data_17471 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 17471 _Entry.Title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for p38 alpha MAPK ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2011-02-15 _Entry.Accession_date 2011-02-15 _Entry.Last_release_date 2011-12-12 _Entry.Original_release_date 2011-12-12 _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 Dana Francis . M. . 17471 2 Wolfgang Peti . . . 17471 3 Rebecca Page . . . 17471 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'Brown University' . 17471 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 17471 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 585 17471 '15N chemical shifts' 273 17471 '1H chemical shifts' 273 17471 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2011-12-12 2011-02-15 original author . 17471 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 6468 'p38 mitogen-activated protein kinase' 17471 PDB 1P38 . 17471 stop_ save_ ############### # Citations # ############### save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 17471 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22057126 _Citation.Full_citation . _Citation.Title 'Structural basis of p38 regulation by hematopoietic tyrosine phosphatase.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Chem. Biol.' _Citation.Journal_name_full 'Nature chemical biology' _Citation.Journal_volume 7 _Citation.Journal_issue 12 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 916 _Citation.Page_last 924 _Citation.Year 2011 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Dana Francis . M. . 17471 1 2 Bartosz Roycki . . . 17471 1 3 Dorothy Koveal . . . 17471 1 4 Gerhard Hummer . . . 17471 1 5 Rebecca Page . . . 17471 1 6 Wolfgang Peti . . . 17471 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 17471 _Assembly.ID 1 _Assembly.Name p38_alpha _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass 40290 _Assembly.Enzyme_commission_number . _Assembly.Details 'monomer, no ligand bound' _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 'p38 alpha' 1 $p38_alpha A . yes native no no . . . 17471 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes BMRB 6468 . . 'solution NMR' . 'Original backbone assignment of the protein used in this study.' 'We have significantly advanced the sequence specific backbone assignment of p38, first published in BMRB6468.' 17471 1 yes PDB 1P38 . . X-ray 2.1 'Crystal structure of the protein used in this study.' . 17471 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'protein kinase' 17471 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_p38_alpha _Entity.Sf_category entity _Entity.Sf_framecode p38_alpha _Entity.Entry_ID 17471 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name p38_alpha _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 ; GHMGSQERPTFYRQELNKTI WEVPERYQNLSPVGSGAYGS VCAAFDTKTGLRVAVKKLSR PFQSIIHAKRTYRELRLLKH MKHENVIGLLDVFTPARSLE EFNDVYLVTHLMGADLNNIV KCQKLTDDHVQFLIYQILRG LKYIHSADIIHRDLKPSNLA VNEDCELKILDFGLARHTDD EMTGYVATRWYRAPEIMLNW MHYNQTVDIWSVGCIMAELL TGRTLFPGTDHIDQLKLILR LVGTPGAELLKKISSESARN YIQSLTQMPKMNFANVFIGA NPLAVDLLEKMLVLDSDKRI TAAQALAHAYFAQYHDPDDE PVADPYDQSFESRDLLIDEW KSLTYDEVISFV ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details 'Residues 1-3 are products of a non-native cloning artifact.' _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 352 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 40290 _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 17940 . p38alpha . . . . . 99.15 349 99.14 99.14 0.00e+00 . . . . 17471 1 2 no BMRB 19930 . Non-phosphorylated_human_p38_alpha_(apo) . . . . . 99.72 367 99.43 99.43 0.00e+00 . . . . 17471 1 3 no BMRB 19934 . Dual-phosphorylated_human_p38_alpha_(apo) . . . . . 99.72 367 98.86 98.86 0.00e+00 . . . . 17471 1 4 no BMRB 19935 . Dual-phosphorylated_human_p38_alpha . . . . . 99.72 367 98.86 98.86 0.00e+00 . . . . 17471 1 5 no BMRB 19936 . dual-phosphorylated_human_p38_alpha_(apo) . . . . . 99.72 367 98.86 98.86 0.00e+00 . . . . 17471 1 6 no BMRB 19937 . dual-phosphorylated_human_p38_alpha_(apo) . . . . . 99.72 367 98.86 98.86 0.00e+00 . . . . 17471 1 7 no PDB 1A9U . "The Complex Structure Of The Map Kinase P38SB203580" . . . . . 100.00 379 99.43 99.43 0.00e+00 . . . . 17471 1 8 no PDB 1BL6 . "The Complex Structure Of The Map Kinase P38SB216995" . . . . . 100.00 379 99.43 99.43 0.00e+00 . . . . 17471 1 9 no PDB 1BL7 . "The Complex Structure Of The Map Kinase P38SB220025" . . . . . 100.00 379 99.43 99.43 0.00e+00 . . . . 17471 1 10 no PDB 1BMK . "The Complex Structure Of The Map Kinase P38SB218655" . . . . . 100.00 379 98.86 98.86 0.00e+00 . . . . 17471 1 11 no PDB 1DI9 . "The Structure Of P38 Mitogen-Activated Protein Kinase In Complex With 4-[3-Methylsulfanylanilino]-6,7- Dimethoxyquinazoline" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 12 no PDB 1IAN . "Human P38 Map Kinase Inhibitor Complex" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 13 no PDB 1KV1 . "P38 Map Kinase In Complex With Inhibitor 1" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 14 no PDB 1KV2 . "Human P38 Map Kinase In Complex With Birb 796" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 15 no PDB 1LEW . "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Nuclear Substrate Mef2a" . . . . . 98.86 360 99.43 99.43 0.00e+00 . . . . 17471 1 16 no PDB 1LEZ . "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Activator Mkk3b" . . . . . 98.86 360 99.43 99.43 0.00e+00 . . . . 17471 1 17 no PDB 1M7Q . "Crystal Structure Of P38 Map Kinase In Complex With A Dihydroquinazolinone Inhibitor" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 18 no PDB 1OUK . "The Structure Of P38 Alpha In Complex With A Pyridinylimidazole Inhibitor" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 19 no PDB 1OUY . "The Structure Of P38 Alpha In Complex With A Dihydropyrido- Pyrimidine Inhibitor" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 20 no PDB 1OVE . "The Structure Of P38 Alpha In Complex With A Dihydroquinolinone" . . . . . 98.86 366 99.71 99.71 0.00e+00 . . . . 17471 1 21 no PDB 1OZ1 . "P38 Mitogen-Activated Kinase In Complex With 4-Azaindole Inhibitor" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 22 no PDB 1P38 . "The Structure Of The Map Kinase P38 At 2.1 Angstoms Resolution" . . . . . 100.00 379 98.86 98.86 0.00e+00 . . . . 17471 1 23 no PDB 1R39 . "The Structure Of P38alpha" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 24 no PDB 1R3C . "The Structure Of P38alpha C162s Mutant" . . . . . 98.86 366 99.71 99.71 0.00e+00 . . . . 17471 1 25 no PDB 1W7H . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 26 no PDB 1W82 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 27 no PDB 1W83 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 28 no PDB 1W84 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 29 no PDB 1WBN . "Fragment Based P38 Inhibitors" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 30 no PDB 1WBO . "Fragment Based P38 Inhibitors" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 31 no PDB 1WBS . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 32 no PDB 1WBT . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-based Lead Generation." . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 33 no PDB 1WBV . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 34 no PDB 1WBW . "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 35 no PDB 1WFC . "Structure Of Apo, Unphosphorylated, P38 Mitogen Activated Protein Kinase P38 (P38 Map Kinase) The Mammalian Homologue Of The Ye" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 36 no PDB 1YQJ . "Crystal Structure Of P38 Alpha In Complex With A Selective Pyridazine Inhibitor" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 37 no PDB 1YW2 . "Mutated Mus Musculus P38 Kinase (Mp38)" . . . . . 98.86 360 98.85 99.14 0.00e+00 . . . . 