . 19937 1 83 76 LYS . 19937 1 84 77 HIS . 19937 1 85 78 MET . 19937 1 86 79 LYS . 19937 1 87 80 HIS . 19937 1 88 81 GLU . 19937 1 89 82 ASN . 19937 1 90 83 VAL . 19937 1 91 84 ILE . 19937 1 92 85 GLY . 19937 1 93 86 LEU . 19937 1 94 87 LEU . 19937 1 95 88 ASP . 19937 1 96 89 VAL . 19937 1 97 90 PHE . 19937 1 98 91 THR . 19937 1 99 92 PRO . 19937 1 100 93 ALA . 19937 1 101 94 ARG . 19937 1 102 95 SER . 19937 1 103 96 LEU . 19937 1 104 97 GLU . 19937 1 105 98 GLU . 19937 1 106 99 PHE . 19937 1 107 100 ASN . 19937 1 108 101 ASP . 19937 1 109 102 VAL . 19937 1 110 103 TYR . 19937 1 111 104 LEU . 19937 1 112 105 VAL . 19937 1 113 106 THR . 19937 1 114 107 HIS . 19937 1 115 108 LEU . 19937 1 116 109 MET . 19937 1 117 110 GLY . 19937 1 118 111 ALA . 19937 1 119 112 ASP . 19937 1 120 113 LEU . 19937 1 121 114 ASN . 19937 1 122 115 ASN . 19937 1 123 116 ILE . 19937 1 124 117 VAL . 19937 1 125 118 LYS . 19937 1 126 119 CYS . 19937 1 127 120 GLN . 19937 1 128 121 LYS . 19937 1 129 122 LEU . 19937 1 130 123 THR . 19937 1 131 124 ASP . 19937 1 132 125 ASP . 19937 1 133 126 HIS . 19937 1 134 127 VAL . 19937 1 135 128 GLN . 19937 1 136 129 PHE . 19937 1 137 130 LEU . 19937 1 138 131 ILE . 19937 1 139 132 TYR . 19937 1 140 133 GLN . 19937 1 141 134 ILE . 19937 1 142 135 LEU . 19937 1 143 136 ARG . 19937 1 144 137 GLY . 19937 1 145 138 LEU . 19937 1 146 139 LYS . 19937 1 147 140 TYR . 19937 1 148 141 ILE . 19937 1 149 142 HIS . 19937 1 150 143 SER . 19937 1 151 144 ALA . 19937 1 152 145 ASP . 19937 1 153 146 ILE . 19937 1 154 147 ILE . 19937 1 155 148 HIS . 19937 1 156 149 ARG . 19937 1 157 150 ASP . 19937 1 158 151 LEU . 19937 1 159 152 LYS . 19937 1 160 153 PRO . 19937 1 161 154 SER . 19937 1 162 155 ASN . 19937 1 163 156 LEU . 19937 1 164 157 ALA . 19937 1 165 158 VAL . 19937 1 166 159 ASN . 19937 1 167 160 GLU . 19937 1 168 161 ASP . 19937 1 169 162 CYS . 19937 1 170 163 GLU . 19937 1 171 164 LEU . 19937 1 172 165 LYS . 19937 1 173 166 ILE . 19937 1 174 167 LEU . 19937 1 175 168 ASP . 19937 1 176 169 PHE . 19937 1 177 170 GLY . 19937 1 178 171 LEU . 19937 1 179 172 ALA . 19937 1 180 173 ARG . 19937 1 181 174 HIS . 19937 1 182 175 THR . 19937 1 183 176 ASP . 19937 1 184 177 ASP . 19937 1 185 178 GLU . 19937 1 186 179 MET . 19937 1 187 180 TPO . 19937 1 188 181 GLY . 19937 1 189 182 PTR . 19937 1 190 183 VAL . 19937 1 191 184 ALA . 19937 1 192 185 THR . 19937 1 193 186 ARG . 19937 1 194 187 TRP . 19937 1 195 188 TYR . 19937 1 196 189 ARG . 19937 1 197 190 ALA . 19937 1 198 191 PRO . 19937 1 199 192 GLU . 19937 1 200 193 ILE . 19937 1 201 194 MET . 19937 1 202 195 LEU . 19937 1 203 196 ASN . 19937 1 204 197 TRP . 19937 1 205 198 MET . 19937 1 206 199 HIS . 19937 1 207 200 TYR . 19937 1 208 201 ASN . 19937 1 209 202 GLN . 19937 1 210 203 THR . 19937 1 211 204 VAL . 19937 1 212 205 ASP . 19937 1 213 206 ILE . 19937 1 214 207 TRP . 19937 1 215 208 SER . 19937 1 216 209 VAL . 19937 1 217 210 GLY . 19937 1 218 211 CYS . 19937 1 219 212 ILE . 19937 1 220 213 MET . 19937 1 221 214 ALA . 19937 1 222 215 GLU . 19937 1 223 216 LEU . 19937 1 224 217 LEU . 19937 1 225 218 THR . 19937 1 226 219 GLY . 19937 1 227 220 ARG . 19937 1 228 221 THR . 19937 1 229 222 LEU . 19937 1 230 223 PHE . 19937 1 231 224 PRO . 19937 1 232 225 GLY . 19937 1 233 226 THR . 19937 1 234 227 ASP . 19937 1 235 228 HIS . 19937 1 236 229 ILE . 19937 1 237 230 ASP . 19937 1 238 231 GLN . 19937 1 239 232 LEU . 19937 1 240 233 LYS . 19937 1 241 234 LEU . 19937 1 242 235 ILE . 19937 1 243 236 LEU . 19937 1 244 237 ARG . 19937 1 245 238 LEU . 19937 1 246 239 VAL . 19937 1 247 240 GLY . 19937 1 248 241 THR . 19937 1 249 242 PRO . 19937 1 250 243 GLY . 19937 1 251 244 ALA . 19937 1 252 245 GLU . 19937 1 253 246 LEU . 19937 1 254 247 LEU . 19937 1 255 248 LYS . 19937 1 256 249 LYS . 19937 1 257 250 ILE . 19937 1 258 251 SER . 19937 1 259 252 SER . 19937 1 260 253 GLU . 19937 1 261 254 SER . 19937 1 262 255 ALA . 19937 1 263 256 ARG . 19937 1 264 257 ASN . 19937 1 265 258 TYR . 19937 1 266 259 ILE . 19937 1 267 260 GLN . 19937 1 268 261 SER . 19937 1 269 262 LEU . 19937 1 270 263 THR . 19937 1 271 264 GLN . 19937 1 272 265 MET . 19937 1 273 266 PRO . 19937 1 274 267 LYS . 19937 1 275 268 MET . 19937 1 276 269 ASN . 19937 1 277 270 PHE . 19937 1 278 271 ALA . 19937 1 279 272 ASN . 19937 1 280 273 VAL . 19937 1 281 274 PHE . 19937 1 282 275 ILE . 19937 1 283 276 GLY . 19937 1 284 277 ALA . 19937 1 285 278 ASN . 19937 1 286 279 PRO . 19937 1 287 280 LEU . 19937 1 288 281 ALA . 19937 1 289 282 VAL . 19937 1 290 283 ASP . 19937 1 291 284 LEU . 19937 1 292 285 LEU . 19937 1 293 286 GLU . 19937 1 294 287 LYS . 19937 1 295 288 MET . 19937 1 296 289 LEU . 19937 1 297 290 VAL . 19937 1 298 291 LEU . 19937 1 299 292 ASP . 19937 1 300 293 SER . 19937 1 301 294 ASP . 19937 1 302 295 LYS . 19937 1 303 296 ARG . 19937 1 304 297 ILE . 19937 1 305 298 THR . 19937 1 306 299 ALA . 19937 1 307 300 ALA . 19937 1 308 301 GLN . 19937 1 309 302 ALA . 19937 1 310 303 LEU . 19937 1 311 304 ALA . 19937 1 312 305 HIS . 19937 1 313 306 ALA . 19937 1 314 307 TYR . 19937 1 315 308 PHE . 19937 1 316 309 ALA . 19937 1 317 310 GLN . 19937 1 318 311 TYR . 19937 1 319 312 HIS . 19937 1 320 313 ASP . 19937 1 321 314 PRO . 19937 1 322 315 ASP . 19937 1 323 316 ASP . 19937 1 324 317 GLU . 19937 1 325 318 PRO . 19937 1 326 319 VAL . 19937 1 327 320 ALA . 19937 1 328 321 ASP . 19937 1 329 322 PRO . 19937 1 330 323 TYR . 19937 1 331 324 ASP . 19937 1 332 325 GLN . 19937 1 333 326 SER . 19937 1 334 327 PHE . 19937 1 335 328 GLU . 19937 1 336 329 SER . 19937 1 337 330 ARG . 19937 1 338 331 ASP . 19937 1 339 332 LEU . 19937 1 340 333 LEU . 19937 1 341 334 ILE . 19937 1 342 335 ASP . 19937 1 343 336 GLU . 19937 1 344 337 TRP . 19937 1 345 338 LYS . 19937 1 346 339 SER . 19937 1 347 340 LEU . 19937 1 348 341 THR . 19937 1 349 342 TYR . 19937 1 350 343 ASP . 19937 1 351 344 GLU . 19937 1 352 345 VAL . 19937 1 353 346 ILE . 19937 1 354 347 SER . 19937 1 355 348 PHE . 19937 1 356 349 VAL . 19937 1 357 350 PRO . 19937 1 358 351 PRO . 19937 1 359 352 PRO . 19937 1 360 353 LEU . 19937 1 361 354 ASP . 19937 1 362 355 GLN . 19937 1 363 356 GLU . 19937 1 364 357 GLU . 19937 1 365 358 MET . 19937 1 366 359 GLU . 19937 1 367 360 SER . 19937 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 19937 1 . ALA 2 2 19937 1 . HIS 3 3 19937 1 . HIS 4 4 19937 1 . HIS 5 5 19937 1 . HIS 6 6 19937 1 . HIS 7 7 19937 1 . HIS 8 8 19937 1 . SER 9 9 19937 1 . GLN 10 10 19937 1 . GLU 11 11 19937 1 . ARG 12 12 19937 1 . PRO 13 13 19937 1 . THR 14 14 19937 1 . PHE 15 15 19937 1 . TYR 16 16 19937 1 . ARG 17 17 19937 1 . GLN 18 18 19937 1 . GLU 19 19 19937 1 . LEU 20 20 19937 1 . ASN 21 21 19937 1 . LYS 22 22 19937 1 . THR 23 23 19937 1 . ILE 24 24 19937 1 . TRP 25 25 19937 1 . GLU 26 26 19937 1 . VAL 27 27 19937 1 . PRO 28 28 19937 1 . GLU 29 29 19937 1 . ARG 30 30 19937 1 . TYR 31 31 19937 1 . GLN 32 32 19937 1 . ASN 33 33 19937 1 . LEU 34 34 19937 1 . SER 35 35 19937 1 . PRO 36 36 19937 1 . VAL 37 37 19937 1 . GLY 38 38 19937 1 . SER 39 39 19937 1 . GLY 40 40 19937 1 . ALA 41 41 19937 1 . TYR 42 42 19937 1 . GLY 43 43 19937 1 . SER 44 44 19937 1 . VAL 45 45 19937 1 . CYS 46 46 19937 1 . ALA 47 47 19937 1 . ALA 48 48 19937 1 . PHE 49 49 19937 1 . ASP 50 50 19937 1 . THR 51 51 19937 1 . LYS 52 52 19937 1 . THR 53 53 19937 1 . GLY 54 54 19937 1 . LEU 55 55 19937 1 . ARG 56 56 19937 1 . VAL 57 57 19937 1 . ALA 58 58 19937 1 . VAL 59 59 19937 1 . LYS 60 60 19937 1 . LYS 61 61 19937 1 . LEU 62 62 19937 1 . SER 63 63 19937 1 . ARG 64 64 19937 1 . PRO 65 65 19937 1 . PHE 66 66 19937 1 . GLN 67 67 19937 1 . SER 68 68 19937 1 . ILE 69 69 19937 1 . ILE 70 70 19937 1 . HIS 71 71 19937 1 . ALA 72 72 19937 1 . LYS 73 73 19937 1 . ARG 74 74 19937 1 . THR 75 75 19937 1 . TYR 76 76 19937 1 . ARG 77 77 19937 1 . GLU 78 78 19937 1 . LEU 79 79 19937 1 . ARG 80 80 19937 1 . LEU 81 81 19937 1 . LEU 82 82 19937 1 . LYS 83 83 19937 1 . HIS 84 84 19937 1 . MET 85 85 19937 1 . LYS 86 86 19937 1 . HIS 87 87 19937 1 . GLU 88 88 19937 1 . ASN 89 89 19937 1 . VAL 90 90 19937 1 . ILE 91 91 19937 1 . GLY 92 92 19937 1 . LEU 93 93 19937 1 . LEU 94 94 19937 1 . ASP 95 95 19937 1 . VAL 96 96 19937 1 . PHE 97 97 19937 1 . THR 98 98 19937 1 . PRO 99 99 19937 1 . ALA 100 100 19937 1 . ARG 101 101 19937 1 . SER 102 102 19937 1 . LEU 103 103 19937 1 . GLU 104 104 19937 1 . GLU 105 105 19937 1 . PHE 106 106 19937 1 . ASN 107 107 19937 1 . ASP 108 108 19937 1 . VAL 109 109 19937 1 . TYR 110 110 19937 1 . LEU 111 111 19937 1 . VAL 112 112 19937 1 . THR 113 113 19937 1 . HIS 114 114 19937 1 . LEU 115 115 19937 1 . MET 116 116 19937 1 . GLY 117 117 19937 1 . ALA 118 118 19937 1 . ASP 119 119 19937 1 . LEU 120 120 19937 1 . ASN 121 121 19937 1 . ASN 122 122 19937 1 . ILE 123 123 19937 1 . VAL 124 124 19937 1 . LYS 125 125 19937 1 . CYS 126 126 19937 1 . GLN 127 127 19937 1 . LYS 128 128 19937 1 . LEU 129 129 19937 1 . THR 130 130 19937 1 . ASP 131 131 19937 1 . ASP 132 132 19937 1 . HIS 133 133 19937 1 . VAL 134 134 19937 1 . GLN 135 135 19937 1 . PHE 136 136 19937 1 . LEU 137 137 19937 1 . ILE 138 138 19937 1 . TYR 139 139 19937 1 . GLN 140 140 19937 1 . ILE 141 141 19937 1 . LEU 142 142 19937 1 . ARG 143 143 19937 1 . GLY 144 144 19937 1 . LEU 145 145 19937 1 . LYS 146 146 19937 1 . TYR 147 147 19937 1 . ILE 148 148 19937 1 . HIS 149 149 19937 1 . SER 150 150 19937 1 . ALA 151 151 19937 1 . ASP 152 152 19937 1 . ILE 153 153 19937 1 . ILE 154 154 19937 1 . HIS 155 155 19937 1 . ARG 156 156 19937 1 . ASP 157 157 19937 1 . LEU 158 158 19937 1 . LYS 159 159 19937 1 . PRO 160 160 19937 1 . SER 161 161 19937 1 . ASN 162 162 19937 1 . LEU 163 163 19937 1 . ALA 164 164 19937 1 . VAL 165 165 19937 1 . ASN 166 166 19937 1 . GLU 167 167 19937 1 . ASP 168 168 19937 1 . CYS 169 169 19937 1 . GLU 170 170 19937 1 . LEU 171 171 19937 1 . LYS 172 172 19937 1 . ILE 173 173 19937 1 . LEU 174 174 19937 1 . ASP 175 175 19937 1 . PHE 176 176 19937 1 . GLY 177 177 19937 1 . LEU 178 178 19937 1 . ALA 179 179 19937 1 . ARG 180 180 19937 1 . HIS 181 181 19937 1 . THR 182 182 19937 1 . ASP 183 183 19937 1 . ASP 184 184 19937 1 . GLU 185 185 19937 1 . MET 186 186 19937 1 . TPO 187 187 19937 1 . GLY 188 188 19937 1 . PTR 189 189 19937 1 . VAL 190 190 19937 1 . ALA 191 191 19937 1 . THR 192 192 19937 1 . ARG 193 193 19937 1 . TRP 194 194 19937 1 . TYR 195 195 19937 1 . ARG 196 196 19937 1 . ALA 197 197 19937 1 . PRO 198 198 19937 1 . GLU 199 199 19937 1 . ILE 200 200 19937 1 . MET 201 201 19937 1 . LEU 202 202 19937 1 . ASN 203 203 19937 1 . TRP 204 204 19937 1 . MET 205 205 19937 1 . HIS 206 