17471 1 38 no PDB 1YWR . "Crystal Structure Analysis Of Inactive P38 Kinase Domain In Complex With A Monocyclic Pyrazolone Inhibitor" . . . . . 98.86 360 99.14 99.43 0.00e+00 . . . . 17471 1 39 no PDB 1ZYJ . "Human P38 Map Kinase In Complex With Inhibitor 1a" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 40 no PDB 1ZZ2 . "Two Classes Of P38alpha Map Kinase Inhibitors Having A Common Diphenylether Core But Exhibiting Divergent Binding Modes" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 41 no PDB 1ZZL . "Crystal Structure Of P38 With Triazolopyridine" . . . . . 98.30 351 100.00 100.00 0.00e+00 . . . . 17471 1 42 no PDB 2BAJ . "P38alpha Bound To Pyrazolourea" . . . . . 99.72 365 99.43 99.43 0.00e+00 . . . . 17471 1 43 no PDB 2BAK . "P38alpha Map Kinase Bound To Mpaq" . . . . . 99.72 365 99.43 99.43 0.00e+00 . . . . 17471 1 44 no PDB 2BAL . "P38alpha Map Kinase Bound To Pyrazoloamine" . . . . . 99.72 365 99.15 99.15 0.00e+00 . . . . 17471 1 45 no PDB 2BAQ . "P38alpha Bound To Ro3201195" . . . . . 99.72 365 98.86 99.15 0.00e+00 . . . . 17471 1 46 no PDB 2EWA . "Dual Binding Mode Of Pyridinylimidazole To Map Kinase P38" . . . . . 100.00 379 99.43 99.43 0.00e+00 . . . . 17471 1 47 no PDB 2FSL . "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-A" . . . . . 99.72 367 98.86 98.86 0.00e+00 . . . . 17471 1 48 no PDB 2FSM . "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-B" . . . . . 99.72 367 98.86 98.86 0.00e+00 . . . . 17471 1 49 no PDB 2FSO . "Mitogen Activated Protein Kinase P38alpha (D176a) Activating Mutant" . . . . . 99.72 367 99.15 99.15 0.00e+00 . . . . 17471 1 50 no PDB 2FST . "Mitogen Activated Protein Kinase P38alpha (d176a+f327l) Activating Mutant" . . . . . 99.72 367 98.86 98.86 0.00e+00 . . . . 17471 1 51 no PDB 2GFS . "P38 Kinase Crystal Structure In Complex With Ro3201195" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 52 no PDB 2GHL . "Mutant Mus Musculus P38 Kinase Domain In Complex With Inhibitor Pg-874743" . . . . . 98.01 348 98.84 99.13 0.00e+00 . . . . 17471 1 53 no PDB 2GHM . "Mutated Map Kinase P38 (Mus Musculus) In Complex With Inhbitor Pg-895449" . . . . . 98.01 348 98.84 99.13 0.00e+00 . . . . 17471 1 54 no PDB 2GTM . "Mutated Mouse P38 Map Kinase Domain In Complex With Inhibitor Pg-892579" . . . . . 98.01 348 99.42 99.42 0.00e+00 . . . . 17471 1 55 no PDB 2GTN . "Mutated Map Kinase P38 (mus Musculus) In Complex With Inhbitor Pg-951717" . . . . . 98.01 348 99.42 99.42 0.00e+00 . . . . 17471 1 56 no PDB 2I0H . "The Structure Of P38alpha In Complex With An Arylpyridazinone" . . . . . 98.86 366 99.71 99.71 0.00e+00 . . . . 17471 1 57 no PDB 2LGC . "Joint Nmr And X-Ray Refinement Reveals The Structure Of A Novel Dibenzo[a,D]cycloheptenone InhibitorP38 MAP KINASE COMPLEX IN S" . . . . . 98.86 359 100.00 100.00 0.00e+00 . . . . 17471 1 58 no PDB 2NPQ . "A Novel Lipid Binding Site In The P38 Alpha Map Kinase" . . . . . 99.72 367 99.43 99.43 0.00e+00 . . . . 17471 1 59 no PDB 2OKR . "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 60 no PDB 2ONL . "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 61 no PDB 2OZA . "Structure Of P38alpha Complex" . . . . . 99.72 366 98.86 98.86 0.00e+00 . . . . 17471 1 62 no PDB 2PUU . "Crystal Structure Of P38 Complex With 1-(5-Tert-Butyl-2-P- Tolyl-2h-Pyrazol-3-Yl)-3-[4-(6-Morpholin-4-Ylmethyl- Pyridin-3-Yl)na" . . . . . 98.01 348 98.84 98.84 0.00e+00 . . . . 17471 1 63 no PDB 2QD9 . "P38 Alpha Map Kinase Inhibitor Based On Heterobicyclic Scaffolds" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 64 no PDB 2RG5 . "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11b" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 65 no PDB 2RG6 . "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11j" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 66 no PDB 2Y8O . "Crystal Structure Of Human P38alpha Complexed With A Mapk Docking Peptide" . . . . . 98.86 362 99.71 99.71 0.00e+00 . . . . 17471 1 67 no PDB 2YIS . "Triazolopyridine Inhibitors Of P38 Kinase." . . . . . 98.86 359 100.00 100.00 0.00e+00 . . . . 17471 1 68 no PDB 2YIW . "Triazolopyridine Inhibitors Of P38 Kinase" . . . . . 98.86 359 100.00 100.00 0.00e+00 . . . . 17471 1 69 no PDB 2YIX . "Triazolopyridine Inhibitors Of P38" . . . . . 98.30 351 100.00 100.00 0.00e+00 . . . . 17471 1 70 no PDB 2ZAZ . "Crystal Structure Of P38 In Complex With 4-Anilino Quinoline Inhibitor" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 71 no PDB 2ZB0 . "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 72 no PDB 2ZB1 . "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 73 no PDB 3BV2 . "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 30" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 74 no PDB 3BV3 . "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 2" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 75 no PDB 3BX5 . "P38 Alpha Map Kinase Complexed With Bms-640994" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 76 no PDB 3C5U . "P38 Alpha Map Kinase Complexed With A Benzothiazole Based Inhibitor" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 77 no PDB 3CTQ . "Structure Of Map Kinase P38 In Complex With A 1-O-Tolyl-1,2, 3-Triazole-4-Carboxamide" . . . . . 98.01 348 98.84 98.84 0.00e+00 . . . . 17471 1 78 no PDB 3D7Z . "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 79 no PDB 3D83 . "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" . . . . . 98.86 360 99.43 99.43 0.00e+00 . . . . 17471 1 80 no PDB 3DS6 . "P38 Complex With A Phthalazine Inhibitor" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 81 no PDB 3DT1 . "P38 Complexed With A Quinazoline Inhibitor" . . . . . 98.86 383 100.00 100.00 0.00e+00 . . . . 17471 1 82 no PDB 3E92 . "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" . . . . . 99.72 371 99.15 99.15 0.00e+00 . . . . 17471 1 83 no PDB 3E93 . "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" . . . . . 99.72 371 99.15 99.15 0.00e+00 . . . . 17471 1 84 no PDB 3FC1 . "Crystal Structure Of P38 Kinase Bound To Pyrimido-Pyridazinone Inhibitor" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 85 no PDB 3FI4 . "P38 Kinase Crystal Structure In Complex With Ro4499" . . . . . 98.86 372 99.71 100.00 0.00e+00 . . . . 17471 1 86 no PDB 3FKL . "P38 Kinase Crystal Structure In Complex With Ro9552" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 87 no PDB 3FKN . "P38 Kinase Crystal Structure In Complex With Ro7125" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 88 no PDB 3FKO . "P38 Kinase Crystal Structure In Complex With Ro3668" . . . . . 98.86 372 99.71 100.00 0.00e+00 . . . . 17471 1 89 no PDB 3FL4 . "P38 Kinase Crystal Structure In Complex With Ro5634" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 90 no PDB 3FLN . "P38 Kinase Crystal Structure In Complex With R1487" . . . . . 98.86 372 99.71 100.00 0.00e+00 . . . . 17471 1 91 no PDB 3FLQ . "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-((S)-2-Methanesulfonyl-1-Methyl- Ethylamino)-8-Methyl-" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 92 no PDB 3FLS . "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-((R)-2-Methanesulfonyl-1-Methyl- Ethylamino)-8-Methyl-" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 93 no PDB 3FLW . "P38 Kinase Crystal Structure In Complex With Pamapimod" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 94 no PDB 3FLY . "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-Isopropylamino-8-Methyl-8h-Pyrido[2,3- D]pyrimidin-7-O" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 95 no PDB 3FLZ . "P38 Kinase Crystal Structure In Complex With 8-Methyl-6-Phenoxy-2- (Tetrahydro-Pyran-4-Ylamino)-8h-Pyrido[2,3-D]pyrimidin-7-One" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 96 no PDB 3FMH . "P38 Kinase Crystal Structure In Complex With 6-(2,4-Difluoro-Phenoxy)- 8-Methyl-2-((R)-1-Methyl-2-Tetrazol-2-Yl-Ethylamino)-8h-" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 97 no PDB 3FMJ . "P38 Kinase Crystal Structure In Complex With 4-(5-Methyl-3-Phenyl- Isoxazol-4-Yl)-Pyrimidin-2-Ylamine" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 98 no PDB 3FMK . "P38 Kinase Crystal Structure In Complex With 6-(2,4-Difluoro-Phenoxy)- 8-Methyl-2-((S)-1-Methyl-2-Tetrazol-2-Yl-Ethylamino)-8h-" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 99 no PDB 3FML . "P38 Kinase Crystal Structure In Complex With Ro6224" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 100 no PDB 3FMM . "P38 Kinase Crystal Structure In Complex With Ro6226" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 101 no PDB 3FMN . "P38 Kinase Crystal Structure In Complex With Ro2530" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 102 no PDB 3FSF . "P38 Kinase Crystal Structure In Complex With 3-(2,6- Dichloro-Phenyl)-7-[4-(2-Diethylamino-Ethoxy)-Phenylamino]- 1-Methyl-3,4-D" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 103 no PDB 3FSK . "P38 Kinase Crystal Structure In Complex With Ro6257" . . . . . 98.86 372 100.00 100.00 0.00e+00 . . . . 17471 1 104 no PDB 3GC7 . "The Structure Of P38alpha In Complex With A Dihydroquinazolinone" . . . . . 98.86 366 99.71 99.71 0.00e+00 . . . . 17471 1 105 no PDB 3GCP . "Human P38 Map Kinase In Complex With Sb203580" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 106 no PDB 3GCQ . "Human P38 Map Kinase In Complex With Rl45" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 107 no PDB 3GCS . "Human P38 Map Kinase In Complex With Sorafenib" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 108 no PDB 3GCU . "Human P38 Map Kinase In Complex With Rl48" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 109 no PDB 3GCV . "Human P38 Map Kinase In Complex With Rl62" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 110 no PDB 3GFE . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 111 no PDB 3GI3 . "Crystal Structure Of A N-Phenyl-N'-Naphthylurea Analog In Complex With P38 Map Kinase" . . . . . 98.86 360 99.43 99.43 0.00e+00 . . . . 17471 1 112 no PDB 3HA8 . "The Complex Structure Of The Map Kinase P38COMPOUND 14B" . . . . . 100.00 379 99.43 99.43 0.00e+00 . . . . 17471 1 113 no PDB 3HEC . "P38 In Complex With Imatinib" . . . . . 98.01 348 100.00 100.00 0.00e+00 . . . . 17471 1 114 no PDB 3HEG . "P38 In Complex With Sorafenib" . . . . . 98.01 348 100.00 100.00 0.00e+00 . . . . 17471 1 115 no PDB 3HL7 . "Crystal Structure Of Human P38alpha Complexed With Sd-0006" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 116 no PDB 3HLL . "Crystal Structure Of Human P38alpha Complexed With Ph-797804" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 117 no PDB 3HP2 . "Crystal Structure Of Human P38alpha Complexed With A Pyridinone Compound" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 118 no PDB 3HP5 . "Crystal Structure Of Human P38alpha Complexed With A Pyrimidopyridazinone Compound" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 119 no PDB 3HRB . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 98.86 359 100.00 100.00 0.00e+00 . . . . 17471 1 120 no PDB 3HUB . "Human P38 Map Kinase In Complex With Scios-469" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 121 no PDB 3HUC . "Human P38 Map Kinase In Complex With Rl40" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 122 no PDB 3HV3 . "Human P38 Map Kinase In Complex With Rl49" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 123 no PDB 3HV4 . "Human P38 Map Kinase In Complex With Rl51" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 124 no PDB 3HV5 . "Human P38 Map Kinase In Complex With Rl24" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 125 no PDB 3HV6 . "Human P38 Map Kinase In Complex With Rl39" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 126 no PDB 3HV7 . "Human P38 Map Kinase In Complex With Rl38" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 127 no PDB 3HVC . "Crystal Structure Of Human P38alpha Map Kinase" . . . . . 98.86 362 100.00 100.00 0.00e+00 . . . . 17471 1 128 no PDB 3IPH . "Crystal Structure Of P38 In Complex With A Biphenylamide Inhibitor" . . . . . 98.86 360 99.43 99.43 0.00e+00 . . . . 17471 1 129 no PDB 3ITZ . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridazine Inhibitor" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 130 no PDB 3IW5 . "Human P38 Map Kinase In Complex With An Indole Derivative" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 131 no PDB 3IW6 . "Human P38 Map Kinase In Complex With A Benzylpiperazin- Pyrrol" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 132 no PDB 3IW7 . "Human P38 Map Kinase In Complex With An Imidazo-Pyridine" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 133 no PDB 3IW8 . "Structure Of Inactive Human P38 Map Kinase In Complex With A Thiazole-Urea" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 134 no PDB 3K3I . "P38alpha Bound To Novel Dgf-Out Compound Pf-00215955" . . . . . 98.01 350 100.00 100.00 0.00e+00 . . . . 17471 1 135 no PDB 3K3J . "P38alpha Bound To Novel Dfg-Out Compound Pf-00416121" . . . . . 98.86 362 100.00 100.00 0.00e+00 . . . . 17471 1 136 no PDB 3KF7 . "Crystal Structure Of Human P38alpha Complexed With A Triazolopyrimidine Compound" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 137 no PDB 3KQ7 . "Structure Of Human P38alpha With N-[4-Methyl-3-(6-{[2-(1- Methylpyrrolidin-2-Yl)ethyl]amino}pyridine-3-Amido)phenyl]- 2-(Morpho" . . . . . 100.00 380 99.43 99.43 0.00e+00 . . . . 17471 1 138 no PDB 3L8S . "Human P38 Map Kinase In Complex With Cp-547632" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 139 no PDB 3L8X . "P38 Alpha Kinase Complexed With A Pyrazolo-Pyrimidine Based Inhibitor" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 140 no PDB 3LFA . "Human P38 Map Kinase In Complex With Dasatinib" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 141 no PDB 3LFB . "Human P38 Map Kinase In Complex With Rl98" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 142 no PDB 3LFC . "Human P38 Map Kinase In Complex With Rl99" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 143 no PDB 3LFD . "Human P38 Map Kinase In Complex With Rl113" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 144 no PDB 3LFE . "Human P38 Map Kinase In Complex With Rl116" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 145 no PDB 3LFF . "Human P38 Map Kinase In Complex With Rl166" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 146 no PDB 3LHJ . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor." . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 147 no PDB 3MGY . "Mutagenesis Of P38 Map Kinase Eshtablishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out " . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 148 no PDB 3MH0 . "Mutagenesis Of P38 Map Kinase Eshtablishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out " . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 149 no PDB 3MH1 . "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 150 no PDB 3MH2 . "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" . . . . . 98.86 360 99.71 100.00 0.00e+00 . . . . 17471 1 151 no PDB 3MH3 . "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 152 no PDB 3MPA . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 153 no PDB 3MPT . "Crystal Structure Of P38 Kinase In Complex With A Pyrrole-2- Carboxamide Inhibitor" . . . . . 99.72 371 99.43 99.43 0.00e+00 . . . . 17471 1 154 no PDB 3MVL . "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7k" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 155 no PDB 3MVM . "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7v" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 156 no PDB 3MW1 . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 98.86 359 100.00 100.00 0.00e+00 . . . . 17471 1 157 no PDB 3NEW . "P38-Alpha Complexed With Compound 10" . . . . . 98.86 366 99.71 99.71 0.00e+00 . . . . 17471 1 158 no PDB 3NNU . "Crystal Structure Of P38 Alpha In Complex With Dp1376" . . . . . 98.86 354 100.00 100.00 0.00e+00 . . . . 