206 19937 1 . TYR 207 207 19937 1 . ASN 208 208 19937 1 . GLN 209 209 19937 1 . THR 210 210 19937 1 . VAL 211 211 19937 1 . ASP 212 212 19937 1 . ILE 213 213 19937 1 . TRP 214 214 19937 1 . SER 215 215 19937 1 . VAL 216 216 19937 1 . GLY 217 217 19937 1 . CYS 218 218 19937 1 . ILE 219 219 19937 1 . MET 220 220 19937 1 . ALA 221 221 19937 1 . GLU 222 222 19937 1 . LEU 223 223 19937 1 . LEU 224 224 19937 1 . THR 225 225 19937 1 . GLY 226 226 19937 1 . ARG 227 227 19937 1 . THR 228 228 19937 1 . LEU 229 229 19937 1 . PHE 230 230 19937 1 . PRO 231 231 19937 1 . GLY 232 232 19937 1 . THR 233 233 19937 1 . ASP 234 234 19937 1 . HIS 235 235 19937 1 . ILE 236 236 19937 1 . ASP 237 237 19937 1 . GLN 238 238 19937 1 . LEU 239 239 19937 1 . LYS 240 240 19937 1 . LEU 241 241 19937 1 . ILE 242 242 19937 1 . LEU 243 243 19937 1 . ARG 244 244 19937 1 . LEU 245 245 19937 1 . VAL 246 246 19937 1 . GLY 247 247 19937 1 . THR 248 248 19937 1 . PRO 249 249 19937 1 . GLY 250 250 19937 1 . ALA 251 251 19937 1 . GLU 252 252 19937 1 . LEU 253 253 19937 1 . LEU 254 254 19937 1 . LYS 255 255 19937 1 . LYS 256 256 19937 1 . ILE 257 257 19937 1 . SER 258 258 19937 1 . SER 259 259 19937 1 . GLU 260 260 19937 1 . SER 261 261 19937 1 . ALA 262 262 19937 1 . ARG 263 263 19937 1 . ASN 264 264 19937 1 . TYR 265 265 19937 1 . ILE 266 266 19937 1 . GLN 267 267 19937 1 . SER 268 268 19937 1 . LEU 269 269 19937 1 . THR 270 270 19937 1 . GLN 271 271 19937 1 . MET 272 272 19937 1 . PRO 273 273 19937 1 . LYS 274 274 19937 1 . MET 275 275 19937 1 . ASN 276 276 19937 1 . PHE 277 277 19937 1 . ALA 278 278 19937 1 . ASN 279 279 19937 1 . VAL 280 280 19937 1 . PHE 281 281 19937 1 . ILE 282 282 19937 1 . GLY 283 283 19937 1 . ALA 284 284 19937 1 . ASN 285 285 19937 1 . PRO 286 286 19937 1 . LEU 287 287 19937 1 . ALA 288 288 19937 1 . VAL 289 289 19937 1 . ASP 290 290 19937 1 . LEU 291 291 19937 1 . LEU 292 292 19937 1 . GLU 293 293 19937 1 . LYS 294 294 19937 1 . MET 295 295 19937 1 . LEU 296 296 19937 1 . VAL 297 297 19937 1 . LEU 298 298 19937 1 . ASP 299 299 19937 1 . SER 300 300 19937 1 . ASP 301 301 19937 1 . LYS 302 302 19937 1 . ARG 303 303 19937 1 . ILE 304 304 19937 1 . THR 305 305 19937 1 . ALA 306 306 19937 1 . ALA 307 307 19937 1 . GLN 308 308 19937 1 . ALA 309 309 19937 1 . LEU 310 310 19937 1 . ALA 311 311 19937 1 . HIS 312 312 19937 1 . ALA 313 313 19937 1 . TYR 314 314 19937 1 . PHE 315 315 19937 1 . ALA 316 316 19937 1 . GLN 317 317 19937 1 . TYR 318 318 19937 1 . HIS 319 319 19937 1 . ASP 320 320 19937 1 . PRO 321 321 19937 1 . ASP 322 322 19937 1 . ASP 323 323 19937 1 . GLU 324 324 19937 1 . PRO 325 325 19937 1 . VAL 326 326 19937 1 . ALA 327 327 19937 1 . ASP 328 328 19937 1 . PRO 329 329 19937 1 . TYR 330 330 19937 1 . ASP 331 331 19937 1 . GLN 332 332 19937 1 . SER 333 333 19937 1 . PHE 334 334 19937 1 . GLU 335 335 19937 1 . SER 336 336 19937 1 . ARG 337 337 19937 1 . ASP 338 338 19937 1 . LEU 339 339 19937 1 . LEU 340 340 19937 1 . ILE 341 341 19937 1 . ASP 342 342 19937 1 . GLU 343 343 19937 1 . TRP 344 344 19937 1 . LYS 345 345 19937 1 . SER 346 346 19937 1 . LEU 347 347 19937 1 . THR 348 348 19937 1 . TYR 349 349 19937 1 . ASP 350 350 19937 1 . GLU 351 351 19937 1 . VAL 352 352 19937 1 . ILE 353 353 19937 1 . SER 354 354 19937 1 . PHE 355 355 19937 1 . VAL 356 356 19937 1 . PRO 357 357 19937 1 . PRO 358 358 19937 1 . PRO 359 359 19937 1 . LEU 360 360 19937 1 . ASP 361 361 19937 1 . GLN 362 362 19937 1 . GLU 363 363 19937 1 . GLU 364 364 19937 1 . MET 365 365 19937 1 . GLU 366 366 19937 1 . SER 367 367 19937 1 stop_ save_ save_MK2_334-D_peptide _Entity.Sf_category entity _Entity.Sf_framecode MK2_334-D_peptide _Entity.Entry_ID 19937 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name MK2_334/D_peptide _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 ; GPMQSTKVPQTPLHTSRVLK EDKERWEDVKEEMTSALATM RVDYEQIKIKKIEDASNPLL LKRRKKARALEAAALAHWLE HHHHHH ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details 'Corresponding to a.a. 326 400 in human MK2. C-term. 8 a.a. residues are non-natural purification tag.' _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 86 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-30 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 19936 . MK2_334/D_peptide . . . . . 100.00 86 100.00 100.00 1.41e-53 . . . . 19937 2 2 no PDB 1KWP . "Crystal Structure Of Mapkap2" . . . . . 87.21 400 100.00 100.00 4.67e-41 . . . . 19937 2 3 no PDB 1NXK . "Crystal Structure Of Staurosporine Bound To Map Kap Kinase 2" . . . . . 86.05 400 98.65 98.65 3.96e-39 . . . . 19937 2 4 no PDB 1NY3 . "Crystal Structure Of Adp Bound To Map Kap Kinase 2" . . . . . 87.21 400 100.00 100.00 4.67e-41 . . . . 19937 2 5 no PDB 2ONL . "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" . . . . . 87.21 406 100.00 100.00 5.69e-41 . . . . 19937 2 6 no PDB 2OZA . "Structure Of P38alpha Complex" . . . . . 87.21 356 100.00 100.00 2.84e-41 . . . . 19937 2 7 no PDB 2P3G . "Crystal Structure Of A Pyrrolopyridine Inhibitor Bound To Mapkap Kinase-2" . . . . . 53.49 327 100.00 100.00 1.37e-21 . . . . 19937 2 8 no PDB 3FYJ . "Crystal Structure Of An Optimzied Benzothiophene Inhibitor Bound To Mapkap Kinase-2 (Mk-2)" . . . . . 53.49 327 100.00 100.00 1.37e-21 . . . . 19937 2 9 no PDB 3FYK . "Crystal Structure Of A Benzthiophene Lead Bound To Mapkap Kinase-2 (Mk-2)" . . . . . 53.49 327 100.00 100.00 1.37e-21 . . . . 19937 2 10 no DBJ BAE33092 . "unnamed protein product [Mus musculus]" . . . . . 87.21 386 97.33 98.67 1.28e-39 . . . . 19937 2 11 no DBJ BAJ20782 . "mitogen-activated protein kinase-activated protein kinase 2 [synthetic construct]" . . . . . 87.21 400 100.00 100.00 4.67e-41 . . . . 19937 2 12 no EMBL CAA53094 . "MAP kinase activated protein kinase-2 [Homo sapiens]" . . . . . 87.21 396 100.00 100.00 3.59e-41 . . . . 19937 2 13 no EMBL CAA54183 . "MAP kinase-activated protein kinase 2 [Mus musculus]" . . . . . 87.21 385 97.33 98.67 1.01e-39 . . . . 19937 2 14 no EMBL CAA57700 . "MapKap kinase 2 [Cricetulus longicaudatus]" . . . . . 87.21 329 98.67 100.00 7.18e-41 . . . . 19937 2 15 no GB AAH24559 . "Mapkapk2 protein, partial [Mus musculus]" . . . . . 87.21 181 97.33 98.67 2.64e-41 . . . . 19937 2 16 no GB AAH36060 . "Mitogen-activated protein kinase-activated protein kinase 2 [Homo sapiens]" . . . . . 87.21 400 100.00 100.00 4.67e-41 . . . . 19937 2 17 no GB AAH52584 . "Mitogen-activated protein kinase-activated protein kinase 2 [Homo sapiens]" . . . . . 87.21 400 100.00 100.00 4.67e-41 . . . . 19937 2 18 no GB AAH63064 . "MAP kinase-activated protein kinase 2 [Mus musculus]" . . . . . 87.21 386 97.33 98.67 1.28e-39 . . . . 19937 2 19 no GB AIC55551 . "MAPKAPK2, partial [synthetic construct]" . . . . . 87.21 400 100.00 100.00 4.67e-41 . . . . 19937 2 20 no REF NP_032577 . "MAP kinase-activated protein kinase 2 [Mus musculus]" . . . . . 87.21 386 97.33 98.67 1.28e-39 . . . . 19937 2 21 no REF NP_116584 . "MAP kinase-activated protein kinase 2 isoform 2 [Homo sapiens]" . . . . . 87.21 400 100.00 100.00 4.67e-41 . . . . 19937 2 22 no REF XP_001085549 . "PREDICTED: MAP kinase-activated protein kinase 2 isoform 2 [Macaca mulatta]" . . . . . 87.21 402 100.00 100.00 5.29e-41 . . . . 19937 2 23 no REF XP_001164988 . "PREDICTED: MAP kinase-activated protein kinase 2 [Pan troglodytes]" . . . . . 87.21 400 100.00 100.00 5.13e-41 . . . . 19937 2 24 no REF XP_001255255 . "PREDICTED: MAP kinase-activated protein kinase 2 isoform X1 [Bos taurus]" . . . . . 87.21 533 100.00 100.00 1.51e-40 . . . . 19937 2 25 no SP P49136 . "RecName: Full=MAP kinase-activated protein kinase 2; Short=MAPK-activated protein kinase 2; Short=MAPKAP kinase 2; Short=MAPKAP" . . . . . 87.21 329 98.67 100.00 7.18e-41 . . . . 19937 2 26 no SP P49137 . "RecName: Full=MAP kinase-activated protein kinase 2; Short=MAPK-activated protein kinase 2; Short=MAPKAP kinase 2; Short=MAPKAP" . . . . . 87.21 400 100.00 100.00 4.67e-41 . . . . 19937 2 27 no SP P49138 . "RecName: Full=MAP kinase-activated protein kinase 2; Short=MAPK-activated protein kinase 2; Short=MAPKAP kinase 2; Short=MAPKAP" . . . . . 87.21 386 97.33 98.67 1.28e-39 . . . . 19937 2 28 no SP P49139 . "RecName: Full=MAP kinase-activated protein kinase 2; Short=MAPK-activated protein kinase 2; Short=MAPKAP kinase 2; Short=MAPKAP" . . . . . 87.21 366 100.00 100.00 4.18e-41 . . . . 19937 2 29 no TPG DAA21536 . "TPA: MAP kinase-activated protein kinase 2-like [Bos taurus]" . . . . . 87.21 509 100.00 100.00 2.08e-40 . . . . 19937 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 326 GLY . 19937 2 2 327 PRO . 19937 2 3 328 MET . 19937 2 4 329 GLN . 19937 2 5 330 SER . 19937 2 6 331 THR . 19937 2 7 332 LYS . 19937 2 8 333 VAL . 19937 2 9 334 PRO . 19937 2 10 335 GLN . 19937 2 11 336 THR . 19937 2 12 337 PRO . 19937 2 13 338 LEU . 19937 2 14 339 HIS . 19937 2 15 340 THR . 19937 2 16 341 SER . 19937 2 17 342 ARG . 19937 2 18 343 VAL . 19937 2 19 344 LEU . 19937 2 20 345 LYS . 19937 2 21 346 GLU . 19937 2 22 347 ASP . 19937 2 23 348 LYS . 19937 2 24 349 GLU . 19937 2 25 350 ARG . 19937 2 26 351 TRP . 19937 2 27 352 GLU . 19937 2 28 353 ASP . 19937 2 29 354 VAL . 19937 2 30 355 LYS . 19937 2 31 356 GLU . 19937 2 32 357 GLU . 19937 2 33 358 MET . 19937 2 34 359 THR . 19937 2 35 360 SER . 19937 2 36 361 ALA . 19937 2 37 362 LEU . 19937 2 38 363 ALA . 19937 2 39 364 THR . 19937 2 40 365 MET . 19937 2 41 366 ARG . 19937 2 42 367 VAL . 19937 2 43 368 ASP . 19937 2 44 369 TYR . 19937 2 45 370 GLU . 19937 2 46 371 GLN . 19937 2 47 372 ILE . 19937 2 48 373 LYS . 19937 2 49 374 ILE . 19937 2 50 375 LYS . 19937 2 51 376 LYS . 19937 2 52 377 ILE . 19937 2 53 378 GLU . 19937 2 54 379 ASP . 19937 2 55 380 ALA . 19937 2 56 381 SER . 19937 2 57 382 ASN . 19937 2 58 383 PRO . 19937 2 59 384 LEU . 19937 2 60 385 LEU . 19937 2 61 386 LEU . 19937 2 62 387 LYS . 19937 2 63 388 ARG . 19937 2 64 389 ARG . 19937 2 65 390 LYS . 19937 2 66 391 LYS . 19937 2 67 392 ALA . 19937 2 68 393 ARG . 19937 2 69 394 ALA . 19937 2 70 395 LEU . 19937 2 71 396 GLU . 19937 2 72 397 ALA . 19937 2 73 398 ALA . 19937 2 74 399 ALA . 19937 2 75 400 LEU . 19937 2 76 401 ALA . 19937 2 77 402 HIS . 19937 2 78 403 TRP . 19937 2 79 404 LEU . 19937 2 80 405 GLU . 19937 2 81 406 HIS . 19937 2 82 407 HIS . 19937 2 83 408 HIS . 19937 2 84 409 HIS . 19937 2 85 410 HIS . 19937 2 86 411 HIS . 19937 2 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . GLY 1 1 19937 2 . PRO 2 2 19937 2 . MET 3 3 19937 2 . GLN 4 4 19937 2 . SER 5 5 19937 2 . THR 6 6 19937 2 . LYS 7 7 19937 2 . VAL 8 8 19937 2 . PRO 9 9 19937 2 . GLN 10 10 19937 2 . THR 11 11 19937 2 . PRO 12 12 19937 2 . LEU 13 13 19937 2 . HIS 14 14 19937 2 . THR 15 15 19937 2 . SER 16 16 19937 2 . ARG 17 17 19937 2 . VAL 18 18 19937 2 . LEU 19 19 19937 2 . LYS 20 20 19937 2 . GLU 21 21 19937 2 . ASP 22 22 19937 2 . LYS 23 23 19937 2 . GLU 24 24 19937 2 . ARG 25 25 19937 2 . TRP 26 26 19937 2 . GLU 27 27 19937 2 . ASP 28 28 19937 2 . VAL 29 29 19937 2 . LYS 30 30 19937 2 . GLU 31 31 19937 2 . GLU 32 32 19937 2 . MET 33 33 19937 2 . THR 34 34 19937 2 . SER 35 35 19937 2 . ALA 36 36 19937 2 . LEU 37 37 19937 2 . ALA 38 38 19937 2 . THR 39 39 19937 2 . MET 40 40 19937 2 . ARG 41 41 19937 2 . VAL 42 42 19937 2 . ASP 43 43 19937 2 . TYR 44 44 19937 2 . GLU 45 45 19937 2 . GLN 46 46 19937 2 . ILE 47 47 19937 2 . LYS 48 48 19937 2 . ILE 49 49 19937 2 . LYS 50 50 19937 2 . LYS 51 51 19937 2 . ILE 52 52 19937 2 . GLU 53 53 19937 2 . ASP 54 54 19937 2 . ALA 55 55 19937 2 . SER 56 56 19937 2 . ASN 57 57 19937 2 . PRO 58 58 19937 2 . LEU 59 59 19937 2 . LEU 60 60 19937 2 . LEU 61 61 19937 2 . LYS 62 62 19937 2 . ARG 63 63 19937 2 . ARG 64 64 19937 2 . LYS 65 65 19937 2 . LYS 66 66 19937 2 . ALA 67 67 19937 2 . ARG 68 68 19937 2 . ALA 69 69 19937 2 . LEU 70 70 19937 2 . GLU 71 71 19937 2 . ALA 72 72 19937 2 . ALA 73 73 19937 2 . ALA 74 74 19937 2 . LEU 75 75 19937 2 . ALA 76 76 19937 2 . HIS 77 77 19937 2 . TRP 78 78 19937 2 . LEU 79 79 19937 2 . GLU 80 80 19937 2 . HIS 81 81 19937 2 . HIS 82 82 19937 2 . HIS 83 83 19937 2 . HIS 84 84 19937 2 . HIS 85 85 19937 2 . HIS 86 86 19937 2 stop_ save_ save_entity_ADP _Entity.Sf_category entity _Entity.Sf_framecode entity_ADP _Entity.Entry_ID 19937 _Entity.ID 3 _Entity.BMRB_code ADP _Entity.Name ADENOSINE-5'-DIPHOSPHATE _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components 1 _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 3 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 427.201 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID ADENOSINE-5'-DIPHOSPHATE BMRB 19937 3 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID ADENOSINE-5'-DIPHOSPHATE BMRB 19937 3 ADP 'Three letter code' 19937 3 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 1 ADP $chem_comp_ADP 19937 3 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 19937 _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 $dual-phosphorylated_human_p38_alpha_(apo) . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 19937 1 2 2 $MK2_334-D_peptide . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 19937 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 19937 _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 $dual-phosphorylated_human_p38_alpha_(apo) . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET15b . . . . . . 19937 1 2 2 $MK2_334-D_peptide . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET28b . . . . . . 19937 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_ADP _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_ADP _Chem_comp.Entry_ID 19937 _Chem_comp.ID ADP _Chem_comp.Provenance PDB _Chem_comp.Name ADENOSINE-5'-DIPHOSPHATE _Chem_comp.Type NON-POLYMER _Chem_comp.BMRB_code ADP _Chem_comp.PDB_code ADP _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-11-20 _Chem_comp.Modified_date 2012-11-20 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code ADP _Chem_comp.Number_atoms_all 42 _Chem_comp.Number_atoms_nh 27 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID A _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic yes _Chem_comp.Formula 'C10 H15 N5 O10 P2' _Chem_comp.Formula_weight 427.201 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1PHP _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N SMILES 'OpenEye OEToolkits' 1.5.0 19937 ADP c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 19937 ADP InChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1 InChI InChI 1.03 19937 ADP Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O SMILES_CANONICAL CACTVS 3.341 19937 ADP Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O SMILES CACTVS 3.341 19937 ADP O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O SMILES ACDLabs 10.04 19937 ADP XTWYTFMLZFPYCI-KQYNXXCUSA-N InChIKey InChI 1.03 19937 ADP stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methyl phosphono hydrogen phosphate' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 19937 ADP 'adenosine 5'-(trihydrogen diphosphate)' 'SYSTEMATIC NAME' ACDLabs 10.04 19937 ADP stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID PB PB PB PB . P . . N 0 . . . 1 no no . . . . 44.669 . 2.928 . 38.556 . 1.162 -0.221 -5.685 1 . 19937 ADP O1B O1B O1B O1B . O . . N 0 . . . 1 no no . . . . 46.021 . 3.508 . 38.317 . 1.725 1.133 -5.492 2 . 19937 ADP O2B O2B O2B O2B . O . . N 0 . . . 1 no no . . . . 43.709 . 3.812 . 37.905 . 2.190 -1.112 -6.546 3 . 19937 ADP O3B O3B O3B O3B . O . . N 0 . . . 1 no no . . . . 44.459 . 1.449 . 38.382 . -0.240 -0.113 -6.467 4 . 19937 ADP PA PA PA PA . P . . S 0 . . . 1 no no . . . . 43.230 . 2.955 . 41.110 . -0.105 0.025 -3.446 5 . 19937 ADP O1A O1A O1A O1A . O . . N 0 . . . 1 no no . . . . 41.975 . 3.497 . 40.573 . 0.476 1.376 -3.288 6 . 19937 ADP O2A O2A O2A O2A . O . . N 0 . . . 1 no no . . . . 42.962 . 1.501 . 41.401 . -1.487 0.129 -4.266 7 . 19937 ADP O3A O3A O3A O3A . O . . N 0 . . . 1 no no . . . . 44.522 . 3.210 . 40.212 . 0.925 -0.913 -4.250 8 . 19937 ADP O5' O5' O5' O5* . O . . N 0 . . . 1 no no . . . . 43.462 . 3.832 . 42.407 . -0.389 -0.609 -1.994 9 . 19937 ADP C5' C5' C5' C5* . C . . N 0 . . . 1 no no . . . . 43.735 . 5.246 . 42.335 . -1.307 0.264 -1.333 10 . 19937 ADP C4' C4' C4' C4* . C . . R 0 . . . 1 no no . . . . 43.095 . 5.810 . 43.626 . -1.620 -0.284 0.059 11 . 19937 ADP O4' O4' O4' O4* . O . . N 0 . . . 1 no no . . . . 43.764 . 5.261 . 44.779 . -0.417 -0.348 0.857 12 . 19937 ADP C3' C3' C3' C3* . C . . S 0 . . . 1 no no . . . . 43.337 . 7.325 . 43.617 . -2.550 0.683 0.825 13 . 19937 ADP O3' O3' O3' O3* . O . . N 0 . . . 1 no no . . . . 42.056 . 7.988 . 43.560 . -3.907 0.245 0.739 14 . 19937 ADP C2' C2' C2' C2* . C . . R 0 . . . 1 no no . . . . 43.946 . 7.593 . 45.083 . -2.047 0.611 2.286 15 . 19937 ADP O2' O2' O2' O2* . O . . N 0 . . . 1 no no . . . . 43.554 . 8.726 . 45.877 . -3.080 0.129 3.148 16 . 19937 ADP C1' C1' C1' C1* . C . . R 0 . . . 1 no no . . . . 43.613 . 6.275 . 45.813 . -0.871 -0.388 2.227 17 . 19937 ADP N9 N9 N9 N9 . N . . N 0 . . . 1 yes no . . . . 44.375 . 5.781 . 46.991 . 0.201 0.031 3.132 18 . 19937 ADP C8 C8 C8 C8 . C . . N 0 . . . 1 yes no . . . . 45.711 . 5.486 . 47.062 . 1.231 0.870 2.827 19 . 19937 ADP N7 N7 N7 N7 . N . . N 0 . . . 1 yes no . . . . 46.202 . 5.379 . 48.282 . 2.000 1.027 3.865 20 . 19937 ADP C5 C5 C5 C5 . C . . N 0 . . . 1 yes no . . . . 45.067 . 5.597 . 49.064 . 1.509 0.305 4.902 21 . 19937 ADP C6 C6 C6 C6 . C . . N 0 . . . 1 yes no . . . . 44.883 . 5.623 . 50.499 . 1.910 0.087 6.231 22 . 19937 ADP N6 N6 N6 N6 . N . . N 0 . . . 1 no no . . . . 45.912 . 5.433 . 51.325 . 3.044 0.697 6.738 23 . 19937 ADP N1 N1 N1 N1 . N . . N 0 . . . 1 yes no . . . . 43.626 . 5.852 . 50.896 . 1.171 -0.714 6.991 24 . 19937 ADP C2 C2 C2 C2 . C . . N 0 . . . 1 yes no . . . . 42.590 . 6.076 . 50.067 . 0.088 -1.300 6.516 25 . 19937 ADP N3 N3 N3 N3 . N . . N 0 . . . 1 yes no . . . . 42.675 . 6.067 . 48.735 . -0.321 -1.130 5.277 26 . 19937 ADP C4 C4 C4 C4 . C . . N 0 . . . 1 yes no . . . . 43.951 . 5.821 . 48.304 . 0.353 -0.346 4.442 27 . 19937 ADP HOB2 HOB2 HOB2 2HOB . H . . N 0 . . . 0 no no . . . . 42.847 . 3.442 . 38.057 . 2.304 -0.664 -7.396 28 . 19937 ADP HOB3 HOB3 HOB3 3HOB . H . . N 0 . . . 0 no no . . . . 43.597 . 1.079 . 38.534 . -0.572 -1.016 -6.571 29 . 19937 ADP HOA2 HOA2 HOA2 2HOA . H . . N 0 . . . 0 no no . . . . 43.773 . 1.150 . 41.748 . -1.833 -0.770 -4.346 30 . 19937 ADP H5'1 H5'1 H5'1 1H5* . H . . N 0 . . . 0 no no . . . . 44.812 . 5.500 . 42.206 . -2.227 0.330 -1.913 31 . 19937 ADP H5'2 H5'2 H5'2 2H5* . H . . N 0 . . . 0 no no . . . . 43.385 . 5.735 . 41.396 . -0.862 1.255 -1.242 32 . 19937 ADP H4' H4' H4' H4* . H . . N 0 . . . 1 no no . . . . 42.010 . 5.556 . 43.668 . -2.078 -1.270 -0.015 33 . 19937 ADP H3' H3' H3' H3* . H . . N 0 . . . 1 no no . . . . 43.978 . 7.672 . 42.773 . -2.451 1.696 0.435 34 . 19937 ADP HO3' HO3' HO3' *HO3 . H . . N 0 . . . 0 no no . . . . 42.205 . 8.926 . 43.554 . -4.439 0.884 1.233 35 . 19937 ADP H2' H2' H2' H2* . H . . N 0 . . . 1 no no . . . . 45.014 . 7.879 . 44.941 . -1.699 1.589 2.618 36 . 19937 ADP HO2' HO2' HO2' *HO2 . H . . N 0 . . . 0 no no . . . . 43.913 . 8.884 . 46.742 . -3.807 0.764 3.094 37 . 19937 ADP H1' H1' H1' H1* . H . . N 0 . . . 1 no no . . . . 42.621 . 6.482 . 46.279 . -1.212 -1.391 2.485 38 . 19937 ADP H8 H8 H8 H8 . H . . N 0 . . . 1 no no . . . . 46.358 . 5.341 . 46.181 . 1.387 1.335 1.865 39 . 19937 ADP HN61 HN61 HN61 1HN6 . H . . N 0 . . . 0 no no . . . . 45.782 . 5.451 . 52.336 . 3.308 0.542 7.658 40 . 19937 ADP HN62 HN62 HN62 2HN6 . H . . N 0 . . . 0 no no . . . . 46.639 . 6.107 . 51.086 . 3.577 1.277 6.172 41 . 19937 ADP H2 H2 H2 H2 . H . . N 0 . . . 1 no no . . . . 41.601 . 6.281 . 50.510 . -0.482 -1.944 7.169 42 . 19937 ADP stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . DOUB PB O1B no N 1 . 19937 ADP 2 . SING PB O2B no N 2 . 19937 ADP 3 . SING PB O3B no N 3 . 19937 ADP 4 . SING PB O3A no N 4 . 19937 ADP 5 . SING O2B HOB2 no N 5 . 19937 ADP 6 . SING O3B HOB3 no N 6 . 19937 ADP 7 . DOUB PA O1A no N 7 . 19937 ADP 8 . SING PA O2A no N 8 . 19937 ADP 9 . SING PA O3A no N 9 . 19937 ADP 10 . SING PA O5' no N 10 . 19937 ADP 11 . SING O2A HOA2 no N 11 . 19937 ADP 12 . SING O5' C5' no N 12 . 19937 ADP 13 . SING C5' C4' no N 13 . 19937 ADP 14 . SING C5' H5'1 no N 14 . 19937 ADP 15 . SING C5' H5'2 no N 15 . 19937 ADP 16 . SING C4' O4' no N 16 . 19937 ADP 17 . SING C4' C3' no N 17 . 19937 ADP 18 . SING C4' H4' no N 18 . 19937 ADP 19 . SING O4' C1' no N 19 . 19937 ADP 20 . SING C3' O3' no N 20 . 19937 ADP 21 . SING C3' C2' no N 21 . 19937 ADP 22 . SING C3' H3' no N 22 . 19937 ADP 23 . SING O3' HO3' no N 23 . 19937 ADP 24 . SING C2' O2' no N 24 . 19937 ADP 25 . SING C2' C1' no N 25 . 19937 ADP 26 . SING C2' H2' no N 26 . 19937 ADP 27 . SING O2' HO2' no N 27 . 19937 ADP 28 . SING C1' N9 no N 28 . 19937 ADP 29 . SING C1' H1' no N 29 . 19937 ADP 30 . SING N9 C8 yes N 30 . 19937 ADP 31 . SING N9 C4 yes N 31 . 19937 ADP 32 . DOUB C8 N7 yes N 32 . 19937 ADP 33 . SING C8 H8 no N 33 . 19937 ADP 34 . SING N7 C5 yes N 34 . 19937 ADP 35 . SING C5 C6 yes N 35 . 19937 ADP 36 . DOUB C5 C4 yes N 36 . 19937 ADP 37 . SING C6 N6 no N 37 . 19937 ADP 38 . DOUB C6 N1 yes N 38 . 19937 ADP 39 . SING N6 HN61 no N 39 . 