17471 1 159 no PDB 3NNV . "Crystal Structure Of P38 Alpha In Complex With Dp437" . . . . . 98.86 354 100.00 100.00 0.00e+00 . . . . 17471 1 160 no PDB 3NNW . "Crystal Structure Of P38 Alpha In Complex With Dp802" . . . . . 98.86 354 100.00 100.00 0.00e+00 . . . . 17471 1 161 no PDB 3NNX . "Crystal Structure Of Phosphorylated P38 Alpha In Complex With Dp802" . . . . . 98.86 354 99.71 99.71 0.00e+00 . . . . 17471 1 162 no PDB 3NWW . "P38 Alpha Kinase Complexed With A 2-aminothiazol-5-yl-pyrimidine Based Inhibitor" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 163 no PDB 3O8P . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 164 no PDB 3O8T . "Conformational Plasticity Of P38 Map Kinase Dfg-Motif Mutants In Response To Inhibitor Binding" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 165 no PDB 3O8U . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 98.86 360 99.71 100.00 0.00e+00 . . . . 17471 1 166 no PDB 3OBG . "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 167 no PDB 3OBJ . "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 168 no PDB 3OC1 . "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 169 no PDB 3OCG . "P38 Alpha Kinase Complexed With A 5-Amino-Pyrazole Based Inhibitor" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 170 no PDB 3OD6 . "Crystal Structure Of P38alpha Y323t Active Mutant" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 171 no PDB 3ODY . "Crystal Structure Of P38alpha Y323q Active Mutant" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 172 no PDB 3ODZ . "Crystal Structure Of P38alpha Y323r Active Mutant" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 173 no PDB 3OEF . "Crystal Structure Of Y323f Inactive Mutant Of P38alpha Map Kinase" . . . . . 98.86 360 99.71 100.00 0.00e+00 . . . . 17471 1 174 no PDB 3P4K . "The Third Conformation Of P38a Map Kinase Observed In Phosphorylated P38a And In Solution" . . . . . 99.43 370 98.86 99.14 0.00e+00 . . . . 17471 1 175 no PDB 3P5K . "P38 Inhibitor-Bound" . . . . . 99.72 366 98.86 98.86 0.00e+00 . . . . 17471 1 176 no PDB 3P78 . "P38 Inhibitor-Bound" . . . . . 99.72 366 98.86 98.86 0.00e+00 . . . . 17471 1 177 no PDB 3P79 . "P38 Inhibitor-Bound" . . . . . 99.72 366 98.86 98.86 0.00e+00 . . . . 17471 1 178 no PDB 3P7A . "P38 Inhibitor-Bound" . . . . . 99.72 366 98.86 98.86 0.00e+00 . . . . 17471 1 179 no PDB 3P7B . "P38 Inhibitor-Bound" . . . . . 99.72 366 98.86 98.86 0.00e+00 . . . . 17471 1 180 no PDB 3P7C . "P38 Inhibitor-Bound" . . . . . 99.72 366 98.86 98.86 0.00e+00 . . . . 17471 1 181 no PDB 3PG3 . "Human P38 Map Kinase In Complex With Rl182" . . . . . 99.15 360 98.85 98.85 0.00e+00 . . . . 17471 1 182 no PDB 3PY3 . "Crystal Structure Of Phosphorylated P38alpha Map Kinase" . . . . . 100.00 380 98.01 98.01 0.00e+00 . . . . 17471 1 183 no PDB 3QUD . "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino-Benzophenone" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 184 no PDB 3QUE . "Human P38 Map Kinase In Complex With Skepinone-l" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 185 no PDB 3RIN . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 186 no PDB 3ROC . "Crystal Structure Of Human P38 Alpha Complexed With A Pyrimidinone Compound" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 187 no PDB 3S3I . "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" . . . . . 98.30 349 100.00 100.00 0.00e+00 . . . . 17471 1 188 no PDB 3S4Q . "P38 Alpha Kinase Complexed With A Pyrazolo-Triazine Based Inhibitor" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 189 no PDB 3TG1 . "Crystal Structure Of P38alpha In Complex With A Mapk Docking Partner" . . . . . 100.00 380 98.58 98.58 0.00e+00 . . . . 17471 1 190 no PDB 3U8W . "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Triazolopyridazinone Inhibitor" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 191 no PDB 3UVP . "Human P38 Map Kinase In Complex With A Benzamide Substituted Benzosuberone" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 192 no PDB 3UVQ . "Human P38 Map Kinase In Complex With A Dibenzosuberone Derivative" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 193 no PDB 3UVR . "Human P38 Map Kinase In Complex With Km064" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 194 no PDB 3ZS5 . "Structural Basis For Kinase Selectivity Of Three Clinical P38alpha Inhibitors" . . . . . 98.86 362 100.00 100.00 0.00e+00 . . . . 17471 1 195 no PDB 3ZSG . "X-Ray Structure Of P38alpha Bound To Tak-715" . . . . . 98.86 362 100.00 100.00 0.00e+00 . . . . 17471 1 196 no PDB 3ZSH . "X-Ray Structure Of P38alpha Bound To Scio-469" . . . . . 98.86 362 100.00 100.00 0.00e+00 . . . . 17471 1 197 no PDB 3ZSI . "X-Ray Structure Of P38alpha Bound To Vx-745" . . . . . 98.86 362 100.00 100.00 0.00e+00 . . . . 17471 1 198 no PDB 3ZYA . "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino- Dibenzosuberone" . . . . . 98.86 366 100.00 100.00 0.00e+00 . . . . 17471 1 199 no PDB 4A9Y . "P38alpha Map Kinase Bound To Cmpd 8" . . . . . 99.72 365 99.43 99.43 0.00e+00 . . . . 17471 1 200 no PDB 4AA0 . "P38alpha Map Kinase Bound To Cmpd 2" . . . . . 99.72 365 99.43 99.43 0.00e+00 . . . . 17471 1 201 no PDB 4AA4 . "P38alpha Map Kinase Bound To Cmpd 22" . . . . . 99.72 365 99.43 99.43 0.00e+00 . . . . 17471 1 202 no PDB 4AA5 . "P38alpha Map Kinase Bound To Cmpd 33" . . . . . 99.72 365 99.15 99.15 0.00e+00 . . . . 17471 1 203 no PDB 4AAC . "P38alpha Map Kinase Bound To Cmpd 29" . . . . . 99.72 365 99.43 99.43 0.00e+00 . . . . 17471 1 204 no PDB 4DLI . "Human P38 Map Kinase In Complex With Rl87" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 205 no PDB 4DLJ . "Human P38 Map Kinase In Complex With Rl163" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 206 no PDB 4E5A . "The W197a Mutant Of P38a Map Kinase" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 207 no PDB 4E5B . "Structure Of P38a Map Kinase Without Bog" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 208 no PDB 4E6A . "P38a-pia23 Complex" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 209 no PDB 4E6C . "P38a-perifosine Complex" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 210 no PDB 4E8A . "The Crystal Structure Of P38a Map Kinase In Complex With Pia24" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 211 no PDB 4EH2 . "Human P38 Map Kinase In Complex With Np-F1 And Rl87" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 212 no PDB 4EH3 . "Human P38 Map Kinase In Complex With Np-F2 And Rl87" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 213 no PDB 4EH4 . "Human P38 Map Kinase In Complex With Np-F3 And Rl87" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 214 no PDB 4EH5 . "Human P38 Map Kinase In Complex With Np-F4 And Rl87" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 215 no PDB 4EH6 . "Human P38 Map Kinase In Complex With Np-F5 And Rl87" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 216 no PDB 4EH7 . "Human P38 Map Kinase In Complex With Np-F6 And Rl87" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 217 no PDB 4EH8 . "Human P38 Map Kinase In Complex With Np-F7 And Rl87" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 218 no PDB 4EH9 . "Human P38 Map Kinase In Complex With Np-F11 And Rl87" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 219 no PDB 4EHV . "Human P38 Map Kinase In Complex With Np-F10 And Rl87" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 220 no PDB 4EWQ . "Human P38 Alpha Mapk In Complex With A Pyridazine Based Inhibitor" . . . . . 99.15 383 99.43 99.43 0.00e+00 . . . . 17471 1 221 no PDB 4F9W . "Human P38alpha Mapk In Complex With A Novel And Selective Small Molecule Inhibitor" . . . . . 99.15 383 99.71 99.71 0.00e+00 . . . . 17471 1 222 no PDB 4F9Y . "Human P38 Alpha Mapk In Complex With A Novel And Selective Small Molecule Inhibitor" . . . . . 99.15 383 99.71 99.71 0.00e+00 . . . . 17471 1 223 no PDB 4FA2 . "Human P38 Alpha Mitogen-activated Kinase In Complex With Sb239063" . . . . . 