19937 ADP 40 . SING N6 HN62 no N 40 . 19937 ADP 41 . SING N1 C2 yes N 41 . 19937 ADP 42 . DOUB C2 N3 yes N 42 . 19937 ADP 43 . SING C2 H2 no N 43 . 19937 ADP 44 . SING N3 C4 yes N 44 . 19937 ADP stop_ save_ save_chem_comp_TPO _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_TPO _Chem_comp.Entry_ID 19937 _Chem_comp.ID TPO _Chem_comp.Provenance PDB _Chem_comp.Name PHOSPHOTHREONINE _Chem_comp.Type 'L-PEPTIDE LINKING' _Chem_comp.BMRB_code TPO _Chem_comp.PDB_code TPO _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-11-20 _Chem_comp.Modified_date 2012-11-20 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code T _Chem_comp.Three_letter_code TPO _Chem_comp.Number_atoms_all 22 _Chem_comp.Number_atoms_nh 12 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/C4H10NO6P/c1-2(3(5)4(6)7)11-12(8,9)10/h2-3H,5H2,1H3,(H,6,7)(H2,8,9,10)/t2-,3+/m1/s1 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID THR _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms PHOSPHONOTHREONINE _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C4 H10 N O6 P' _Chem_comp.Formula_weight 199.099 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1FMO _Chem_comp.Processing_site EBI _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID CC(C(C(=O)O)N)OP(=O)(O)O SMILES 'OpenEye OEToolkits' 1.5.0 19937 TPO C[C@H]([C@@H](C(=O)O)N)OP(=O)(O)O SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 19937 TPO C[C@@H](O[P](O)(O)=O)[C@H](N)C(O)=O SMILES_CANONICAL CACTVS 3.341 19937 TPO C[CH](O[P](O)(O)=O)[CH](N)C(O)=O SMILES CACTVS 3.341 19937 TPO InChI=1S/C4H10NO6P/c1-2(3(5)4(6)7)11-12(8,9)10/h2-3H,5H2,1H3,(H,6,7)(H2,8,9,10)/t2-,3+/m1/s1 InChI InChI 1.03 19937 TPO O=P(O)(O)OC(C(N)C(=O)O)C SMILES ACDLabs 10.04 19937 TPO USRGIUJOYOXOQJ-GBXIJSLDSA-N InChIKey InChI 1.03 19937 TPO stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '(2S,3R)-2-amino-3-phosphonooxy-butanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 19937 TPO O-phosphono-L-threonine 'SYSTEMATIC NAME' ACDLabs 10.04 19937 TPO stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID N N N N . N . . N 0 . . . 1 no no . . . . 21.891 . 2.133 . -14.748 . 1.153 -1.040 2.377 1 . 19937 TPO CA CA CA CA . C . . S 0 . . . 1 no no . . . . 22.318 . 2.994 . -13.673 . 0.572 0.199 1.844 2 . 19937 TPO CB CB CB CB . C . . R 0 . . . 1 no no . . . . 21.313 . 4.075 . -13.361 . 1.111 0.449 0.434 3 . 19937 TPO CG2 CG2 CG2 CG2 . C . . N 0 . . . 1 no no . . . . 21.837 . 5.045 . -12.302 . 2.634 0.580 0.485 4 . 19937 TPO OG1 OG1 OG1 OG1 . O . . N 0 . . . 1 no no . . . . 20.898 . 4.716 . -14.523 . 0.755 -0.645 -0.412 5 . 19937 TPO P P P P . P . . N 0 . . . 1 no no . . . . 19.424 . 4.424 . -14.993 . -0.142 -0.039 -1.603 6 . 19937 TPO O1P O1P O1P O1P . O . . N 0 . . . 1 no no . . . . 19.358 . 5.014 . -16.321 . 0.644 0.968 -2.350 7 . 19937 TPO O2P O2P O2P O2P . O . . N 0 . . . 1 no no . . . . 19.243 . 2.986 . -14.834 . -0.580 -1.224 -2.601 8 . 19937 TPO O3P O3P O3P O3P . O . . N 0 . . . 1 no no . . . . 18.506 . 5.082 . -14.021 . -1.456 0.656 -0.985 9 . 19937 TPO C C C C . C . . N 0 . . . 1 no no . . . . 22.539 . 2.278 . -12.384 . -0.927 0.070 1.794 10 . 19937 TPO O O O O . O . . N 0 . . . 1 no no . . . . 21.778 . 1.390 . -12.005 . -1.435 -1.012 1.626 11 . 19937 TPO OXT OXT OXT OXT . O . . N 0 . . . 1 no yes . . . . 23.582 . 2.721 . -11.720 . -1.700 1.159 1.935 12 . 19937 TPO H H H H . H . . N 0 . . . 1 no no . . . . 22.570 . 1.402 . -14.958 . 2.154 -0.949 2.296 13 . 19937 TPO H2 H2 H2 2HN . H . . N 0 . . . 1 no yes . . . . 21.663 . 2.673 . -15.582 . 0.877 -1.782 1.751 14 . 19937 TPO HA HA HA HA . H . . N 0 . . . 1 no no . . . . 23.275 . 3.418 . -14.056 . 0.844 1.034 2.490 15 . 19937 TPO HB HB HB HB . H . . N 0 . . . 1 no no . . . . 20.410 . 3.593 . -12.916 . 0.680 1.369 0.039 16 . 19937 TPO HG21 HG21 HG21 1HG2 . H . . N 0 . . . 0 no no . . . . 21.094 . 5.844 . -12.071 . 3.065 -0.339 0.881 17 . 19937 TPO HG22 HG22 HG22 2HG2 . H . . N 0 . . . 0 no no . . . . 22.154 . 4.506 . -11.378 . 3.018 0.758 -0.518 18 . 19937 TPO HG23 HG23 HG23 3HG2 . H . . N 0 . . . 0 no no . . . . 22.821 . 5.477 . -12.598 . 2.906 1.415 1.131 19 . 19937 TPO HOP2 HOP2 HOP2 2HOP . H . . N 0 . . . 0 no no . . . . 18.353 . 2.809 . -15.117 . -1.114 -0.819 -3.298 20 . 19937 TPO HOP3 HOP3 HOP3 3HOP . H . . N 0 . . . 0 no no . . . . 17.616 . 4.905 . -14.304 . -1.938 -0.033 -0.509 21 . 19937 TPO HXT HXT HXT HXT . H . . N 0 . . . 1 no yes . . . . 23.722 . 2.264 . -10.898 . -2.662 1.076 1.902 22 . 19937 TPO stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N CA no N 1 . 19937 TPO 2 . SING N H no N 2 . 19937 TPO 3 . SING N H2 no N 3 . 19937 TPO 4 . SING CA CB no N 4 . 19937 TPO 5 . SING CA C no N 5 . 19937 TPO 6 . SING CA HA no N 6 . 19937 TPO 7 . SING CB CG2 no N 7 . 19937 TPO 8 . SING CB OG1 no N 8 . 19937 TPO 9 . SING CB HB no N 9 . 19937 TPO 10 . SING CG2 HG21 no N 10 . 19937 TPO 11 . SING CG2 HG22 no N 11 . 19937 TPO 12 . SING CG2 HG23 no N 12 . 19937 TPO 13 . SING OG1 P no N 13 . 19937 TPO 14 . DOUB P O1P no N 14 . 19937 TPO 15 . SING P O2P no N 15 . 19937 TPO 16 . SING P O3P no N 16 . 19937 TPO 17 . SING O2P HOP2 no N 17 . 19937 TPO 18 . SING O3P HOP3 no N 18 . 19937 TPO 19 . DOUB C O no N 19 . 19937 TPO 20 . SING C OXT no N 20 . 19937 TPO 21 . SING OXT HXT no N 21 . 19937 TPO stop_ save_ save_chem_comp_PTR _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_PTR _Chem_comp.Entry_ID 19937 _Chem_comp.ID PTR _Chem_comp.Provenance PDB _Chem_comp.Name O-PHOSPHOTYROSINE _Chem_comp.Type 'L-PEPTIDE LINKING' _Chem_comp.BMRB_code PTR _Chem_comp.PDB_code PTR _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-11-20 _Chem_comp.Modified_date 2012-11-20 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code Y _Chem_comp.Three_letter_code PTR _Chem_comp.Number_atoms_all 29 _Chem_comp.Number_atoms_nh 17 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/C9H12NO6P/c10-8(9(11)12)5-6-1-3-7(4-2-6)16-17(13,14)15/h1-4,8H,5,10H2,(H,11,12)(H2,13,14,15)/t8-/m0/s1 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID TYR _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms PHOSPHONOTYROSINE _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic yes _Chem_comp.Formula 'C9 H12 N O6 P' _Chem_comp.Formula_weight 261.168 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID c1cc(ccc1CC(C(=O)O)N)OP(=O)(O)O SMILES 'OpenEye OEToolkits' 1.5.0 19937 PTR c1cc(ccc1C[C@@H](C(=O)O)N)OP(=O)(O)O SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 19937 PTR DCWXELXMIBXGTH-QMMMGPOBSA-N InChIKey InChI 1.03 19937 PTR InChI=1S/C9H12NO6P/c10-8(9(11)12)5-6-1-3-7(4-2-6)16-17(13,14)15/h1-4,8H,5,10H2,(H,11,12)(H2,13,14,15)/t8-/m0/s1 InChI InChI 1.03 19937 PTR N[C@@H](Cc1ccc(O[P](O)(O)=O)cc1)C(O)=O SMILES_CANONICAL CACTVS 3.341 19937 PTR N[CH](Cc1ccc(O[P](O)(O)=O)cc1)C(O)=O SMILES CACTVS 3.341 19937 PTR O=P(Oc1ccc(cc1)CC(C(=O)O)N)(O)O SMILES ACDLabs 10.04 19937 PTR stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '(2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 19937 PTR O-phosphono-L-tyrosine 'SYSTEMATIC NAME' ACDLabs 10.04 19937 PTR stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID N N N N . N . . N 0 . . . 1 no no . . . . 46.366 . 11.139 . -0.665 . 1.298 0.975 3.302 1 . 19937 PTR CA CA CA CA . C . . S 0 . . . 1 no no . . . . 44.969 . 11.616 . -0.749 . -0.036 0.399 3.512 2 . 19937 PTR C C C C . C . . N 0 . . . 1 no no . . . . 44.978 . 13.010 . -1.358 . -0.148 -0.106 4.928 3 . 19937 PTR O O O O . O . . N 0 . . . 1 no no . . . . 43.891 . 13.514 . -1.708 . 0.833 -0.507 5.505 4 . 19937 PTR OXT OXT OXT OXT . O . . N 0 . . . 1 no yes . . . . 46.088 . 13.575 . -1.497 . -1.339 -0.110 5.546 5 . 19937 PTR CB CB CB CB . C . . N 0 . . . 1 no no . . . . 44.332 . 11.618 . 0.644 . -0.250 -0.760 2.538 6 . 19937 PTR CG CG CG CG . C . . N 0 . . . 1 yes no . . . . 44.885 . 12.640 . 1.620 . -0.138 -0.254 1.123 7 . 19937 PTR CD1 CD1 CD1 CD1 . C . . N 0 . . . 1 yes no . . . . 45.913 . 12.302 . 2.506 . 1.089 -0.250 0.487 8 . 19937 PTR CD2 CD2 CD2 CD2 . C . . N 0 . . . 1 yes no . . . . 44.319 . 13.921 . 1.716 . -1.264 0.198 0.461 9 . 19937 PTR CE1 CE1 CE1 CE1 . C . . N 0 . . . 1 yes no . . . . 46.364 . 13.214 . 3.480 . 1.194 0.212 -0.810 10 . 19937 PTR CE2 CE2 CE2 CE2 . C . . N 0 . . . 1 yes no . . . . 44.753 . 14.849 . 2.683 . -1.163 0.668 -0.834 11 . 19937 PTR CZ CZ CZ CZ . C . . N 0 . . . 1 yes no . . . . 45.772 . 14.487 . 3.562 . 0.067 0.673 -1.474 12 . 19937 PTR OH OH OH OH . O . . N 0 . . . 1 no no . . . . 46.216 . 15.385 . 4.594 . 0.168 1.129 -2.750 13 . 19937 PTR P P P P . P . . N 0 . . . 1 no no . . . . 45.382 . 15.884 . 5.757 . -0.065 -0.136 -3.717 14 . 19937 PTR O1P O1P O1P O1P . O . . N 0 . . . 1 no no . . . . 44.096 . 16.422 . 5.355 . -1.409 -0.705 -3.467 15 . 19937 PTR O2P O2P O2P O2P . O . . N 0 . . . 1 no no . . . . 46.274 . 16.938 . 6.218 . 0.040 0.334 -5.253 16 . 19937 PTR O3P O3P O3P O3P . O . . N 0 . . . 1 no no . . . . 45.279 . 14.830 . 6.778 . 1.053 -1.253 -3.419 17 . 19937 PTR H H H 1HN . H . . N 0 . . . 1 no no . . . . 46.360 . 10.204 . -0.256 . 1.963 0.235 3.473 18 . 19937 PTR HN2 HN2 HN2 2HN . H . . N 0 . . . 1 no yes . . . . 46.972 . 11.785 . -0.159 . 1.365 1.204 2.322 19 . 19937 PTR HA HA HA HA . H . . N 0 . . . 1 no no . . . . 44.360 . 10.939 . -1.392 . -0.793 1.164 3.339 20 . 19937 PTR HXT HXT HXT HXT . H . . N 0 . . . 1 no yes . . . . 46.093 . 14.445 . -1.877 . -1.411 -0.435 6.454 21 . 19937 PTR HB2 HB2 HB2 1HB . H . . N 0 . . . 1 no no . . . . 43.226 . 11.735 . 0.556 . 0.506 -1.525 2.711 22 . 19937 PTR HB3 HB3 HB3 2HB . H . . N 0 . . . 1 no no . . . . 44.388 . 10.597 . 1.089 . -1.241 -1.187 2.694 23 . 19937 PTR HD1 HD1 HD1 HD1 . H . . N 0 . . . 1 no no . . . . 46.374 . 11.302 . 2.435 . 1.966 -0.609 1.004 24 . 19937 PTR HD2 HD2 HD2 HD2 . H . . N 0 . . . 1 no no . . . . 43.515 . 14.204 . 1.015 . -2.222 0.194 0.959 25 . 19937 PTR HE1 HE1 HE1 HE1 . H . . N 0 . . . 1 no no . . . . 47.174 . 12.933 . 4.173 . 2.154 0.216 -1.306 26 . 19937 PTR HE2 HE2 HE2 HE2 . H . . N 0 . . . 1 no no . . . . 44.298 . 15.851 . 2.751 . -2.041 1.026 -1.349 27 . 19937 PTR HO2P HO2P HO2P PHO2 . H . . N 0 . . . 0 no no . . . . 45.751 . 17.250 . 6.947 . -0.105 -0.451 -5.797 28 . 19937 PTR HO3P HO3P HO3P PHO3 . H . . N 0 . . . 0 no no . . . . 44.756 . 15.142 . 7.507 . 1.911 -0.843 -3.593 29 . 19937 PTR stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N CA no N 1 . 19937 PTR 2 . SING N H no N 2 . 19937 PTR 3 . SING N HN2 no N 3 . 19937 PTR 4 . SING CA C no N 4 . 19937 PTR 5 . SING CA CB no N 5 . 19937 PTR 6 . SING CA HA no N 6 . 19937 PTR 7 . DOUB C O no N 7 . 19937 PTR 8 . SING C OXT no N 8 . 19937 PTR 9 . SING OXT HXT no N 9 . 