99.15 383 99.71 99.71 0.00e+00 . . . . 17471 1 224 no PDB 4GEO . "P38a Map Kinase Def-pocket Penta Mutant (m194a, L195a, H228a, I229a, Y258a)" . . . . . 99.72 367 98.01 98.01 0.00e+00 . . . . 17471 1 225 no PDB 4KA3 . "Structure Of Map Kinase In Complex With A Docking Peptide" . . . . . 98.86 360 99.43 99.43 0.00e+00 . . . . 17471 1 226 no PDB 4KIN . "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 5-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 227 no PDB 4KIP . "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 2-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 228 no PDB 4KIQ . "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With Ethyl 6-((5-(cyclopropylcarbamoyl)-2-methylpheny" . . . . . 99.72 366 99.43 99.43 0.00e+00 . . . . 17471 1 229 no PDB 4L8M . "Human P38 Map Kinase In Complex With A Dibenzoxepinone" . . . . . 99.15 360 100.00 100.00 0.00e+00 . . . . 17471 1 230 no PDB 4LOO . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (monoclinic Crystal Form)" . . . . . 98.86 361 99.43 99.43 0.00e+00 . . . . 17471 1 231 no PDB 4LOP . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form)" . . . . . 98.86 361 99.43 99.43 0.00e+00 . . . . 17471 1 232 no PDB 4LOQ . "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form With Bound Sulphate)" . . . . . 98.86 361 99.43 99.43 0.00e+00 . . . . 17471 1 233 no PDB 4R3C . "Crystal Structure Of P38 Alpha Map Kinase In Complex With A Novel Isoform Selective Drug Candidate" . . . . . 99.15 383 99.43 99.43 0.00e+00 . . . . 17471 1 234 no PDB 4TYH . "Ternary Complex Of P38 And Mk2 With A P38 Inhibitor" . . . . . 97.73 348 99.42 99.42 0.00e+00 . . . . 17471 1 235 no DBJ BAB85654 . "Alternative spliced variant of p38alpha EXIP [Homo sapiens]" . . . . . 71.88 307 100.00 100.00 0.00e+00 . . . . 17471 1 236 no DBJ BAE21782 . "unnamed protein product [Mus musculus]" . . . . . 98.86 360 99.43 99.43 0.00e+00 . . . . 17471 1 237 no DBJ BAE30324 . "unnamed protein product [Mus musculus]" . . . . . 77.27 283 99.63 99.63 0.00e+00 . . . . 17471 1 238 no DBJ BAE31659 . "unnamed protein product [Mus musculus]" . . . . . 77.27 283 99.63 99.63 0.00e+00 . . . . 17471 1 239 no DBJ BAF84398 . "unnamed protein product [Homo sapiens]" . . . . . 98.86 360 99.71 99.71 0.00e+00 . . . . 17471 1 240 no EMBL CAG38743 . "MAPK14 [Homo sapiens]" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 241 no GB AAA20888 . "MAP kinase [Mus musculus]" . . . . . 98.86 360 99.43 99.43 0.00e+00 . . . . 17471 1 242 no GB AAA57456 . "CSaids binding protein [Homo sapiens]" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 243 no GB AAA74301 . "MAP kinase [Homo sapiens]" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 244 no GB AAB51285 . "p38 mitogen activated protein kinase [Rattus norvegicus]" . . . . . 98.86 360 98.28 98.85 0.00e+00 . . . . 17471 1 245 no GB AAC36131 . "p38 mitogen activated protein kinase [Canis lupus familiaris]" . . . . . 98.86 360 99.43 100.00 0.00e+00 . . . . 17471 1 246 no PRF 2111247A . "p38 mitogen-activated protein kinase" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 247 no PRF 2124426A . "Mxi2 protein" . . . . . 79.55 297 99.64 99.64 0.00e+00 . . . . 17471 1 248 no REF NP_001003206 . "mitogen-activated protein kinase 14 [Canis lupus familiaris]" . . . . . 98.86 360 99.43 100.00 0.00e+00 . . . . 17471 1 249 no REF NP_001136366 . "mitogen-activated protein kinase 14 [Ovis aries]" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 250 no REF NP_001161985 . "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" . . . . . 77.27 283 99.63 99.63 0.00e+00 . . . . 17471 1 251 no REF NP_001161986 . "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" . . . . . 77.27 283 99.63 99.63 0.00e+00 . . . . 17471 1 252 no REF NP_036081 . "mitogen-activated protein kinase 14 isoform 1 [Mus musculus]" . . . . . 98.86 360 99.43 99.43 0.00e+00 . . . . 17471 1 253 no SP O02812 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Mitogen-activated protein " . . . . . 98.86 360 99.43 100.00 0.00e+00 . . . . 17471 1 254 no SP P47811 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=CRK1; AltName: Full=Mitoge" . . . . . 98.86 360 99.43 99.43 0.00e+00 . . . . 17471 1 255 no SP P70618 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=CRK1; AltName: Full=Mitoge" . . . . . 98.86 360 98.56 99.14 0.00e+00 . . . . 17471 1 256 no SP Q16539 . "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Cytokine suppressive anti-" . . . . . 98.86 360 100.00 100.00 0.00e+00 . . . . 17471 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'mitogen-activated protein kinase' 17471 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 . GLY . 17471 1 2 . HIS . 17471 1 3 . MET . 17471 1 4 . GLY . 17471 1 5 . SER . 17471 1 6 . GLN . 17471 1 7 . GLU . 17471 1 8 . ARG . 17471 1 9 . PRO . 17471 1 10 . THR . 17471 1 11 . PHE . 17471 1 12 . TYR . 17471 1 13 . ARG . 17471 1 14 . GLN . 17471 1 15 . GLU . 17471 1 16 . LEU . 17471 1 17 . ASN . 17471 1 18 . LYS . 17471 1 19 . THR . 17471 1 20 . ILE . 17471 1 21 . TRP . 17471 1 22 . GLU . 17471 1 23 . VAL . 17471 1 24 . PRO . 17471 1 25 . GLU . 17471 1 26 . ARG . 17471 1 27 . TYR . 17471 1 28 . GLN . 17471 1 29 . ASN . 17471 1 30 . LEU . 17471 1 31 . SER . 17471 1 32 . PRO . 17471 1 33 . VAL . 17471 1 34 . GLY . 17471 1 35 . SER . 17471 1 36 . GLY . 17471 1 37 . ALA . 17471 1 38 . TYR . 17471 1 39 . GLY . 17471 1 40 . SER . 17471 1 41 . VAL . 17471 1 42 . CYS . 17471 1 43 . ALA . 17471 1 44 . ALA . 17471 1 45 . PHE . 17471 1 46 . ASP . 17471 1 47 . THR . 17471 1 48 . LYS . 17471 1 49 . THR . 17471 1 50 . GLY . 17471 1 51 . LEU . 17471 1 52 . ARG . 17471 1 53 . VAL . 17471 1 54 . ALA . 17471 1 55 . VAL . 17471 1 56 . LYS . 17471 1 57 . LYS . 17471 1 58 . LEU . 17471 1 59 . SER . 17471 1 60 . ARG . 17471 1 61 . PRO . 17471 1 62 . PHE . 17471 1 63 . GLN . 17471 1 64 . SER . 17471 1 65 . ILE . 17471 1 66 . ILE . 17471 1 67 . HIS . 17471 1 68 . ALA . 17471 1 69 . LYS . 17471 1 70 . ARG . 17471 1 71 . THR . 17471 1 72 . TYR . 17471 1 73 . ARG . 17471 1 74 . GLU . 17471 1 75 . LEU . 17471 1 76 . ARG . 17471 1 77 . LEU . 17471 1 78 . LEU . 17471 1 79 . LYS . 17471 1 80 . HIS . 17471 1 81 . MET . 17471 1 82 . LYS . 17471 1 83 . HIS . 17471 1 84 . GLU . 17471 1 85 . ASN . 17471 1 86 . VAL . 17471 1 87 . ILE . 17471 1 88 . GLY . 17471 1 89 . LEU . 17471 1 90 . LEU . 17471 1 91 . ASP . 17471 1 92 . VAL . 17471 1 93 . PHE . 17471 1 94 . THR . 17471 1 95 . PRO . 17471 1 96 . ALA . 17471 1 97 . ARG . 17471 1 98 . SER . 17471 1 99 . LEU . 17471 1 100 . GLU . 17471 1 101 . GLU . 17471 1 102 . PHE . 17471 1 103 . ASN . 17471 1 104 . ASP . 17471 1 105 . VAL . 17471 1 106 . TYR . 17471 1 107 . LEU . 17471 1 108 . VAL . 17471 1 109 . THR . 17471 1 110 . HIS . 17471 1 111 . LEU . 17471 1 112 . MET . 17471 1 113 . GLY . 17471 1 114 . ALA . 17471 1 115 . ASP . 17471 1 116 . LEU . 17471 1 117 . ASN . 17471 1 118 . ASN . 17471 1 119 . ILE . 17471 1 120 . VAL . 17471 1 121 . LYS . 17471 1 122 . CYS . 17471 1 123 . GLN . 17471 1 124 . LYS . 17471 1 125 . LEU . 17471 1 126 . THR . 17471 1 127 . ASP . 17471 1 128 . ASP . 17471 1 129 . HIS . 17471 1 130 . VAL . 17471 1 131 . GLN . 17471 1 132 . PHE . 17471 1 133 . LEU . 17471 1 134 . ILE . 17471 1 135 . TYR . 17471 1 136 . GLN . 17471 1 137 . ILE . 17471 1 138 . LEU . 17471 1 139 . ARG . 17471 1 140 . GLY . 17471 1 141 . LEU . 17471 1 142 . LYS . 17471 1 143 . TYR . 17471 1 144 . ILE . 17471 1 145 . HIS . 17471 1 146 . SER . 17471 1 147 . ALA . 17471 1 148 . ASP . 17471 1 149 . ILE . 17471 1 150 . ILE . 17471 1 151 . HIS . 17471 1 152 . ARG . 17471 1 153 . ASP . 17471 1 154 . LEU . 17471 1 155 . LYS . 17471 1 156 . PRO . 17471 1 157 . SER . 17471 1 158 . ASN . 17471 1 159 . LEU . 17471 1 160 . ALA . 17471 1 161 . VAL . 17471 1 162 . ASN . 17471 1 163 . GLU . 17471 1 164 . ASP . 17471 1 165 . CYS . 17471 1 166 . GLU . 17471 1 167 . LEU . 17471 1 168 . LYS . 17471 1 169 . ILE . 