19937 PTR 10 . SING CB CG no N 10 . 19937 PTR 11 . SING CB HB2 no N 11 . 19937 PTR 12 . SING CB HB3 no N 12 . 19937 PTR 13 . DOUB CG CD1 yes N 13 . 19937 PTR 14 . SING CG CD2 yes N 14 . 19937 PTR 15 . SING CD1 CE1 yes N 15 . 19937 PTR 16 . SING CD1 HD1 no N 16 . 19937 PTR 17 . DOUB CD2 CE2 yes N 17 . 19937 PTR 18 . SING CD2 HD2 no N 18 . 19937 PTR 19 . DOUB CE1 CZ yes N 19 . 19937 PTR 20 . SING CE1 HE1 no N 20 . 19937 PTR 21 . SING CE2 CZ yes N 21 . 19937 PTR 22 . SING CE2 HE2 no N 22 . 19937 PTR 23 . SING CZ OH no N 23 . 19937 PTR 24 . SING OH P no N 24 . 19937 PTR 25 . DOUB P O1P no N 25 . 19937 PTR 26 . SING P O2P no N 26 . 19937 PTR 27 . SING P O3P no N 27 . 19937 PTR 28 . SING O2P HO2P no N 28 . 19937 PTR 29 . SING O3P HO3P no N 29 . 19937 PTR stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_4 _Sample.Sf_category sample _Sample.Sf_framecode sample_4 _Sample.Entry_ID 19937 _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 'dual-phosphorylated human p38 alpha (apo)' '[U-2H15N13C, ILVM-methyl-1H13C]' . . 1 $dual-phosphorylated_human_p38_alpha_(apo) . . 0.2 . . mM . . . . 19937 1 2 TRIS '[U-100% 2H]' . . . . . . 25 . . mM . . . . 19937 1 3 'potassium chloride' 'natural abundance' . . . . . . 150 . . mM . . . . 19937 1 4 DTT [U-2H] . . . . . . 5 . . mM . . . . 19937 1 5 'MK2 334/D peptide' 'natural abundance' . . 2 $MK2_334-D_peptide . . 0.2 . . mM . . . . 19937 1 6 ADP 'natural abundance' . . 3 $entity_ADP . . 5 . . mM . . . . 19937 1 7 H2O 'natural abundance' . . . . . . 90 . . % . . . . 19937 1 8 D2O '[U-100% 2H]' . . . . . . 10 . . % . . . . 19937 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 19937 _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 temperature 298 . K 19937 1 pH 7.5 . pH 19937 1 pressure 1 . atm 19937 1 'ionic strength' 150 . mM 19937 1 stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 19937 _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' . . 19937 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 19937 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 19937 _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 . . 19937 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 19937 2 stop_ save_ save_CARA _Software.Sf_category software _Software.Sf_framecode CARA _Software.Entry_ID 19937 _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.' . . 19937 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 19937 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 19937 _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 19937 _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 19937 _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 19937 _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 . . . 19937 1 2 spectrometer_2 Bruker Avance . 700 . . . 19937 1 3 spectrometer_3 Bruker Avance . 800 . . . 19937 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 19937 _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_4 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19937 1 2 H(CCCO)NH no . . . . . . . . . . 1 $sample_4 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19937 1 3 HCCH-TOCSY no . . . . . . . . . . 1 $sample_4 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19937 1 4 '3D 1H-13C NOESY aliphatic' no . . . . . . . . . . 1 $sample_4 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19937 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 19937 _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 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 19937 1 C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 19937 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_4 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_4 _Assigned_chem_shift_list.Entry_ID 19937 _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 . . . 19937 1 2 H(CCCO)NH . . . 19937 1 3 HCCH-TOCSY . . . 19937 1 4 '3D 1H-13C NOESY aliphatic' . . . 19937 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 0.31 0.014 . 2 . . . . 13 LEU HD1 . 19937 1 2 . 1 1 20 20 LEU HD12 H 1 0.31 0.014 . 2 . . . . 13 LEU HD1 . 19937 1 3 . 1 1 20 20 LEU HD13 H 1 0.31 0.014 . 2 . . . . 13 LEU HD1 . 19937 1 4 . 1 1 20 20 LEU HD21 H 1 0.587 0.014 . 2 . . . . 13 LEU HD2 . 19937 1 5 . 1 1 20 20 LEU HD22 H 1 0.587 0.014 . 2 . . . . 13 LEU HD2 . 19937 1 6 . 1 1 20 20 LEU HD23 H 1 0.587 0.014 . 2 . . . . 13 LEU HD2 . 19937 1 7 . 1 1 20 20 LEU CD1 C 13 25.421 0.045 . 1 . . . . 13 LEU CD1 . 19937 1 8 . 1 1 20 20 LEU CD2 C 13 24.34 0.045 . 1 . . . . 13 LEU CD2 . 19937 1 9 . 1 1 24 24 ILE HD11 H 1 0.739 0.014 . 1 . . . . 17 ILE HD1 . 19937 1 10 . 1 1 24 24 ILE HD12 H 1 0.739 0.014 . 1 . . . . 17 ILE HD1 . 19937 1 11 . 1 1 24 24 ILE HD13 H 1 0.739 0.014 . 1 . . . . 17 ILE HD1 . 19937 1 12 . 1 1 24 24 ILE CD1 C 13 10.653 0.045 . 1 . . . . 17 ILE CD1 . 19937 1 13 . 1 1 27 27 VAL HG11 H 1 0.865 0.014 . 2 . . . . 20 VAL HG1 . 19937 1 14 . 1 1 27 27 VAL HG12 H 1 0.865 0.014 . 2 . . . . 20 VAL HG1 . 19937 1 15 . 1 1 27 27 VAL HG13 H 1 0.865 0.014 . 2 . . . . 20 VAL HG1 . 19937 1 16 . 1 1 27 27 VAL HG21 H 1 0.636 0.014 . 2 . . . . 20 VAL HG2 . 19937 1 17 . 1 1 27 27 VAL HG22 H 1 0.636 0.014 . 2 . . . . 20 VAL HG2 . 19937 1 18 . 1 1 27 27 VAL HG23 H 1 0.636 0.014 . 2 . . . . 20 VAL HG2 . 19937 1 19 . 1 1 27 27 VAL CG1 C 13 21.572 0.045 . 1 . . . . 20 VAL CG1 . 19937 1 20 . 1 1 27 27 VAL CG2 C 13 19.325 0.045 . 1 . . . . 20 VAL CG2 . 19937 1 21 . 1 1 34 34 LEU HD11 H 1 0.7 0.014 . 2 . . . . 27 LEU HD1 . 19937 1 22 . 1 1 34 34 LEU HD12 H 1 0.7 0.014 . 2 . . . . 27 LEU HD1 . 19937 1 23 . 1 1 34 34 LEU HD13 H 1 0.7 0.014 . 2 . . . . 27 LEU HD1 . 19937 1 24 . 1 1 34 34 LEU HD21 H 1 0.566 0.014 . 2 . . . . 27 LEU HD2 . 19937 1 25 . 1 1 34 34 LEU HD22 H 1 0.566 0.014 . 2 . . . . 27 LEU HD2 . 19937 1 26 . 1 1 34 34 LEU HD23 H 1 0.566 0.014 . 2 . . . . 27 LEU HD2 . 19937 1 27 . 1 1 34 34 LEU CD1 C 13 24.654 0.045 . 1 . . . . 27 LEU CD1 . 19937 1 28 . 1 1 34 34 LEU CD2 C 13 24.392 0.045 . 1 . . . . 27 LEU CD2 . 19937 1 29 . 1 1 55 55 LEU HD11 H 1 0.772 0.014 . 2 . . . . 48 LEU HD1 . 19937 1 30 . 1 1 55 55 LEU HD12 H 1 0.772 0.014 . 2 . . . . 48 LEU HD1 . 19937 1 31 . 1 1 55 55 LEU HD13 H 1 0.772 0.014 . 2 . . . . 48 LEU HD1 . 19937 1 32 . 1 1 55 55 LEU HD21 H 1 0.908 0.014 . 2 . . . . 48 LEU HD2 . 19937 1 33 . 1 1 55 55 LEU HD22 H 1 0.908 0.014 . 2 . . . . 48 LEU HD2 . 19937 1 34 . 1 1 55 55 LEU HD23 H 1 0.908 0.014 . 2 . . . . 48 LEU HD2 . 19937 1 35 . 1 1 55 55 LEU CD1 C 13 24.826 0.045 . 1 . . . . 48 LEU CD1 . 19937 1 36 . 1 1 55 55 LEU CD2 C 13 22.347 0.045 . 1 . . . . 48 LEU CD2 . 19937 1 37 . 1 1 57 57 VAL HG11 H 1 0.767 0.014 . 2 . . . . 50 VAL HG1 . 19937 1 38 . 1 1 57 57 VAL HG12 H 1 0.767 0.014 . 2 . . . . 50 VAL HG1 . 19937 1 39 . 1 1 57 57 VAL HG13 H 1 0.767 0.014 . 2 . . . . 50 VAL HG1 . 19937 1 40 . 1 1 57 57 VAL HG21 H 1 0.603 0.014 . 2 . . . . 50 VAL HG2 . 19937 1 41 . 1 1 57 57 VAL HG22 H 1 0.603 0.014 . 2 . . . . 50 VAL HG2 . 19937 1 42 . 1 1 57 57 VAL HG23 H 1 0.603 0.014 . 2 . . . . 50 VAL HG2 . 19937 1 43 . 1 1 57 57 VAL CG1 C 13 22.138 0.045 . 1 . . . . 50 VAL CG1 . 19937 1 44 . 1 1 57 57 VAL CG2 C 13 18.523 0.045 . 1 . . . . 50 VAL CG2 . 19937 1 45 . 1 1 59 59 VAL HG11 H 1 1.044 0.014 . 2 . . . . 52 VAL HG1 . 19937 1 46 . 1 1 59 59 VAL HG12 H 1 1.044 0.014 . 2 . . . . 52 VAL HG1 . 19937 1 47 . 1 1 59 59 VAL HG13 H 1 1.044 0.014 . 2 . . . . 52 VAL HG1 . 19937 1 48 . 1 1 59 59 VAL HG21 H 1 0.482 0.014 . 2 . . . . 52 VAL HG2 . 19937 1 49 . 1 1 59 59 VAL HG22 H 1 0.482 0.014 . 2 . . . . 52 VAL HG2 . 19937 1 50 . 1 1 59 59 VAL HG23 H 1 0.482 0.014 . 2 . . . . 52 VAL HG2 . 19937 1 51 . 1 1 59 59 VAL CG1 C 13 22.267 0.045 . 1 . . . . 52 VAL CG1 . 19937 1 52 . 1 1 59 59 VAL CG2 C 13 20.211 0.045 . 1 . . . . 52 VAL CG2 . 19937 1 53 . 1 1 62 62 LEU HD11 H 1 0.765 0.014 . 2 . . . . 55 LEU HD1 . 19937 1 54 . 1 1 62 62 LEU HD12 H 1 0.765 0.014 . 2 . . . . 55 LEU HD1 . 19937 1 55 . 1 1 62 62 LEU HD13 H 1 0.765 0.014 . 2 . . . . 55 LEU HD1 . 19937 1 56 . 1 1 62 62 LEU HD21 H 1 0.726 0.014 . 2 . . . . 55 LEU HD2 . 19937 1 57 . 1 1 62 62 LEU HD22 H 1 0.726 0.014 . 2 . . . . 55 LEU HD2 . 19937 1 58 . 1 1 62 62 LEU HD23 H 1 0.726 0.014 . 2 . . . . 55 LEU HD2 . 19937 1 59 . 1 1 62 62 LEU CD1 C 13 25.449 0.045 . 1 . . . . 55 LEU CD1 . 19937 1 60 . 1 1 62 62 LEU CD2 C 13 22.873 0.045 . 1 . . . . 55 LEU CD2 . 19937 1 61 . 1 1 69 69 ILE HD11 H 1 0.935 0.014 . 1 . . . . 62 ILE HD1 . 19937 1 62 . 1 1 69 69 ILE HD12 H 1 0.935 0.014 . 1 . . . . 62 ILE HD1 . 19937 1 63 . 1 1 69 69 ILE HD13 H 1 0.935 0.014 . 1 . . . . 62 ILE HD1 . 19937 1 64 . 1 1 69 69 ILE CD1 C 13 13.704 0.045 . 1 . . . . 62 ILE CD1 . 19937 1 65 . 1 1 70 70 ILE HD11 H 1 0.849 0.014 . 1 . . . . 63 ILE HD1 . 19937 1 66 . 1 1 70 70 ILE HD12 H 1 0.849 0.014 . 1 . . . . 63 ILE HD1 . 19937 1 67 . 1 1 70 70 ILE HD13 H 1 0.849 0.014 . 1 . . . . 63 ILE HD1 . 19937 1 68 . 1 1 70 70 ILE CD1 C 13 12.348 0.045 . 1 . . . . 63 ILE CD1 . 19937 1 69 . 1 1 79 79 LEU HD11 H 1 0.875 0.014 . 2 . . . . 72 LEU HD1 . 19937 1 70 . 1 1 79 79 LEU HD12 H 1 0.875 0.014 . 2 . . . . 72 LEU HD1 . 19937 1 71 . 1 1 79 79 LEU HD13 H 1 0.875 0.014 . 2 . . . . 72 LEU HD1 . 19937 1 72 . 1 1 79 79 LEU HD21 H 1 0.923 0.014 . 2 . . . . 72 LEU HD2 . 19937 1 73 . 1 1 79 79 LEU HD22 H 1 0.923 0.014 . 2 . . . . 72 LEU HD2 . 19937 1 74 . 1 1 79 79 LEU HD23 H 1 0.923 0.014 . 2 . . . . 72 LEU HD2 . 19937 1 75 . 1 1 79 79 LEU CD1 C 13 24.764 0.045 . 1 . . . . 72 LEU CD1 . 19937 1 76 . 1 1 79 79 LEU CD2 C 13 28.551 0.045 . 1 . . . . 72 LEU CD2 . 19937 1 77 . 1 1 81 81 LEU HD11 H 1 0.627 0.014 . 2 . . . . 74 LEU HD1 . 19937 1 78 . 1 1 81 81 LEU HD12 H 1 0.627 0.014 . 2 . . . . 74 LEU HD1 . 19937 1 79 . 1 1 81 81 LEU HD13 H 1 0.627 0.014 . 2 . . . . 74 LEU HD1 . 19937 1 80 . 1 1 81 81 LEU HD21 H 1 0.48 0.014 . 2 . . . . 74 LEU HD2 . 19937 1 81 . 1 1 81 81 LEU HD22 H 1 0.48 0.014 . 2 . . . . 74 LEU HD2 . 19937 1 82 . 1 1 81 81 LEU HD23 H 1 0.48 0.014 . 2 . . . . 74 LEU HD2 . 19937 1 83 . 1 1 81 81 LEU CD1 C 13 25.306 0.045 . 1 . . . . 74 LEU CD1 . 19937 1 84 . 1 1 81 81 LEU CD2 C 13 23.952 0.045 . 1 . . . . 74 LEU CD2 . 19937 1 85 . 1 1 85 85 MET HE1 H 1 1.566 0.014 . 1 . . . . 78 MET HE . 19937 1 86 . 1 1 85 85 MET HE2 H 1 1.566 0.014 . 1 . . . . 78 MET HE . 19937 1 87 . 1 1 85 85 MET HE3 H 1 1.566 0.014 . 1 . . . . 78 MET HE . 19937 1 88 . 1 1 85 85 MET CE C 13 17.877 0.045 . 1 . . . . 78 MET CE . 19937 1 89 . 1 1 90 90 VAL HG11 H 1 1.307 0.014 . 2 . . . . 83 VAL HG1 . 19937 1 90 . 1 1 90 90 VAL HG12 H 1 1.307 0.014 . 2 . . . . 83 VAL HG1 . 19937 1 91 . 1 1 90 90 VAL HG13 H 1 1.307 0.014 . 2 . . . . 83 VAL HG1 . 19937 1 92 . 