17471 1 170 . LEU . 17471 1 171 . ASP . 17471 1 172 . PHE . 17471 1 173 . GLY . 17471 1 174 . LEU . 17471 1 175 . ALA . 17471 1 176 . ARG . 17471 1 177 . HIS . 17471 1 178 . THR . 17471 1 179 . ASP . 17471 1 180 . ASP . 17471 1 181 . GLU . 17471 1 182 . MET . 17471 1 183 . THR . 17471 1 184 . GLY . 17471 1 185 . TYR . 17471 1 186 . VAL . 17471 1 187 . ALA . 17471 1 188 . THR . 17471 1 189 . ARG . 17471 1 190 . TRP . 17471 1 191 . TYR . 17471 1 192 . ARG . 17471 1 193 . ALA . 17471 1 194 . PRO . 17471 1 195 . GLU . 17471 1 196 . ILE . 17471 1 197 . MET . 17471 1 198 . LEU . 17471 1 199 . ASN . 17471 1 200 . TRP . 17471 1 201 . MET . 17471 1 202 . HIS . 17471 1 203 . TYR . 17471 1 204 . ASN . 17471 1 205 . GLN . 17471 1 206 . THR . 17471 1 207 . VAL . 17471 1 208 . ASP . 17471 1 209 . ILE . 17471 1 210 . TRP . 17471 1 211 . SER . 17471 1 212 . VAL . 17471 1 213 . GLY . 17471 1 214 . CYS . 17471 1 215 . ILE . 17471 1 216 . MET . 17471 1 217 . ALA . 17471 1 218 . GLU . 17471 1 219 . LEU . 17471 1 220 . LEU . 17471 1 221 . THR . 17471 1 222 . GLY . 17471 1 223 . ARG . 17471 1 224 . THR . 17471 1 225 . LEU . 17471 1 226 . PHE . 17471 1 227 . PRO . 17471 1 228 . GLY . 17471 1 229 . THR . 17471 1 230 . ASP . 17471 1 231 . HIS . 17471 1 232 . ILE . 17471 1 233 . ASP . 17471 1 234 . GLN . 17471 1 235 . LEU . 17471 1 236 . LYS . 17471 1 237 . LEU . 17471 1 238 . ILE . 17471 1 239 . LEU . 17471 1 240 . ARG . 17471 1 241 . LEU . 17471 1 242 . VAL . 17471 1 243 . GLY . 17471 1 244 . THR . 17471 1 245 . PRO . 17471 1 246 . GLY . 17471 1 247 . ALA . 17471 1 248 . GLU . 17471 1 249 . LEU . 17471 1 250 . LEU . 17471 1 251 . LYS . 17471 1 252 . LYS . 17471 1 253 . ILE . 17471 1 254 . SER . 17471 1 255 . SER . 17471 1 256 . GLU . 17471 1 257 . SER . 17471 1 258 . ALA . 17471 1 259 . ARG . 17471 1 260 . ASN . 17471 1 261 . TYR . 17471 1 262 . ILE . 17471 1 263 . GLN . 17471 1 264 . SER . 17471 1 265 . LEU . 17471 1 266 . THR . 17471 1 267 . GLN . 17471 1 268 . MET . 17471 1 269 . PRO . 17471 1 270 . LYS . 17471 1 271 . MET . 17471 1 272 . ASN . 17471 1 273 . PHE . 17471 1 274 . ALA . 17471 1 275 . ASN . 17471 1 276 . VAL . 17471 1 277 . PHE . 17471 1 278 . ILE . 17471 1 279 . GLY . 17471 1 280 . ALA . 17471 1 281 . ASN . 17471 1 282 . PRO . 17471 1 283 . LEU . 17471 1 284 . ALA . 17471 1 285 . VAL . 17471 1 286 . ASP . 17471 1 287 . LEU . 17471 1 288 . LEU . 17471 1 289 . GLU . 17471 1 290 . LYS . 17471 1 291 . MET . 17471 1 292 . LEU . 17471 1 293 . VAL . 17471 1 294 . LEU . 17471 1 295 . ASP . 17471 1 296 . SER . 17471 1 297 . ASP . 17471 1 298 . LYS . 17471 1 299 . ARG . 17471 1 300 . ILE . 17471 1 301 . THR . 17471 1 302 . ALA . 17471 1 303 . ALA . 17471 1 304 . GLN . 17471 1 305 . ALA . 17471 1 306 . LEU . 17471 1 307 . ALA . 17471 1 308 . HIS . 17471 1 309 . ALA . 17471 1 310 . TYR . 17471 1 311 . PHE . 17471 1 312 . ALA . 17471 1 313 . GLN . 17471 1 314 . TYR . 17471 1 315 . HIS . 17471 1 316 . ASP . 17471 1 317 . PRO . 17471 1 318 . ASP . 17471 1 319 . ASP . 17471 1 320 . GLU . 17471 1 321 . PRO . 17471 1 322 . VAL . 17471 1 323 . ALA . 17471 1 324 . ASP . 17471 1 325 . PRO . 17471 1 326 . TYR . 17471 1 327 . ASP . 17471 1 328 . GLN . 17471 1 329 . SER . 17471 1 330 . PHE . 17471 1 331 . GLU . 17471 1 332 . SER . 17471 1 333 . ARG . 17471 1 334 . ASP . 17471 1 335 . LEU . 17471 1 336 . LEU . 17471 1 337 . ILE . 17471 1 338 . ASP . 17471 1 339 . GLU . 17471 1 340 . TRP . 17471 1 341 . LYS . 17471 1 342 . SER . 17471 1 343 . LEU . 17471 1 344 . THR . 17471 1 345 . TYR . 17471 1 346 . ASP . 17471 1 347 . GLU . 17471 1 348 . VAL . 17471 1 349 . ILE . 17471 1 350 . SER . 17471 1 351 . PHE . 17471 1 352 . VAL . 17471 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . GLY 1 1 17471 1 . HIS 2 2 17471 1 . MET 3 3 17471 1 . GLY 4 4 17471 1 . SER 5 5 17471 1 . GLN 6 6 17471 1 . GLU 7 7 17471 1 . ARG 8 8 17471 1 . PRO 9 9 17471 1 . THR 10 10 17471 1 . PHE 11 11 17471 1 . TYR 12 12 17471 1 . ARG 13 13 17471 1 . GLN 14 14 17471 1 . GLU 15 15 17471 1 . LEU 16 16 17471 1 . ASN 17 17 17471 1 . LYS 18 18 17471 1 . THR 19 19 17471 1 . ILE 20 20 17471 1 . TRP 21 21 17471 1 . GLU 22 22 17471 1 . VAL 23 23 17471 1 . PRO 24 24 17471 1 . GLU 25 25 17471 1 . ARG 26 26 17471 1 . TYR 27 27 17471 1 . GLN 28 28 17471 1 . ASN 29 29 17471 1 . LEU 30 30 17471 1 . SER 31 31 17471 1 . PRO 32 32 17471 1 . VAL 33 33 17471 1 . GLY 34 34 17471 1 . SER 35 35 17471 1 . GLY 36 36 17471 1 . ALA 37 37 17471 1 . TYR 38 38 17471 1 . GLY 39 39 17471 1 . SER 40 40 17471 1 . VAL 41 41 17471 1 . CYS 42 42 17471 1 . ALA 43 43 17471 1 . ALA 44 44 17471 1 . PHE 45 45 17471 1 . ASP 46 46 17471 1 . THR 47 47 17471 1 . LYS 48 48 17471 1 . THR 49 49 17471 1 . GLY 50 50 17471 1 . LEU 51 51 17471 1 . ARG 52 52 17471 1 . VAL 53 53 17471 1 . ALA 54 54 17471 1 . VAL 55 55 17471 1 . LYS 56 56 17471 1 . LYS 57 57 17471 1 . LEU 58 58 17471 1 . SER 59 59 17471 1 . ARG 60 60 17471 1 . PRO 61 61 17471 1 . PHE 62 62 17471 1 . GLN 63 63 17471 1 . SER 64 64 17471 1 . ILE 65 65 17471 1 . ILE 66 66 17471 1 . HIS 67 67 17471 1 . ALA 68 68 17471 1 . LYS 69 69 17471 1 . ARG 70 70 17471 1 . THR 71 71 17471 1 . TYR 72 72 17471 1 . ARG 73 73 17471 1 . GLU 74 74 17471 1 . LEU 75 75 17471 1 . ARG 76 76 17471 1 . LEU 77 77 17471 1 . LEU 78 78 17471 1 . LYS 79 79 17471 1 . HIS 80 80 17471 1 . MET 81 81 17471 1 . LYS 82 82 17471 1 . HIS 83 83 17471 1 . GLU 84 84 17471 1 . ASN 85 85 17471 1 . VAL 86 86 17471 1 . ILE 87 87 17471 1 . GLY 88 88 17471 1 . LEU 89 89 17471 1 . LEU 90 90 17471 1 . ASP 91 91 17471 1 . VAL 92 92 17471 1 . PHE 93 93 17471 1 . THR 94 94 17471 1 . PRO 95 95 17471 1 . ALA 96 96 17471 1 . ARG 97 97 17471 1 . SER 98 98 17471 1 . LEU 99 99 17471 1 . GLU 100 100 17471 1 . GLU 101 101 17471 1 . PHE 102 102 17471 1 . ASN 103 103 17471 1 . ASP 104 104 17471 1 . VAL 105 105 17471 1 . TYR 106 106 17471 1 . LEU 107 107 17471 1 . VAL 108 108 17471 1 . THR 109 109 17471 1 . HIS 110 110 17471 1 . LEU 111 111 17471 1 . MET 112 112 17471 1 . GLY 113 113 17471 1 . ALA 114 114 17471 1 . ASP 115 115 17471 1 . LEU 116 116 17471 1 . ASN 117 117 17471 1 . ASN 118 118 17471 1 . ILE 119 119 17471 1 . VAL 120 120 17471 1 . LYS 121 121 17471 1 . CYS 122 122 17471 1 . GLN 123 123 17471 1 . LYS 124 124 17471 1 . LEU 125 125 17471 1 . THR 126 126 17471 1 . ASP 127 127 17471 1 . ASP 128 128 17471 1 . HIS 129 129 17471 1 . VAL 130 130 17471 1 . GLN 131 131 17471 1 . PHE 132 132 17471 1 . LEU 133 133 17471 1 . ILE 134 134 17471 1 . TYR 135 135 17471 1 . GLN 136 136 17471 1 . ILE 137 137 17471 1 . LEU 138 138 17471 1 . ARG 139 139 17471 1 . GLY 140 140 17471 1 . LEU 141 141 17471 1 . LYS 142 142 17471 1 . TYR 143 143 17471 1 . ILE 144 144 17471 1 . HIS 145 145 17471 1 . SER 146 146 17471 1 . ALA 147 147 17471 1 . ASP 148 148 17471 1 . ILE 149 149 17471 1 . ILE 150 150 17471 1 . HIS 151 151 17471 1 . ARG 152 152 17471 1 . ASP 153 153 17471 1 . LEU 154 154 17471 1 . LYS 155 155 17471 1 . PRO 156 156 17471 1 . SER 157 157 17471 1 . ASN 158 158 17471 1 . LEU 159 159 17471 1 . ALA 160 160 17471 1 . VAL 161 161 17471 1 . ASN 162 162 17471 1 . GLU 163 163 17471 1 . ASP 164 164 17471 1 . CYS 165 165 17471 1 . GLU 166 166 17471 1 . LEU 167 167 17471 1 . LYS 168 168 17471 1 . ILE 169 169 17471 1 . LEU 170 170 17471 1 . ASP 171 171 17471 1 . PHE 172 172 17471 1 . GLY 173 173 17471 1 . LEU 174 174 17471 1 . ALA 175 175 17471 1 . ARG 176 176 17471 1 . HIS 177 177 17471 1 . THR 178 178 17471 1 . ASP 179 179 17471 1 . ASP 180 180 17471 1 . GLU 181 181 17471 1 . MET 182 182 17471 1 . THR 183 183 17471 1 . GLY 184 184 17471 1 . TYR 185 185 17471 1 . VAL 186 186 17471 1 . ALA 187 187 17471 1 . THR 188 188 17471 1 . ARG 189 189 17471 1 . TRP 190 190 17471 1 . TYR 191 191 17471 1 . ARG 192 192 17471 1 . ALA 193 193 17471 1 . PRO 194 194 17471 1 . GLU 195 195 17471 1 . ILE 196 196 17471 1 . MET 197 197 17471 1 . LEU 198 198 17471 1 . ASN 199 199 17471 1 . TRP 200 200 17471 1 . MET 201 201 17471 1 . HIS 202 202 17471 1 . TYR 203 203 17471 1 . ASN 204 204 17471 1 . GLN 205 205 17471 1 . THR 206 206 17471 1 . VAL 207 207 17471 1 . ASP 208 208 17471 1 . ILE 209 209 17471 1 . TRP 210 210 17471 1 . SER 211 211 17471 1 . VAL 212 212 17471 1 . GLY 213 213 17471 1 . CYS 214 214 17471 1 . ILE 215 215 17471 1 . MET 216 216 17471 1 . ALA 217 217 17471 1 . GLU 218 218 17471 1 . LEU 219 219 17471 1 . LEU 220 220 17471 1 . THR 221 221 17471 1 . GLY 222 222 17471 1 . ARG 223 223 17471 1 . THR 224 224 17471 1 . LEU 225 225 17471 1 . PHE 226 226 17471 1 . PRO 227 227 17471 1 . GLY 228 228 17471 1 . THR 229 229 17471 1 . ASP 230 230 17471 1 . HIS 231 231 17471 1 . ILE 232 232 17471 1 . ASP 233 233 17471 1 . GLN 234 234 17471 1 . LEU 235 235 17471 1 . LYS 236 236 17471 1 . LEU 237 237 17471 1 . ILE 238 238 17471 1 . LEU 239 239 17471 1 . ARG 240 240 17471 1 . LEU 241 241 17471 1 . VAL 242 242 17471 1 . GLY 243 243 17471 1 . THR 244 244 17471 1 . PRO 245 245 17471 1 . GLY 246 246 17471 1 . ALA 247 247 17471 1 . GLU 248 248 17471 1 . LEU 249 249 17471 1 . LEU 250 250 17471 1 . LYS 251 251 17471 1 . LYS 252 252 17471 1 . ILE 253 253 17471 1 . SER 254 254 17471 1 . SER 255 255 17471 1 . GLU 256 256 17471 1 . SER 257 257 17471 1 . ALA 258 258 17471 1 . ARG 259 259 17471 1 . ASN 260 260 17471 1 . TYR 261 261 17471 1 . ILE 262 262 17471 1 . GLN 263 263 17471 1 . SER 264 264 17471 1 . LEU 265 265 17471 1 . THR 266 266 17471 1 . GLN 267 267 17471 1 . MET 268 268 17471 1 . PRO 269 269 17471 1 . LYS 270 270 17471 1 . MET 271 271 17471 1 . ASN 272 272 17471 1 . PHE 273 273 17471 1 . ALA 274 274 17471 1 . ASN 275 275 17471 1 . VAL 276 276 17471 1 . PHE 277 277 17471 1 . ILE 278 278 17471 1 . GLY 279 279 17471 1 . ALA 280 280 17471 1 . ASN 281 281 17471 1 . PRO 282 282 17471 1 . LEU 283 283 17471 1 . ALA 284 284 17471 1 . VAL 285 285 17471 1 . ASP 286 286 17471 1 . LEU 287 287 17471 1 . LEU 288 288 17471 1 . GLU 289 289 17471 1 . LYS 290 290 17471 1 . MET 291 291 17471 1 . LEU 292 292 17471 1 . VAL 293 293 17471 1 . LEU 294 294 17471 1 . ASP 295 295 17471 1 . SER 296 296 17471 1 . ASP 297 297 17471 1 . LYS 298 298 17471 1 . ARG 299 299 17471 1 . ILE 300 300 17471 1 . THR 301 301 17471 1 . ALA 302 302 17471 1 . ALA 303 303 17471 1 . GLN 304 304 17471 1 . ALA 305 305 17471 1 . LEU 306 306 17471 1 . ALA 307 307 17471 1 . HIS 308 308 17471 1 . ALA 309 309 17471 1 . TYR 310 310 17471 1 . PHE 311 311 17471 1 . ALA 312 312 17471 1 . GLN 313 313 17471 1 . TYR 314 314 17471 1 . HIS 315 315 17471 1 . ASP 316 316 17471 1 . PRO 317 317 17471 1 . ASP 318 318 17471 1 . ASP 319 319 17471 1 . GLU 320 320 17471 1 . PRO 321 321 17471 1 . VAL 322 322 17471 1 . ALA 323 323 17471 1 . ASP 324 324 17471 1 . PRO 325 325 17471 1 . TYR 326 326 17471 1 . ASP 327 327 17471 1 . GLN 328 328 17471 1 . SER 329 329 17471 1 . PHE 330 330 17471 1 . GLU 331 331 17471 1 . SER 332 332 17471 1 . ARG 333 333 17471 1 . ASP 334 334 17471 1 . LEU 335 335 17471 1 . LEU 336 336 17471 1 . ILE 337 337 17471 1 . ASP 338 338 17471 1 . GLU 339 339 17471 1 . TRP 340 340 17471 1 . LYS 341 341 17471 1 . SER 342 342 17471 1 . LEU 343 343 17471 1 . THR 344 344 17471 1 . TYR 345 345 17471 1 . ASP 346 346 17471 1 . GLU 347 347 17471 1 . VAL 348 348 17471 1 . ILE 349 349 17471 1 . SER 350 350 17471 1 . PHE 351 351 17471 1 . VAL 352 352 17471 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 17471 _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 $p38_alpha . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 17471 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 17471 _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 $p38_alpha . 'recombinant technology' 'Escherichia coli' 'Escherichia coli' . 562 Escherichia coli . . . . . . . . . . . . . . . . pRPIB . . . . . . 17471 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 17471 _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 p38_alpha '[U-13C; U-15N; U-2H]' . . 1 $p38_alpha . . 0.58 . . mM . . . . 17471 1 2 HEPES 'natural abundance' . . . . . . 50 . . mM . . . . 17471 1 3 'sodium chloride' 'natural abundance' . . . . . . 150 . . mM . . . . 17471 1 4 DTT 'natural abundance' . . . . . . 5 . . mM . . . . 17471 1 5 H2O 'natural abundance' . . . . . . 90 . . % . . . . 17471 1 6 D2O 'natural abundance' . . . . . . 10 . . % . . . . 17471 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 17471 _Sample.ID 2 _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 'p38 alpha' [U-2H;U-15N] . . 1 $p38_alpha . . 0.2 . . mM . . . . 17471 2 2 HEPES 'natural abundance' . . . . . . 50 . . mM . . . . 17471 2 3 'sodium chloride' 'natural abundance' . . . . . . 150 . . mM . . . . 17471 2 4 DTT 'natural abundance' . . . . . . 5 . . mM . . . . 17471 2 5 H2O 'natural abundance' . . . . . . 90 . . % . . . . 17471 2 6 D2O 'natural abundance' . . . . . . 10 . . % . . . . 17471 2 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 17471 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.15 . M 17471 1 pH 6.8 . pH 17471 1 pressure 1 . atm 17471 1 temperature 298 . K 17471 1 stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 17471 _Software.ID 1 _Software.Name TOPSPIN _Software.Version '1.3 and 2.1' _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 17471 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 17471 1 processing 17471 1 stop_ save_ save_CARA _Software.Sf_category software _Software.Sf_framecode CARA _Software.Entry_ID 17471 _Software.ID 2 _Software.Name CARA _Software.Version 1.8 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Keller and Wuthrich' . . 17471 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 17471 2 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 17471 _NMR_spectrometer.ID 1 _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 17471 _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 . 800 . . . 17471 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 17471 _Experiment_list.ID 1 _Experiment_list.Details 'All experiments were implemented as TROSY-type experiments.' loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17471 1 2 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17471 1 3 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17471 1 4 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17471 1 5 '3D HN(COCA)CB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17471 1 6 '3D 1H-15N NOESY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17471 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 17471 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.251449530 . . . 1 $citation_1 . . 1 $citation_1 17471 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . 1 $citation_1 . . 1 $citation_1 17471 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.101329118 . . . 1 $citation_1 . . 1 $citation_1 17471 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 17471 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 17471 1 2 '3D HNCA' . . . 17471 1 3 '3D HNCACB' . . . 17471 1 4 '3D HN(CO)CA' . . . 17471 1 5 '3D HN(COCA)CB' . . . 17471 1 6 '3D 1H-15N NOESY' . . . 17471 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 3 3 MET CA C 13 55.190 0.250 . 1 . . . . 3 MET CA . 17471 1 2 . 1 1 3 3 MET CB C 13 31.685 0.250 . 1 . . . . 3 MET CB . 17471 1 3 . 1 1 4 4 GLY H H 1 8.346 0.010 . 1 . . . . 4 GLY H . 17471 1 4 . 1 1 4 4 GLY CA C 13 44.812 0.250 . 1 . . . . 4 GLY CA . 17471 1 5 . 1 1 4 4 GLY N N 15 110.960 0.070 . 1 . . . . 4 GLY N . 17471 1 6 . 1 1 5 5 SER H H 1 8.138 0.010 . 1 . . . . 5 SER H . 17471 1 7 . 1 1 5 5 SER CA C 13 58.001 0.250 . 1 . . . . 5 SER CA . 17471 1 8 . 1 1 5 5 SER CB C 13 63.163 0.250 . 1 . . . . 5 SER CB . 17471 1 9 . 1 1 5 5 SER N N 15 116.267 0.070 . 1 . . . . 5 SER N . 17471 1 10 . 1 1 6 6 GLN H H 1 8.389 0.010 . 1 . . . . 6 GLN H . 17471 1 11 . 1 1 6 6 GLN CA C 13 55.404 0.250 . 1 . . . . 6 GLN CA . 17471 1 12 . 1 1 6 6 GLN CB C 13 28.614 0.250 . 1 . . . . 6 GLN CB . 17471 1 13 . 1 1 6 6 GLN N N 15 122.413 0.070 . 1 . . . . 6 GLN N . 17471 1 14 . 