1 1 90 90 VAL HG21 H 1 0.848 0.014 . 2 . . . . 83 VAL HG2 . 19937 1 93 . 1 1 90 90 VAL HG22 H 1 0.848 0.014 . 2 . . . . 83 VAL HG2 . 19937 1 94 . 1 1 90 90 VAL HG23 H 1 0.848 0.014 . 2 . . . . 83 VAL HG2 . 19937 1 95 . 1 1 90 90 VAL CG1 C 13 22.584 0.045 . 1 . . . . 83 VAL CG1 . 19937 1 96 . 1 1 90 90 VAL CG2 C 13 21.704 0.045 . 1 . . . . 83 VAL CG2 . 19937 1 97 . 1 1 91 91 ILE HD11 H 1 1.187 0.014 . 1 . . . . 84 ILE HD1 . 19937 1 98 . 1 1 91 91 ILE HD12 H 1 1.187 0.014 . 1 . . . . 84 ILE HD1 . 19937 1 99 . 1 1 91 91 ILE HD13 H 1 1.187 0.014 . 1 . . . . 84 ILE HD1 . 19937 1 100 . 1 1 91 91 ILE CD1 C 13 15.151 0.045 . 1 . . . . 84 ILE CD1 . 19937 1 101 . 1 1 96 96 VAL HG11 H 1 0.716 0.014 . 2 . . . . 89 VAL HG1 . 19937 1 102 . 1 1 96 96 VAL HG12 H 1 0.716 0.014 . 2 . . . . 89 VAL HG1 . 19937 1 103 . 1 1 96 96 VAL HG13 H 1 0.716 0.014 . 2 . . . . 89 VAL HG1 . 19937 1 104 . 1 1 96 96 VAL HG21 H 1 0.966 0.014 . 2 . . . . 89 VAL HG2 . 19937 1 105 . 1 1 96 96 VAL HG22 H 1 0.966 0.014 . 2 . . . . 89 VAL HG2 . 19937 1 106 . 1 1 96 96 VAL HG23 H 1 0.966 0.014 . 2 . . . . 89 VAL HG2 . 19937 1 107 . 1 1 96 96 VAL CG1 C 13 20.125 0.045 . 1 . . . . 89 VAL CG1 . 19937 1 108 . 1 1 96 96 VAL CG2 C 13 22.93 0.045 . 1 . . . . 89 VAL CG2 . 19937 1 109 . 1 1 109 109 VAL HG11 H 1 0.795 0.014 . 2 . . . . 102 VAL HG1 . 19937 1 110 . 1 1 109 109 VAL HG12 H 1 0.795 0.014 . 2 . . . . 102 VAL HG1 . 19937 1 111 . 1 1 109 109 VAL HG13 H 1 0.795 0.014 . 2 . . . . 102 VAL HG1 . 19937 1 112 . 1 1 109 109 VAL HG21 H 1 0.956 0.014 . 2 . . . . 102 VAL HG2 . 19937 1 113 . 1 1 109 109 VAL HG22 H 1 0.956 0.014 . 2 . . . . 102 VAL HG2 . 19937 1 114 . 1 1 109 109 VAL HG23 H 1 0.956 0.014 . 2 . . . . 102 VAL HG2 . 19937 1 115 . 1 1 109 109 VAL CG1 C 13 21.171 0.045 . 1 . . . . 102 VAL CG1 . 19937 1 116 . 1 1 109 109 VAL CG2 C 13 22.306 0.045 . 1 . . . . 102 VAL CG2 . 19937 1 117 . 1 1 112 112 VAL HG11 H 1 0.871 0.014 . 2 . . . . 105 VAL HG1 . 19937 1 118 . 1 1 112 112 VAL HG12 H 1 0.871 0.014 . 2 . . . . 105 VAL HG1 . 19937 1 119 . 1 1 112 112 VAL HG13 H 1 0.871 0.014 . 2 . . . . 105 VAL HG1 . 19937 1 120 . 1 1 112 112 VAL HG21 H 1 0.734 0.014 . 2 . . . . 105 VAL HG2 . 19937 1 121 . 1 1 112 112 VAL HG22 H 1 0.734 0.014 . 2 . . . . 105 VAL HG2 . 19937 1 122 . 1 1 112 112 VAL HG23 H 1 0.734 0.014 . 2 . . . . 105 VAL HG2 . 19937 1 123 . 1 1 112 112 VAL CG1 C 13 20.851 0.045 . 1 . . . . 105 VAL CG1 . 19937 1 124 . 1 1 112 112 VAL CG2 C 13 21.145 0.045 . 1 . . . . 105 VAL CG2 . 19937 1 125 . 1 1 116 116 MET HE1 H 1 1.798 0.014 . 1 . . . . 109 MET HE . 19937 1 126 . 1 1 116 116 MET HE2 H 1 1.798 0.014 . 1 . . . . 109 MET HE . 19937 1 127 . 1 1 116 116 MET HE3 H 1 1.798 0.014 . 1 . . . . 109 MET HE . 19937 1 128 . 1 1 116 116 MET CE C 13 17.405 0.045 . 1 . . . . 109 MET CE . 19937 1 129 . 1 1 120 120 LEU HD11 H 1 0.771 0.014 . 2 . . . . 113 LEU HD1 . 19937 1 130 . 1 1 120 120 LEU HD12 H 1 0.771 0.014 . 2 . . . . 113 LEU HD1 . 19937 1 131 . 1 1 120 120 LEU HD13 H 1 0.771 0.014 . 2 . . . . 113 LEU HD1 . 19937 1 132 . 1 1 120 120 LEU HD21 H 1 0.703 0.014 . 2 . . . . 113 LEU HD2 . 19937 1 133 . 1 1 120 120 LEU HD22 H 1 0.703 0.014 . 2 . . . . 113 LEU HD2 . 19937 1 134 . 1 1 120 120 LEU HD23 H 1 0.703 0.014 . 2 . . . . 113 LEU HD2 . 19937 1 135 . 1 1 120 120 LEU CD1 C 13 24.363 0.045 . 1 . . . . 113 LEU CD1 . 19937 1 136 . 1 1 120 120 LEU CD2 C 13 24.932 0.045 . 1 . . . . 113 LEU CD2 . 19937 1 137 . 1 1 123 123 ILE HD11 H 1 0.617 0.014 . 1 . . . . 116 ILE HD1 . 19937 1 138 . 1 1 123 123 ILE HD12 H 1 0.617 0.014 . 1 . . . . 116 ILE HD1 . 19937 1 139 . 1 1 123 123 ILE HD13 H 1 0.617 0.014 . 1 . . . . 116 ILE HD1 . 19937 1 140 . 1 1 123 123 ILE CD1 C 13 10.845 0.045 . 1 . . . . 116 ILE CD1 . 19937 1 141 . 1 1 124 124 VAL HG11 H 1 1.029 0.014 . 2 . . . . 117 VAL HG1 . 19937 1 142 . 1 1 124 124 VAL HG12 H 1 1.029 0.014 . 2 . . . . 117 VAL HG1 . 19937 1 143 . 1 1 124 124 VAL HG13 H 1 1.029 0.014 . 2 . . . . 117 VAL HG1 . 19937 1 144 . 1 1 124 124 VAL HG21 H 1 1.064 0.014 . 2 . . . . 117 VAL HG2 . 19937 1 145 . 1 1 124 124 VAL HG22 H 1 1.064 0.014 . 2 . . . . 117 VAL HG2 . 19937 1 146 . 1 1 124 124 VAL HG23 H 1 1.064 0.014 . 2 . . . . 117 VAL HG2 . 19937 1 147 . 1 1 124 124 VAL CG1 C 13 21.298 0.045 . 1 . . . . 117 VAL CG1 . 19937 1 148 . 1 1 124 124 VAL CG2 C 13 22.78 0.045 . 1 . . . . 117 VAL CG2 . 19937 1 149 . 1 1 129 129 LEU HD11 H 1 0.779 0.014 . 2 . . . . 122 LEU HD1 . 19937 1 150 . 1 1 129 129 LEU HD12 H 1 0.779 0.014 . 2 . . . . 122 LEU HD1 . 19937 1 151 . 1 1 129 129 LEU HD13 H 1 0.779 0.014 . 2 . . . . 122 LEU HD1 . 19937 1 152 . 1 1 129 129 LEU HD21 H 1 0.316 0.014 . 2 . . . . 122 LEU HD2 . 19937 1 153 . 1 1 129 129 LEU HD22 H 1 0.316 0.014 . 2 . . . . 122 LEU HD2 . 19937 1 154 . 1 1 129 129 LEU HD23 H 1 0.316 0.014 . 2 . . . . 122 LEU HD2 . 19937 1 155 . 1 1 129 129 LEU CD1 C 13 25.77 0.045 . 1 . . . . 122 LEU CD1 . 19937 1 156 . 1 1 129 129 LEU CD2 C 13 21.845 0.045 . 1 . . . . 122 LEU CD2 . 19937 1 157 . 1 1 134 134 VAL HG11 H 1 1.159 0.014 . 2 . . . . 127 VAL HG1 . 19937 1 158 . 1 1 134 134 VAL HG12 H 1 1.159 0.014 . 2 . . . . 127 VAL HG1 . 19937 1 159 . 1 1 134 134 VAL HG13 H 1 1.159 0.014 . 2 . . . . 127 VAL HG1 . 19937 1 160 . 1 1 134 134 VAL HG21 H 1 1.04 0.014 . 2 . . . . 127 VAL HG2 . 19937 1 161 . 1 1 134 134 VAL HG22 H 1 1.04 0.014 . 2 . . . . 127 VAL HG2 . 19937 1 162 . 1 1 134 134 VAL HG23 H 1 1.04 0.014 . 2 . . . . 127 VAL HG2 . 19937 1 163 . 1 1 134 134 VAL CG1 C 13 23.134 0.045 . 1 . . . . 127 VAL CG1 . 19937 1 164 . 1 1 134 134 VAL CG2 C 13 23.242 0.045 . 1 . . . . 127 VAL CG2 . 19937 1 165 . 1 1 138 138 ILE HD11 H 1 0.54 0.014 . 1 . . . . 131 ILE HD1 . 19937 1 166 . 1 1 138 138 ILE HD12 H 1 0.54 0.014 . 1 . . . . 131 ILE HD1 . 19937 1 167 . 1 1 138 138 ILE HD13 H 1 0.54 0.014 . 1 . . . . 131 ILE HD1 . 19937 1 168 . 1 1 138 138 ILE CD1 C 13 8.354 0.045 . 1 . . . . 131 ILE CD1 . 19937 1 169 . 1 1 141 141 ILE HD11 H 1 0.607 0.014 . 1 . . . . 134 ILE HD1 . 19937 1 170 . 1 1 141 141 ILE HD12 H 1 0.607 0.014 . 1 . . . . 134 ILE HD1 . 19937 1 171 . 1 1 141 141 ILE HD13 H 1 0.607 0.014 . 1 . . . . 134 ILE HD1 . 19937 1 172 . 1 1 141 141 ILE CD1 C 13 14.867 0.045 . 1 . . . . 134 ILE CD1 . 19937 1 173 . 1 1 142 142 LEU HD11 H 1 0.704 0.014 . 2 . . . . 135 LEU HD1 . 19937 1 174 . 1 1 142 142 LEU HD12 H 1 0.704 0.014 . 2 . . . . 135 LEU HD1 . 19937 1 175 . 1 1 142 142 LEU HD13 H 1 0.704 0.014 . 2 . . . . 135 LEU HD1 . 19937 1 176 . 1 1 142 142 LEU HD21 H 1 0.742 0.014 . 2 . . . . 135 LEU HD2 . 19937 1 177 . 1 1 142 142 LEU HD22 H 1 0.742 0.014 . 2 . . . . 135 LEU HD2 . 19937 1 178 . 1 1 142 142 LEU HD23 H 1 0.742 0.014 . 2 . . . . 135 LEU HD2 . 19937 1 179 . 1 1 142 142 LEU CD1 C 13 28.299 0.045 . 1 . . . . 135 LEU CD1 . 19937 1 180 . 1 1 142 142 LEU CD2 C 13 22.15 0.045 . 1 . . . . 135 LEU CD2 . 19937 1 181 . 1 1 148 148 ILE HD11 H 1 0.765 0.014 . 1 . . . . 141 ILE HD1 . 19937 1 182 . 1 1 148 148 ILE HD12 H 1 0.765 0.014 . 1 . . . . 141 ILE HD1 . 19937 1 183 . 1 1 148 148 ILE HD13 H 1 0.765 0.014 . 1 . . . . 141 ILE HD1 . 19937 1 184 . 1 1 148 148 ILE CD1 C 13 13.741 0.045 . 1 . . . . 141 ILE CD1 . 19937 1 185 . 1 1 154 154 ILE HD11 H 1 0.483 0.014 . 1 . . . . 147 ILE HD1 . 19937 1 186 . 1 1 154 154 ILE HD12 H 1 0.483 0.014 . 1 . . . . 147 ILE HD1 . 19937 1 187 . 1 1 154 154 ILE HD13 H 1 0.483 0.014 . 1 . . . . 147 ILE HD1 . 19937 1 188 . 1 1 154 154 ILE CD1 C 13 13.192 0.045 . 1 . . . . 147 ILE CD1 . 19937 1 189 . 1 1 163 163 LEU HD11 H 1 0.632 0.014 . 2 . . . . 156 LEU HD1 . 19937 1 190 . 1 1 163 163 LEU HD12 H 1 0.632 0.014 . 2 . . . . 156 LEU HD1 . 19937 1 191 . 1 1 163 163 LEU HD13 H 1 0.632 0.014 . 2 . . . . 156 LEU HD1 . 19937 1 192 . 1 1 163 163 LEU HD21 H 1 0.75 0.014 . 2 . . . . 156 LEU HD2 . 19937 1 193 . 1 1 163 163 LEU HD22 H 1 0.75 0.014 . 2 . . . . 156 LEU HD2 . 19937 1 194 . 1 1 163 163 LEU HD23 H 1 0.75 0.014 . 2 . . . . 156 LEU HD2 . 19937 1 195 . 1 1 163 163 LEU CD1 C 13 28.249 0.045 . 1 . . . . 156 LEU CD1 . 19937 1 196 . 1 1 163 163 LEU CD2 C 13 25.731 0.045 . 1 . . . . 156 LEU CD2 . 19937 1 197 . 1 1 165 165 VAL HG11 H 1 0.847 0.014 . 2 . . . . 158 VAL HG1 . 19937 1 198 . 1 1 165 165 VAL HG12 H 1 0.847 0.014 . 2 . . . . 158 VAL HG1 . 19937 1 199 . 1 1 165 165 VAL HG13 H 1 0.847 0.014 . 2 . . . . 158 VAL HG1 . 19937 1 200 . 1 1 165 165 VAL HG21 H 1 0.666 0.014 . 2 . . . . 158 VAL HG2 . 19937 1 201 . 1 1 165 165 VAL HG22 H 1 0.666 0.014 . 2 . . . . 158 VAL HG2 . 19937 1 202 . 1 1 165 165 VAL HG23 H 1 0.666 0.014 . 2 . . . . 158 VAL HG2 . 19937 1 203 . 1 1 165 165 VAL CG1 C 13 21.902 0.045 . 1 . . . . 158 VAL CG1 . 19937 1 204 . 1 1 165 165 VAL CG2 C 13 20.723 0.045 . 1 . . . . 158 VAL CG2 . 19937 1 205 . 1 1 171 171 LEU HD11 H 1 0.68 0.014 . 2 . . . . 164 LEU HD1 . 19937 1 206 . 1 1 171 171 LEU HD12 H 1 0.68 0.014 . 2 . . . . 164 LEU HD1 . 19937 1 207 . 1 1 171 171 LEU HD13 H 1 0.68 0.014 . 2 . . . . 164 LEU HD1 . 19937 1 208 . 1 1 171 171 LEU HD21 H 1 -0.041 0.014 . 2 . . . . 164 LEU HD2 . 19937 1 209 . 1 1 171 171 LEU HD22 H 1 -0.041 0.014 . 2 . . . . 164 LEU HD2 . 19937 1 210 . 1 1 171 171 LEU HD23 H 1 -0.041 0.014 . 2 . . . . 164 LEU HD2 . 19937 1 211 . 1 1 171 171 LEU CD1 C 13 27.175 0.045 . 1 . . . . 164 LEU CD1 . 19937 1 212 . 1 1 171 171 LEU CD2 C 13 22.104 0.045 . 1 . . . . 164 LEU CD2 . 19937 1 213 . 1 1 173 173 ILE HD11 H 1 0.945 0.014 . 1 . . . . 166 ILE HD1 . 19937 1 214 . 1 1 173 173 ILE HD12 H 1 0.945 0.014 . 1 . . . . 166 ILE HD1 . 19937 1 215 . 1 1 173 173 ILE HD13 H 1 0.945 0.014 . 1 . . . . 166 ILE HD1 . 19937 1 216 . 1 1 173 173 ILE CD1 C 13 14.98 0.045 . 1 . . . . 166 ILE CD1 . 19937 1 217 . 1 1 174 174 LEU HD11 H 1 0.208 0.014 . 2 . . . . 167 LEU HD1 . 19937 1 218 . 1 1 174 174 LEU HD12 H 1 0.208 0.014 . 2 . . . . 167 LEU HD1 . 19937 1 219 . 1 1 174 174 LEU HD13 H 1 0.208 0.014 . 2 . . . . 167 LEU HD1 . 19937 1 220 . 1 1 174 174 LEU HD21 H 1 -0.013 0.014 . 2 . . . . 167 LEU HD2 . 19937 1 221 . 1 1 174 174 LEU HD22 H 1 -0.013 0.014 . 2 . . . . 167 LEU HD2 . 19937 1 222 . 1 1 174 174 LEU HD23 H 1 -0.013 0.014 . 2 . . . . 167 LEU HD2 . 19937 1 223 . 1 1 174 174 LEU CD1 C 13 21.391 0.045 . 1 . . . . 167 LEU CD1 . 19937 1 224 . 1 1 174 174 LEU CD2 C 13 23.673 0.045 . 1 . . . . 167 LEU CD2 . 19937 1 225 . 1 1 178 178 LEU HD11 H 1 0.153 0.014 . 2 . . . . 171 LEU HD1 . 19937 1 226 . 1 1 178 178 LEU HD12 H 1 0.153 0.014 . 2 . . . . 171 LEU HD1 . 19937 1 227 . 1 1 178 178 LEU HD13 H 1 0.153 0.014 . 2 . . . . 171 LEU HD1 . 19937 1 228 . 1 1 178 178 LEU HD21 H 1 0.684 0.014 . 2 . . . . 171 LEU HD2 . 19937 1 229 . 1 1 178 178 LEU HD22 H 1 0.684 0.014 . 2 . . . . 171 LEU HD2 . 19937 1 230 . 1 1 178 178 LEU HD23 H 1 0.684 0.014 . 2 . . . . 171 LEU HD2 . 19937 1 231 . 1 1 178 178 LEU CD1 C 13 23.374 0.045 . 1 . . . . 171 LEU CD1 . 19937 1 232 . 1 1 178 178 LEU CD2 C 13 26.765 0.045 . 1 . . . . 171 LEU CD2 . 19937 1 233 . 1 1 186 186 MET HE1 H 1 1.616 0.014 . 1 . . . . 179 MET HE . 19937 1 234 . 1 1 186 186 MET HE2 H 1 1.616 0.014 . 1 . . . . 179 MET HE . 19937 1 235 . 1 1 186 186 MET HE3 H 1 1.616 0.014 . 1 . . . . 179 MET HE . 19937 1 236 . 1 1 186 186 MET CE C 13 18.377 0.045 . 1 . . . . 179 MET CE . 19937 1 237 . 1 1 200 200 ILE HD11 H 1 0.814 0.014 . 1 . . . . 193 ILE HD1 . 19937 1 238 . 1 1 200 200 ILE HD12 H 1 0.814 0.014 . 1 . . . . 193 ILE HD1 . 19937 1 239 . 1 1 200 200 ILE HD13 H 1 0.814 0.014 . 1 . . . . 193 ILE HD1 . 19937 1 240 . 1 1 200 200 ILE CD1 C 13 14.666 0.045 . 1 . . . . 193 ILE CD1 . 19937 1 241 . 1 1 201 201 MET HE1 H 1 1.853 0.014 . 1 . . . . 194 MET HE . 19937 1 242 . 1 1 201 201 MET HE2 H 1 1.853 0.014 . 1 . . . . 194 MET HE . 19937 1 243 . 1 1 201 201 MET HE3 H 1 1.853 0.014 . 1 . . . . 194 MET HE . 19937 1 244 . 1 1 201 201 MET CE C 13 17.313 0.045 . 1 . . . . 194 MET CE . 19937 1 245 . 1 1 205 205 MET HE1 H 1 2.008 0.014 . 1 . . . . 198 MET HE . 19937 1 246 . 1 1 205 205 MET HE2 H 1 2.008 0.014 . 1 . . . . 198 MET HE . 19937 1 247 . 1 1 205 205 MET HE3 H 1 2.008 0.014 . 1 . . . . 198 MET HE . 19937 1 248 . 1 1 205 205 MET CE C 13 17.095 0.045 . 1 . . . . 198 MET CE . 19937 1 249 . 1 1 211 211 VAL HG11 H 1 1.347 0.014 . 2 . . . . 204 VAL HG1 . 19937 1 250 . 1 1 211 211 VAL HG12 H 1 1.347 0.014 . 2 . . . . 204 VAL HG1 . 19937 1 251 . 1 1 211 211 VAL HG13 H 1 1.347 0.014 . 2 . . . . 204 VAL HG1 . 19937 1 252 . 1 1 211 211 VAL HG21 H 1 1.107 0.014 . 2 . . . . 204 VAL HG2 . 19937 1 253 . 1 1 211 211 VAL HG22 H 1 1.107 0.014 . 2 . . . . 204 VAL HG2 . 19937 1 254 . 1 1 211 211 VAL HG23 H 1 1.107 0.014 . 2 . . . . 204 VAL HG2 . 19937 1 255 . 1 1 211 211 VAL CG1 C 13 22.382 0.045 . 1 . . . . 204 VAL CG1 . 19937 1 256 . 1 1 211 211 VAL CG2 C 13 18.322 0.045 . 1 . . . . 204 VAL CG2 . 19937 1 257 . 1 1 213 213 ILE HD11 H 1 0.656 0.014 . 1 . . . . 206 ILE HD1 . 19937 1 258 . 1 1 213 213 ILE HD12 H 1 0.656 0.014 . 1 . . . . 206 ILE HD1 . 19937 1 259 . 1 1 213 213 ILE HD13 H 1 0.656 0.014 . 1 . . . . 206 ILE HD1 . 19937 1 260 . 1 1 213 213 ILE CD1 C 13 8.095 0.045 . 1 . . . . 206 ILE CD1 . 19937 1 261 . 1 1 216 216 VAL HG11 H 1 0.819 0.014 . 2 . . . . 209 VAL HG1 . 19937 1 262 . 1 1 216 216 VAL HG12 H 1 0.819 0.014 . 2 . . . . 209 VAL HG1 . 19937 1 263 . 1 1 216 216 VAL HG13 H 1 0.819 0.014 . 2 . . . . 209 VAL HG1 . 19937 1 264 . 1 1 216 216 VAL HG21 H 1 0.982 0.014 . 2 . . . . 209 VAL HG2 . 19937 1 265 . 1 1 216 216 VAL HG22 H 1 0.982 0.014 . 2 . . . . 209 VAL HG2 . 19937 1 266 . 1 1 216 216 VAL HG23 H 1 0.982 0.014 . 2 . . . . 209 VAL HG2 . 19937 1 267 . 1 1 216 216 VAL CG1 C 13 22.484 0.045 . 1 . . . . 209 VAL CG1 . 19937 1 268 . 1 1 216 216 VAL CG2 C 13 24.639 0.045 . 1 . . . . 209 VAL CG2 . 19937 1 269 . 1 1 219 219 ILE HD11 H 1 0.355 0.014 . 1 . . . . 212 ILE HD1 . 19937 1 270 . 1 1 219 219 ILE HD12 H 1 0.355 0.014 . 1 . . . . 212 ILE HD1 . 19937 1 271 . 1 1 219 219 ILE HD13 H 1 0.355 0.014 . 1 . . . . 212 ILE HD1 . 19937 1 272 . 1 1 219 219 ILE CD1 C 13 13.621 0.045 . 1 . . . . 212 ILE CD1 . 19937 1 273 . 1 1 220 220 MET HE1 H 1 1.744 0.014 . 1 . . . . 213 MET HE . 19937 1 274 . 1 1 220 220 MET HE2 H 1 1.744 0.014 . 1 . . . . 213 MET HE . 19937 1 275 . 1 1 220 220 MET HE3 H 1 1.744 0.014 . 1 . . . . 213 MET HE . 19937 1 276 . 1 1 220 220 MET CE C 13 20.165 0.045 . 1 . . . . 213 MET CE . 19937 1 277 . 1 1 223 223 LEU HD11 H 1 0.792 0.014 . 2 . . . . 216 LEU HD1 . 19937 1 278 . 1 1 223 223 LEU HD12 H 1 0.792 0.014 . 2 . . . . 216 LEU HD1 . 19937 1 279 . 1 1 223 223 LEU HD13 H 1 0.792 0.014 . 2 . . . . 216 LEU HD1 . 19937 1 280 . 1 1 223 223 LEU HD21 H 1 0.674 0.014 . 2 . . . . 216 LEU HD2 . 19937 1 281 . 1 1 223 223 LEU HD22 H 1 0.674 0.014 . 2 . . . . 216 LEU HD2 . 19937 1 282 . 1 1 223 223 LEU HD23 H 1 0.674 0.014 . 2 . . . . 216 LEU HD2 . 19937 1 283 . 1 1 223 223 LEU CD1 C 13 26.123 0.045 . 1 . . . . 216 LEU CD1 . 19937 1 284 . 1 1 223 223 LEU CD2 C 13 21.521 0.045 . 1 . . . . 216 LEU CD2 . 19937 1 285 . 1 1 224 224 LEU HD11 H 1 0.528 0.014 . 2 . . . . 217 LEU HD1 . 19937 1 286 . 1 1 224 224 LEU HD12 H 1 0.528 0.014 . 2 . . . . 217 LEU HD1 . 19937 1 287 . 1 1 224 224 LEU HD13 H 1 0.528 0.014 . 2 . . . . 217 LEU HD1 . 19937 1 288 . 1 1 224 224 LEU HD21 H 1 0.967 0.014 . 2 . . . . 217 LEU HD2 . 19937 1 289 . 1 1 224 224 LEU HD22 H 1 0.967 0.014 . 2 . . . . 217 LEU HD2 . 19937 1 290 . 1 1 224 224 LEU HD23 H 1 0.967 0.014 . 2 . . . . 217 LEU HD2 . 19937 1 291 . 1 1 224 224 LEU CD1 C 13 26.274 0.045 . 1 . . . . 217 LEU CD1 . 19937 1 292 . 1 1 224 224 LEU CD2 C 13 24.232 0.045 . 1 . . . . 217 LEU CD2 . 19937 1 293 . 1 1 229 229 LEU HD11 H 1 0.436 0.014 . 2 . . . . 222 LEU HD1 . 19937 1 294 . 1 1 229 229 LEU HD12 H 1 0.436 0.014 . 2 . . . . 222 LEU HD1 . 19937 1 295 . 1 1 229 229 LEU HD13 H 1 0.436 0.014 . 2 . . . . 222 LEU HD1 . 19937 1 296 . 1 1 229 229 LEU HD21 H 1 0.245 0.014 . 2 . . . . 222 LEU HD2 . 19937 1 297 . 1 1 229 229 LEU HD22 H 1 0.245 0.014 . 2 . . . . 222 LEU HD2 . 19937 1 298 . 1 1 229 229 LEU HD23 H 1 0.245 0.014 . 2 . . . . 222 LEU HD2 . 19937 1 299 . 1 1 229 229 LEU CD1 C 13 21.496 0.045 . 1 . . . . 222 LEU CD1 . 19937 1 300 . 1 1 229 229 LEU CD2 C 13 28.458 0.045 . 1 . . . . 222 LEU CD2 . 19937 1 301 . 1 1 236 236 ILE HD11 H 1 0.453 0.014 . 1 . . . . 229 ILE HD1 . 19937 1 302 . 1 1 236 236 ILE HD12 H 1 0.453 0.014 . 1 . . . . 229 ILE HD1 . 19937 1 303 . 1 1 236 236 ILE HD13 H 1 0.453 0.014 . 1 . . . . 229 ILE HD1 . 19937 1 304 . 1 1 236 236 ILE CD1 C 13 10.403 0.045 . 1 . . . . 229 ILE CD1 . 19937 1 305 . 1 1 242 242 ILE HD11 H 1 0.646 0.014 . 1 . . . . 235 ILE HD1 . 19937 1 306 . 1 1 242 242 ILE HD12 H 1 0.646 0.014 . 1 . . . . 235 ILE HD1 . 19937 1 307 . 1 1 242 242 ILE HD13 H 1 0.646 0.014 . 1 . . . . 235 ILE HD1 . 19937 1 308 . 1 1 242 242 ILE CD1 C 13 14.06 0.045 . 1 . . . . 235 ILE CD1 . 19937 1 309 . 1 1 243 243 LEU HD11 H 1 0.732 0.014 . 2 . . . . 236 LEU HD1 . 19937 1 310 . 1 1 243 243 LEU HD12 H 1 0.732 0.014 . 2 . . . . 236 LEU HD1 . 19937 1 311 . 1 1 243 243 LEU HD13 H 1 0.732 0.014 . 2 . . . . 236 LEU HD1 . 19937 1 312 . 1 1 243 243 LEU HD21 H 1 0.823 0.014 . 2 . . . . 236 LEU HD2 . 19937 1 313 . 1 1 243 243 LEU HD22 H 1 0.823 0.014 . 2 . . . . 236 LEU HD2 . 19937 1 314 . 1 1 243 243 LEU HD23 H 1 0.823 0.014 . 2 . . . . 236 LEU HD2 . 19937 1 315 . 1 1 243 243 LEU CD1 C 13 26.394 0.045 . 1 . . . . 236 LEU CD1 . 19937 1 316 . 1 1 243 243 LEU CD2 C 13 22.849 0.045 . 1 . . . . 236 LEU CD2 . 19937 1 317 . 1 1 245 245 LEU HD11 H 1 0.633 0.014 . 2 . . . . 238 LEU HD1 . 19937 1 318 . 1 1 245 245 LEU HD12 H 1 0.633 0.014 . 2 . . . . 238 LEU HD1 . 19937 1 319 . 1 1 245 245 LEU HD13 H 1 0.633 0.014 . 2 . . . . 238 LEU HD1 . 19937 1 320 . 1 1 245 245 LEU HD21 H 1 0.72 0.014 . 2 . . . . 238 LEU HD2 . 19937 1 321 . 1 1 245 245 LEU HD22 H 1 0.72 0.014 . 2 . . . . 238 LEU HD2 . 19937 1 322 . 1 1 245 245 LEU HD23 H 1 0.72 0.014 . 2 . . . . 238 LEU HD2 . 19937 1 323 . 1 1 245 245 LEU CD1 C 13 23.948 0.045 . 1 . . . . 238 LEU CD1 . 19937 1 324 . 1 1 245 245 LEU CD2 C 13 26.404 0.045 . 1 . . . . 238 LEU CD2 . 19937 1 325 . 1 1 246 246 VAL HG11 H 1 1.446 0.014 . 2 . . . . 239 VAL HG1 . 19937 1 326 . 1 1 246 246 VAL HG12 H 1 1.446 0.014 . 2 . . . . 239 VAL HG1 . 19937 1 327 . 1 1 246 246 VAL HG13 H 1 1.446 0.014 . 2 . . . . 239 VAL HG1 . 19937 1 328 . 1 1 246 246 VAL HG21 H 1 1.279 0.014 . 2 . . . . 239 VAL HG2 . 19937 1 329 . 1 1 246 246 VAL HG22 H 1 1.279 0.014 . 2 . . . . 239 VAL HG2 . 19937 1 330 . 1 1 246 246 VAL HG23 H 1 1.279 0.014 . 2 . . . . 239 VAL HG2 . 19937 1 331 . 1 1 246 246 VAL CG1 C 13 22.209 0.045 . 1 . . . . 239 VAL CG1 . 19937 1 332 . 1 1 246 246 VAL CG2 C 13 19.963 0.045 . 1 . . . . 239 VAL CG2 . 19937 1 333 . 1 1 266 266 ILE HD11 H 1 0.81 0.014 . 1 . . . . 259 ILE HD1 . 19937 1 334 . 1 1 266 266 ILE HD12 H 1 0.81 0.014 . 1 . . . . 259 ILE HD1 . 19937 1 335 . 1 1 266 266 ILE HD13 H 1 0.81 0.014 . 1 . . . . 259 ILE HD1 . 19937 1 336 . 1 1 266 266 ILE CD1 C 13 12.674 0.045 . 1 . . . . 259 ILE CD1 . 19937 1 337 . 1 1 269 269 LEU HD11 H 1 0.794 0.014 . 2 . . . . 262 LEU HD1 . 19937 1 338 . 1 1 269 269 LEU HD12 H 1 0.794 0.014 . 2 . . . . 262 LEU HD1 . 19937 1 339 . 1 1 269 269 LEU HD13 H 1 0.794 0.014 . 2 . . . . 262 LEU HD1 . 19937 1 340 . 1 1 269 269 LEU HD21 H 1 0.75 0.014 . 2 . . . . 262 LEU HD2 . 19937 1 341 . 1 1 269 269 LEU HD22 H 1 0.75 0.014 . 2 . . . . 262 LEU HD2 . 19937 1 342 . 1 1 269 269 LEU HD23 H 1 0.75 0.014 . 2 . . . . 262 LEU HD2 . 19937 1 343 . 1 1 269 269 LEU CD1 C 13 24.935 0.045 . 1 . . . . 262 LEU CD1 . 19937 1 344 . 1 1 269 269 LEU CD2 C 13 23.93 0.045 . 1 . . . . 262 LEU CD2 . 19937 1 345 . 1 1 272 272 MET HE1 H 1 2.076 0.014 . 1 . . . . 265 MET HE . 19937 1 346 . 1 1 272 272 MET HE2 H 1 2.076 0.014 . 1 . . . . 265 MET HE . 19937 1 347 . 1 1 272 272 MET HE3 H 1 2.076 0.014 . 1 . . . . 265 MET HE . 19937 1 348 . 1 1 272 272 MET CE C 13 17.394 0.045 . 1 . . . . 265 MET CE . 19937 1 349 . 1 1 275 275 MET HE1 H 1 2.067 0.014 . 1 . . . . 268 MET HE . 19937 1 350 . 1 1 275 275 MET HE2 H 1 2.067 0.014 . 1 . . . . 268 MET HE . 19937 1 351 . 1 1 275 275 MET HE3 H 1 2.067 0.014 . 1 . . . . 268 MET HE . 19937 1 352 . 1 1 275 275 MET CE C 13 17.054 0.045 . 1 . . . . 268 MET CE . 19937 1 353 . 1 1 280 280 VAL HG11 H 1 -0.158 0.014 . 2 . . . . 273 VAL HG1 . 19937 1 354 . 1 1 280 280 VAL HG12 H 1 -0.158 0.014 . 2 . . . . 273 VAL HG1 . 19937 1 355 . 1 1 280 280 VAL HG13 H 1 -0.158 0.014 . 2 . . . . 273 VAL HG1 . 19937 1 356 . 1 1 280 280 VAL HG21 H 1 0.69 0.014 . 2 . . . . 273 VAL HG2 . 19937 1 357 . 1 1 280 280 VAL HG22 H 1 0.69 0.014 . 2 . . . . 273 VAL HG2 . 19937 1 358 . 1 1 280 280 VAL HG23 H 1 0.69 0.014 . 2 . . . . 273 VAL HG2 . 19937 1 359 . 1 1 280 280 VAL CG1 C 13 19.466 0.045 . 1 . . . . 273 VAL CG1 . 19937 1 360 . 1 1 280 280 VAL CG2 C 13 21.243 0.045 . 1 . . . . 273 VAL CG2 . 19937 1 361 . 1 1 282 282 ILE HD11 H 1 0.863 0.014 . 1 . . . . 275 ILE HD1 . 19937 1 362 . 1 1 282 282 ILE HD12 H 1 0.863 0.014 . 1 . . . . 275 ILE HD1 . 19937 1 363 . 1 1 282 282 ILE HD13 H 1 0.863 0.014 . 1 . . . . 275 ILE HD1 . 19937 1 364 . 1 1 282 282 ILE CD1 C 13 12.238 0.045 . 1 . . . . 275 ILE CD1 . 19937 1 365 . 1 1 287 287 LEU HD11 H 1 0.954 0.014 . 2 . . . . 280 LEU HD1 . 19937 1 366 . 1 1 287 287 LEU HD12 H 1 0.954 0.014 . 2 . . . . 280 LEU HD1 . 19937 1 367 . 1 1 287 287 LEU HD13 H 1 0.954 0.014 . 2 . . . . 280 LEU HD1 . 19937 1 368 . 1 1 287 287 LEU HD21 H 1 0.871 0.014 . 2 . . . . 280 LEU HD2 . 19937 1 369 . 1 1 287 287 LEU HD22 H 1 0.871 0.014 . 2 . . . . 280 LEU HD2 . 19937 1 370 . 1 1 287 287 LEU HD23 H 1 0.871 0.014 . 2 . . . . 280 LEU HD2 . 19937 1 371 . 1 1 287 287 LEU CD1 C 13 25.48 0.045 . 1 . . . . 280 LEU CD1 . 19937 1 372 . 1 1 287 287 LEU CD2 C 13 22.621 0.045 . 1 . . . . 280 LEU CD2 . 19937 1 373 . 1 1 289 289 VAL HG11 H 1 1.006 0.014 . 2 . . . . 282 VAL HG1 . 19937 1 374 . 1 1 289 289 VAL HG12 H 1 1.006 0.014 . 2 . . . . 282 VAL HG1 . 19937 1 375 . 1 1 289 289 VAL HG13 H 1 1.006 0.014 . 2 . . . . 282 VAL HG1 . 19937 1 376 . 1 1 289 289 VAL HG21 H 1 0.983 0.014 . 2 . . . . 282 VAL HG2 . 19937 1 377 . 1 1 289 289 VAL HG22 H 1 0.983 0.014 . 2 . . . . 282 VAL HG2 . 19937 1 378 . 1 1 289 289 VAL HG23 H 1 0.983 0.014 . 2 . . . . 282 VAL HG2 . 19937 1 379 . 1 1 289 289 VAL CG1 C 13 22.768 0.045 . 1 . . . . 282 VAL CG1 . 19937 1 380 . 1 1 289 289 VAL CG2 C 13 23.63 0.045 . 1 . . . . 282 VAL CG2 . 19937 1 381 . 1 1 291 291 LEU HD11 H 1 0.659 0.014 . 2 . . . . 284 LEU HD1 . 19937 1 382 . 1 1 291 291 LEU HD12 H 1 0.659 0.014 . 2 . . . . 284 LEU HD1 . 19937 1 383 . 1 1 291 291 LEU HD13 H 1 0.659 0.014 . 2 . . . . 284 LEU HD1 . 19937 1 384 . 1 1 291 291 LEU HD21 H 1 0.698 0.014 . 2 . . . . 284 LEU HD2 . 19937 1 385 . 1 1 291 291 LEU HD22 H 1 0.698 0.014 . 2 . . . . 284 LEU HD2 . 19937 1 386 . 1 1 291 291 LEU HD23 H 1 0.698 0.014 . 2 . . . . 284 LEU HD2 . 19937 1 387 . 1 1 291 291 LEU CD1 C 13 22.53 0.045 . 1 . . . . 284 LEU CD1 . 19937 1 388 . 1 1 291 291 LEU CD2 C 13 28.344 0.045 . 1 . . . . 284 LEU CD2 . 19937 1 389 . 1 1 292 292 LEU HD11 H 1 -0.037 0.014 . 2 . . . . 285 LEU HD1 . 19937 1 390 . 1 1 292 292 LEU HD12 H 1 -0.037 0.014 . 2 . . . . 285 LEU HD1 . 19937 1 391 . 1 1 292 292 LEU HD13 H 1 -0.037 0.014 . 2 . . . . 285 LEU HD1 . 19937 1 392 . 1 1 292 292 LEU HD21 H 1 0.571 0.014 . 2 . . . . 285 LEU HD2 . 19937 1 393 . 1 1 292 292 LEU HD22 H 1 0.571 0.014 . 2 . . . . 285 LEU HD2 . 19937 1 394 . 1 1 292 292 LEU HD23 H 1 0.571 0.014 . 2 . . . . 285 LEU HD2 . 19937 1 395 . 1 1 292 292 LEU CD1 C 13 24.459 0.045 . 1 . . . . 285 LEU CD1 . 19937 1 396 . 1 1 292 292 LEU CD2 C 13 24.828 0.045 . 1 . . . . 285 LEU CD2 . 19937 1 397 . 1 1 295 295 MET HE1 H 1 1.919 0.014 . 1 . . . . 288 MET HE . 19937 1 398 . 1 1 295 295 MET HE2 H 1 1.919 0.014 . 1 . . . . 288 MET HE . 19937 1 399 . 1 1 295 295 MET HE3 H 1 1.919 0.014 . 1 . . . . 288 MET HE . 19937 1 400 . 1 1 295 295 MET CE C 13 18.665 0.045 . 1 . . . . 288 MET CE . 19937 1 401 . 1 1 296 296 LEU HD11 H 1 0.517 0.014 . 2 . . . . 289 LEU HD1 . 19937 1 402 . 1 1 296 296 LEU HD12 H 1 0.517 0.014 . 2 . . . . 289 LEU HD1 . 19937 1 403 . 1 1 296 296 LEU HD13 H 1 0.517 0.014 . 2 . . . . 289 LEU HD1 . 19937 1 404 . 1 1 296 296 LEU HD21 H 1 -0.273 0.014 . 2 . . . . 289 LEU HD2 . 19937 1 405 . 1 1 296 296 LEU HD22 H 1 -0.273 0.014 . 2 . . . . 289 LEU HD2 . 19937 1 406 . 1 1 296 296 LEU HD23 H 1 -0.273 0.014 . 2 . . . . 289 LEU HD2 . 19937 1 407 . 1 1 296 296 LEU CD1 C 13 26.496 0.045 . 1 . . . . 289 LEU CD1 . 19937 1 408 . 1 1 296 296 LEU CD2 C 13 21.624 0.045 . 1 . . . . 289 LEU CD2 . 19937 1 409 . 1 1 297 297 VAL HG11 H 1 1.078 0.014 . 2 . . . . 290 VAL HG1 . 19937 1 410 . 1 1 297 297 VAL HG12 H 1 1.078 0.014 . 2 . . . . 290 VAL HG1 . 19937 1 411 . 1 1 297 297 VAL HG13 H 1 1.078 0.014 . 2 . . . . 290 VAL HG1 . 19937 1 412 . 1 1 297 297 VAL HG21 H 1 0.962 0.014 . 2 . . . . 290 VAL HG2 . 19937 1 413 . 1 1 297 297 VAL HG22 H 1 0.962 0.014 . 2 . . . . 290 VAL HG2 . 19937 1 414 . 1 1 297 297 VAL HG23 H 1 0.962 0.014 . 2 . . . . 290 VAL HG2 . 19937 1 415 . 1 1 297 297 VAL CG1 C 13 21.886 0.045 . 1 . . . . 290 VAL CG1 . 19937 1 416 . 1 1 297 297 VAL CG2 C 13 21.369 0.045 . 1 . . . . 290 VAL CG2 . 19937 1 417 . 1 1 298 298 LEU HD11 H 1 0.869 0.014 . 2 . . . . 291 LEU HD1 . 19937 1 418 . 1 1 298 298 LEU HD12 H 1 0.869 0.014 . 2 . . . . 291 LEU HD1 . 19937 1 419 . 1 1 298 298 LEU HD13 H 1 0.869 0.014 . 2 . . . . 291 LEU HD1 . 19937 1 420 . 1 1 298 298 LEU HD21 H 1 0.845 0.014 . 2 . . . . 291 LEU HD2 . 19937 1 421 . 1 1 298 298 LEU HD22 H 1 0.845 0.014 . 2 . . . . 291 LEU HD2 . 19937 1 422 . 1 1 298 298 LEU HD23 H 1 0.845 0.014 . 2 . . . . 291 LEU HD2 . 19937 1 423 . 1 1 298 298 LEU CD1 C 13 24.454 0.045 . 1 . . . . 291 LEU CD1 . 19937 1 424 . 1 1 298 298 LEU CD2 C 13 24.003 0.045 . 1 . . . . 291 LEU CD2 . 19937 1 425 . 1 1 304 304 ILE HD11 H 1 0.83 0.014 . 1 . . . . 297 ILE HD1 . 19937 1 426 . 1 1 304 304 ILE HD12 H 1 0.83 0.014 . 1 . . . . 297 ILE HD1 . 19937 1 427 . 1 1 304 304 ILE HD13 H 1 0.83 0.014 . 1 . . . . 297 ILE HD1 . 19937 1 428 . 1 1 304 304 ILE CD1 C 13 13.974 0.045 . 1 . . . . 297 ILE CD1 . 19937 1 429 . 1 1 310 310 LEU HD11 H 1 0.755 0.014 . 2 . . . . 303 LEU HD1 . 19937 1 430 . 1 1 310 310 LEU HD12 H 1 0.755 0.014 . 2 . . . . 303 LEU HD1 . 19937 1 431 . 1 1 310 310 LEU HD13 H 1 0.755 0.014 . 2 . . . . 303 LEU HD1 . 19937 1 432 . 1 1 310 310 LEU HD21 H 1 0.424 0.014 . 2 . . . . 303 LEU HD2 . 19937 1 433 . 1 1 310 310 LEU HD22 H 1 0.424 0.014 . 2 . . . . 303 LEU HD2 . 19937 1 434 . 1 1 310 310 LEU HD23 H 1 0.424 0.014 . 2 . . . . 303 LEU HD2 . 19937 1 435 . 1 1 310 310 LEU CD1 C 13 27.018 0.045 . 1 . . . . 303 LEU CD1 . 19937 1 436 . 1 1 310 310 LEU CD2 C 13 25.11 0.045 . 1 . . . . 303 LEU CD2 . 19937 1 437 . 1 1 326 326 VAL HG11 H 1 1.093 0.014 . 2 . . . . 319 VAL HG1 . 19937 1 438 . 1 1 326 326 VAL HG12 H 1 1.093 0.014 . 2 . . . . 319 VAL HG1 . 19937 1 439 . 1 1 326 326 VAL HG13 H 1 1.093 0.014 . 2 . . . . 319 VAL HG1 . 19937 1 440 . 1 1 326 326 VAL HG21 H 1 0.945 0.014 . 2 . . . . 319 VAL HG2 . 19937 1 441 . 1 1 326 326 VAL HG22 H 1 0.945 0.014 . 2 . . . . 319 VAL HG2 . 19937 1 442 . 1 1 326 326 VAL HG23 H 1 0.945 0.014 . 2 . . . . 319 VAL HG2 . 19937 1 443 . 1 1 326 326 VAL CG1 C 13 22.469 0.045 . 1 . . . . 319 VAL CG1 . 19937 1 444 . 1 1 326 326 VAL CG2 C 13 17.25 0.045 . 1 . . . . 319 VAL CG2 . 19937 1 445 . 1 1 339 339 LEU HD11 H 1 -0.488 0.014 . 2 . . . . 332 LEU HD1 . 19937 1 446 . 1 1 339 339 LEU HD12 H 1 -0.488 0.014 . 2 . . . . 332 LEU HD1 . 19937 1 447 . 1 1 339 339 LEU HD13 H 1 -0.488 0.014 . 2 . . . . 332 LEU HD1 . 19937 1 448 . 1 1 339 339 LEU HD21 H 1 0.281 0.014 . 2 . . . . 332 LEU HD2 . 19937 1 449 . 1 1 339 339 LEU HD22 H 1 0.281 0.014 . 2 . . . . 332 LEU HD2 . 19937 1 450 . 1 1 339 339 LEU HD23 H 1 0.281 0.014 . 2 . . . . 332 LEU HD2 . 19937 1 451 . 1 1 339 339 LEU CD1 C 13 24.378 0.045 . 1 . . . . 332 LEU CD1 . 19937 1 452 . 1 1 339 339 LEU CD2 C 13 22.358 0.045 . 1 . . . . 332 LEU CD2 . 19937 1 453 . 1 1 340 340 LEU HD11 H 1 0.959 0.014 . 2 . . . . 333 LEU HD1 . 19937 1 454 . 1 1 340 340 LEU HD12 H 1 0.959 0.014 . 2 . . . . 333 LEU HD1 . 19937 1 455 . 1 1 340 340 LEU HD13 H 1 0.959 0.014 . 2 . . . . 333 LEU HD1 . 19937 1 456 . 1 1 340 340 LEU HD21 H 1 0.959 0.014 . 2 . . . . 333 LEU HD2 . 19937 1 457 . 1 1 340 340 LEU HD22 H 1 0.959 0.014 . 2 . . . . 333 LEU HD2 . 19937 1 458 . 1 1 340 340 LEU HD23 H 1 0.959 0.014 . 2 . . . . 333 LEU HD2 . 19937 1 459 . 1 1 340 340 LEU CD1 C 13 25.209 0.045 . 1 . . . . 333 LEU CD1 . 19937 1 460 . 1 1 340 340 LEU CD2 C 13 22.094 0.045 . 1 . . . . 333 LEU CD2 . 19937 1 461 . 1 1 341 341 ILE HD11 H 1 1.238 0.014 . 1 . . . . 334 ILE HD1 . 19937 1 462 . 1 1 341 341 ILE HD12 H 1 1.238 0.014 . 1 . . . . 334 ILE HD1 . 19937 1 463 . 1 1 341 341 ILE HD13 H 1 1.238 0.014 . 1 . . . . 334 ILE HD1 . 19937 1 464 . 1 1 341 341 ILE CD1 C 13 13.439 0.045 . 1 . . . . 334 ILE CD1 . 19937 1 465 . 1 1 347 347 LEU HD11 H 1 0.152 0.014 . 2 . . . . 340 LEU HD1 . 19937 1 466 . 1 1 347 347 LEU HD12 H 1 0.152 0.014 . 2 . . . . 340 LEU HD1 . 19937 1 467 . 1 1 347 347 LEU HD13 H 1 0.152 0.014 . 2 . . . . 340 LEU HD1 . 19937 1 468 . 1 1 347 347 LEU HD21 H 1 0.579 0.014 . 2 . . . . 340 LEU HD2 . 19937 1 469 . 1 1 347 347 LEU HD22 H 1 0.579 0.014 . 2 . . . . 340 LEU HD2 . 19937 1 470 . 1 1 347 347 LEU HD23 H 1 0.579 0.014 . 2 . . . . 340 LEU HD2 . 19937 1 471 . 1 1 347 347 LEU CD1 C 13 25.515 0.045 . 1 . . . . 340 LEU CD1 . 19937 1 472 . 1 1 347 347 LEU CD2 C 13 22.748 0.045 . 1 . . . . 340 LEU CD2 . 19937 1 473 . 1 1 352 352 VAL HG11 H 1 0.889 0.014 . 2 . . . . 345 VAL HG1 . 19937 1 474 . 1 1 352 352 VAL HG12 H 1 0.889 0.014 . 2 . . . . 345 VAL HG1 . 19937 1 475 . 1 1 352 352 VAL HG13 H 1 0.889 0.014 . 2 . . . . 345 VAL HG1 . 19937 1 476 . 1 1 352 352 VAL HG21 H 1 1.121 0.014 . 2 . . . . 345 VAL HG2 . 19937 1 477 . 1 1 352 352 VAL HG22 H 1 1.121 0.014 . 2 . . . . 345 VAL HG2 . 19937 1 478 . 1 1 352 352 VAL HG23 H 1 1.121 0.014 . 2 . . . . 345 VAL HG2 . 19937 1 479 . 1 1 352 352 VAL CG1 C 13 21.156 0.045 . 1 . . . . 345 VAL CG1 . 19937 1 480 . 1 1 352 352 VAL CG2 C 13 23.141 0.045 . 1 . . . . 345 VAL CG2 . 19937 1 481 . 1 1 353 353 ILE HD11 H 1 0.506 0.014 . 1 . . . . 346 ILE HD1 . 19937 1 482 . 1 1 353 353 ILE HD12 H 1 0.506 0.014 . 1 . . . . 346 ILE HD1 . 19937 1 483 . 1 1 353 353 ILE HD13 H 1 0.506 0.014 . 1 . . . . 346 ILE HD1 . 19937 1 484 . 1 1 353 353 ILE CD1 C 13 11.828 0.045 . 1 . . . . 346 ILE CD1 . 19937 1 485 . 1 1 356 356 VAL HG11 H 1 0.869 0.014 . 2 . . . . 349 VAL HG1 . 19937 1 486 . 1 1 356 356 VAL HG12 H 1 0.869 0.014 . 2 . . . . 349 VAL HG1 . 19937 1 487 . 1 1 356 356 VAL HG13 H 1 0.869 0.014 . 2 . . . . 349 VAL HG1 . 19937 1 488 . 1 1 356 356 VAL HG21 H 1 0.829 0.014 . 2 . . . . 349 VAL HG2 . 19937 1 489 . 1 1 356 356 VAL HG22 H 1 0.829 0.014 . 2 . . . . 349 VAL HG2 . 19937 1 490 . 1 1 356 356 VAL HG23 H 1 0.829 0.014 . 2 . . . . 349 VAL HG2 . 19937 1 491 . 1 1 356 356 VAL CG1 C 13 20.412 0.045 . 1 . . . . 349 VAL CG1 . 19937 1 492 . 1 1 356 356 VAL CG2 C 13 20.447 0.045 . 1 . . . . 349 VAL CG2 . 19937 1 493 . 1 1 360 360 LEU HD11 H 1 0.925 0.014 . 2 . . . . 353 LEU HD1 . 19937 1 494 . 1 1 360 360 LEU HD12 H 1 0.925 0.014 . 2 . . . . 353 LEU HD1 . 19937 1 495 . 1 1 360 360 LEU HD13 H 1 0.925 0.014 . 2 . . . . 353 LEU HD1 . 19937 1 496 . 1 1 360 360 LEU HD21 H 1 0.877 0.014 . 2 . . . . 353 LEU HD2 . 19937 1 497 . 1 1 360 360 LEU HD22 H 1 0.877 0.014 . 2 . . . . 353 LEU HD2 . 19937 1 498 . 1 1 360 360 LEU HD23 H 1 0.877 0.014 . 2 . . . . 353 LEU HD2 . 19937 1 499 . 1 1 360 360 LEU CD1 C 13 25.049 0.045 . 1 . . . . 353 LEU CD1 . 19937 1 500 . 1 1 360 360 LEU CD2 C 13 23.422 0.045 . 1 . . . . 353 LEU CD2 . 19937 1 501 . 1 1 365 365 MET HE1 H 1 2.105 0.014 . 1 . . . . 358 MET HE . 19937 1 502 . 1 1 365 365 MET HE2 H 1 2.105 0.014 . 1 . . . . 358 MET HE . 19937 1 503 . 1 1 365 365 MET HE3 H 1 2.105 0.014 . 1 . . . . 358 MET HE . 19937 1 504 . 1 1 365 365 MET CE C 13 17.046 0.045 . 1 . . . . 358 MET CE . 19937 1 stop_ save_