1 1 7 7 GLU H H 1 8.276 0.010 . 1 . . . . 7 GLU H . 17471 1 15 . 1 1 7 7 GLU CA C 13 55.779 0.250 . 1 . . . . 7 GLU CA . 17471 1 16 . 1 1 7 7 GLU CB C 13 29.365 0.250 . 1 . . . . 7 GLU CB . 17471 1 17 . 1 1 7 7 GLU N N 15 122.700 0.070 . 1 . . . . 7 GLU N . 17471 1 18 . 1 1 8 8 ARG H H 1 8.332 0.010 . 1 . . . . 8 ARG H . 17471 1 19 . 1 1 8 8 ARG CA C 13 53.717 0.250 . 1 . . . . 8 ARG CA . 17471 1 20 . 1 1 8 8 ARG CB C 13 29.698 0.250 . 1 . . . . 8 ARG CB . 17471 1 21 . 1 1 8 8 ARG N N 15 125.403 0.070 . 1 . . . . 8 ARG N . 17471 1 22 . 1 1 9 9 PRO CA C 13 62.205 0.250 . 1 . . . . 9 PRO CA . 17471 1 23 . 1 1 9 9 PRO CB C 13 31.480 0.250 . 1 . . . . 9 PRO CB . 17471 1 24 . 1 1 10 10 THR H H 1 8.418 0.010 . 1 . . . . 10 THR H . 17471 1 25 . 1 1 10 10 THR CA C 13 62.660 0.250 . 1 . . . . 10 THR CA . 17471 1 26 . 1 1 10 10 THR CB C 13 68.880 0.250 . 1 . . . . 10 THR CB . 17471 1 27 . 1 1 10 10 THR N N 15 117.617 0.070 . 1 . . . . 10 THR N . 17471 1 28 . 1 1 11 11 PHE H H 1 8.729 0.010 . 1 . . . . 11 PHE H . 17471 1 29 . 1 1 11 11 PHE CA C 13 56.555 0.250 . 1 . . . . 11 PHE CA . 17471 1 30 . 1 1 11 11 PHE CB C 13 41.172 0.250 . 1 . . . . 11 PHE CB . 17471 1 31 . 1 1 11 11 PHE N N 15 127.438 0.070 . 1 . . . . 11 PHE N . 17471 1 32 . 1 1 12 12 TYR H H 1 9.089 0.010 . 1 . . . . 12 TYR H . 17471 1 33 . 1 1 12 12 TYR CA C 13 55.538 0.250 . 1 . . . . 12 TYR CA . 17471 1 34 . 1 1 12 12 TYR CB C 13 40.148 0.250 . 1 . . . . 12 TYR CB . 17471 1 35 . 1 1 12 12 TYR N N 15 120.358 0.070 . 1 . . . . 12 TYR N . 17471 1 36 . 1 1 13 13 ARG H H 1 8.385 0.010 . 1 . . . . 13 ARG H . 17471 1 37 . 1 1 13 13 ARG CA C 13 54.092 0.250 . 1 . . . . 13 ARG CA . 17471 1 38 . 1 1 13 13 ARG CB C 13 32.914 0.250 . 1 . . . . 13 ARG CB . 17471 1 39 . 1 1 13 13 ARG N N 15 120.323 0.070 . 1 . . . . 13 ARG N . 17471 1 40 . 1 1 14 14 GLN H H 1 8.934 0.010 . 1 . . . . 14 GLN H . 17471 1 41 . 1 1 14 14 GLN CA C 13 54.494 0.250 . 1 . . . . 14 GLN CA . 17471 1 42 . 1 1 14 14 GLN CB C 13 32.368 0.250 . 1 . . . . 14 GLN CB . 17471 1 43 . 1 1 14 14 GLN N N 15 122.785 0.070 . 1 . . . . 14 GLN N . 17471 1 44 . 1 1 15 15 GLU H H 1 8.790 0.010 . 1 . . . . 15 GLU H . 17471 1 45 . 1 1 15 15 GLU CA C 13 55.110 0.250 . 1 . . . . 15 GLU CA . 17471 1 46 . 1 1 15 15 GLU CB C 13 29.706 0.250 . 1 . . . . 15 GLU CB . 17471 1 47 . 1 1 15 15 GLU N N 15 125.887 0.070 . 1 . . . . 15 GLU N . 17471 1 48 . 1 1 16 16 LEU H H 1 8.942 0.010 . 1 . . . . 16 LEU H . 17471 1 49 . 1 1 16 16 LEU CA C 13 53.557 0.250 . 1 . . . . 16 LEU CA . 17471 1 50 . 1 1 16 16 LEU CB C 13 43.492 0.250 . 1 . . . . 16 LEU CB . 17471 1 51 . 1 1 16 16 LEU N N 15 128.790 0.070 . 1 . . . . 16 LEU N . 17471 1 52 . 1 1 17 17 ASN H H 1 7.250 0.010 . 1 . . . . 17 ASN H . 17471 1 53 . 1 1 17 17 ASN CA C 13 53.664 0.250 . 1 . . . . 17 ASN CA . 17471 1 54 . 1 1 17 17 ASN CB C 13 36.715 0.250 . 1 . . . . 17 ASN CB . 17471 1 55 . 1 1 17 17 ASN N N 15 116.253 0.070 . 1 . . . . 17 ASN N . 17471 1 56 . 1 1 18 18 LYS H H 1 8.830 0.010 . 1 . . . . 18 LYS H . 17471 1 57 . 1 1 18 18 LYS CA C 13 57.363 0.250 . 1 . . . . 18 LYS CA . 17471 1 58 . 1 1 18 18 LYS CB C 13 28.887 0.250 . 1 . . . . 18 LYS CB . 17471 1 59 . 1 1 18 18 LYS N N 15 110.200 0.070 . 1 . . . . 18 LYS N . 17471 1 60 . 1 1 19 19 THR H H 1 7.806 0.010 . 1 . . . . 19 THR H . 17471 1 61 . 1 1 19 19 THR CA C 13 60.946 0.250 . 1 . . . . 19 THR CA . 17471 1 62 . 1 1 19 19 THR CB C 13 70.723 0.250 . 1 . . . . 19 THR CB . 17471 1 63 . 1 1 19 19 THR N N 15 115.941 0.070 . 1 . . . . 19 THR N . 17471 1 64 . 1 1 20 20 ILE H H 1 8.553 0.010 . 1 . . . . 20 ILE H . 17471 1 65 . 1 1 20 20 ILE CA C 13 59.742 0.250 . 1 . . . . 20 ILE CA . 17471 1 66 . 1 1 20 20 ILE CB C 13 35.917 0.250 . 1 . . . . 20 ILE CB . 17471 1 67 . 1 1 20 20 ILE N N 15 125.788 0.070 . 1 . . . . 20 ILE N . 17471 1 68 . 1 1 21 21 TRP H H 1 9.227 0.010 . 1 . . . . 21 TRP H . 17471 1 69 . 1 1 21 21 TRP CA C 13 56.529 0.250 . 1 . . . . 21 TRP CA . 17471 1 70 . 1 1 21 21 TRP CB C 13 28.546 0.250 . 1 . . . . 21 TRP CB . 17471 1 71 . 1 1 21 21 TRP N N 15 131.308 0.070 . 1 . . . . 21 TRP N . 17471 1 72 . 1 1 22 22 GLU H H 1 8.222 0.010 . 1 . . . . 22 GLU H . 17471 1 73 . 1 1 22 22 GLU CA C 13 54.547 0.250 . 1 . . . . 22 GLU CA . 17471 1 74 . 1 1 22 22 GLU CB C 13 30.525 0.250 . 1 . . . . 22 GLU CB . 17471 1 75 . 1 1 22 22 GLU N N 15 128.263 0.070 . 1 . . . . 22 GLU N . 17471 1 76 . 1 1 23 23 VAL H H 1 7.608 0.010 . 1 . . . . 23 VAL H . 17471 1 77 . 1 1 23 23 VAL CA C 13 55.886 0.250 . 1 . . . . 23 VAL CA . 17471 1 78 . 1 1 23 23 VAL CB C 13 33.187 0.250 . 1 . . . . 23 VAL CB . 17471 1 79 . 1 1 23 23 VAL N N 15 112.747 0.070 . 1 . . . . 23 VAL N . 17471 1 80 . 1 1 24 24 PRO CA C 13 61.509 0.250 . 1 . . . . 24 PRO CA . 17471 1 81 . 1 1 24 24 PRO CB C 13 31.412 0.250 . 1 . . . . 24 PRO CB . 17471 1 82 . 1 1 25 25 GLU H H 1 8.068 0.010 . 1 . . . . 25 GLU H . 17471 1 83 . 1 1 25 25 GLU CA C 13 58.162 0.250 . 1 . . . . 25 GLU CA . 17471 1 84 . 1 1 25 25 GLU CB C 13 28.955 0.250 . 1 . . . . 25 GLU CB . 17471 1 85 . 1 1 25 25 GLU N N 15 119.212 0.070 . 1 . . . . 25 GLU N . 17471 1 86 . 1 1 26 26 ARG H H 1 7.407 0.010 . 1 . . . . 26 ARG H . 17471 1 87 . 1 1 26 26 ARG CA C 13 57.385 0.250 . 1 . . . . 26 ARG CA . 17471 1 88 . 1 1 26 26 ARG CB C 13 29.706 0.250 . 1 . . . . 26 ARG CB . 17471 1 89 . 1 1 26 26 ARG N N 15 117.646 0.070 . 1 . . . . 26 ARG N . 17471 1 90 . 1 1 27 27 TYR H H 1 7.742 0.010 . 1 . . . . 27 TYR H . 17471 1 91 . 1 1 27 27 TYR CA C 13 56.930 0.250 . 1 . . . . 27 TYR CA . 17471 1 92 . 1 1 27 27 TYR CB C 13 37.008 0.250 . 1 . . . . 27 TYR CB . 17471 1 93 . 1 1 27 27 TYR N N 15 118.387 0.070 . 1 . . . . 27 TYR N . 17471 1 94 . 1 1 28 28 GLN H H 1 9.138 0.010 . 1 . . . . 28 GLN H . 17471 1 95 . 1 1 28 28 GLN CA C 13 53.262 0.250 . 1 . . . . 28 GLN CA . 17471 1 96 . 1 1 28 28 GLN CB C 13 32.504 0.250 . 1 . . . . 28 GLN CB . 17471 1 97 . 1 1 28 28 GLN N N 15 122.815 0.070 . 1 . . . . 28 GLN N . 17471 1 98 . 1 1 29 29 ASN H H 1 8.775 0.010 . 1 . . . . 29 ASN H . 17471 1 99 . 1 1 29 29 ASN CA C 13 53.209 0.250 . 1 . . . . 29 ASN CA . 17471 1 100 . 1 1 29 29 ASN CB C 13 36.258 0.250 . 1 . . . . 29 ASN CB . 17471 1 101 . 1 1 29 29 ASN N N 15 117.790 0.070 . 1 . . . . 29 ASN N . 17471 1 102 . 1 1 30 30 LEU H H 1 8.484 0.010 . 1 . . . . 30 LEU H . 17471 1 103 . 1 1 30 30 LEU CA C 13 56.582 0.250 . 1 . . . . 30 LEU CA . 17471 1 104 . 1 1 30 30 LEU CB C 13 40.557 0.250 . 1 . . . . 30 LEU CB . 17471 1 105 . 1 1 30 30 LEU N N 15 120.480 0.070 . 1 . . . . 30 LEU N . 17471 1 106 . 1 1 31 31 SER H H 1 8.709 0.010 . 1 . . . . 31 SER H . 17471 1 107 . 1 1 31 31 SER CA C 13 54.226 0.250 . 1 . . . . 31 SER CA . 17471 1 108 . 1 1 31 31 SER CB C 13 64.171 0.250 . 1 . . . . 31 SER CB . 17471 1 109 . 1 1 31 31 SER N N 15 116.358 0.070 . 1 . . . . 31 SER N . 17471 1 110 . 1 1 32 32 PRO CA C 13 64.106 0.250 . 1 . . . . 32 PRO CA . 17471 1 111 . 1 1 32 32 PRO CB C 13 31.412 0.250 . 1 . . . . 32 PRO CB . 17471 1 112 . 1 1 33 33 VAL H H 1 8.564 0.010 . 1 . . . . 33 VAL H . 17471 1 113 . 1 1 33 33 VAL CA C 13 61.669 0.250 . 1 . . . . 33 VAL CA . 17471 1 114 . 1 1 33 33 VAL CB C 13 33.114 0.250 . 1 . . . . 33 VAL CB . 17471 1 115 . 1 1 33 33 VAL N N 15 121.177 0.070 . 1 . . . . 33 VAL N . 17471 1 116 . 1 1 34 34 GLY H H 1 7.766 0.010 . 1 . . . . 34 GLY H . 17471 1 117 . 1 1 34 34 GLY CA C 13 45.176 0.250 . 1 . . . . 34 GLY CA . 17471 1 118 . 1 1 34 34 GLY N N 15 108.805 0.070 . 1 . . . . 34 GLY N . 17471 1 119 . 1 1 35 35 SER H H 1 8.347 0.010 . 1 . . . . 35 SER H . 17471 1 120 . 1 1 35 35 SER CA C 13 57.600 0.250 . 1 . . . . 35 SER CA . 17471 1 121 . 1 1 35 35 SER CB C 13 64.376 0.250 . 1 . . . . 35 SER CB . 17471 1 122 . 1 1 35 35 SER N N 15 115.586 0.070 . 1 . . . . 35 SER N . 17471 1 123 . 1 1 36 36 GLY H H 1 8.121 0.010 . 1 . . . . 36 GLY H . 17471 1 124 . 1 1 36 36 GLY CA C 13 44.406 0.250 . 1 . . . . 36 GLY CA . 17471 1 125 . 1 1 36 36 GLY N N 15 110.707 0.070 . 1 . . . . 36 GLY N . 17471 1 126 . 1 1 37 37 ALA H H 1 8.431 0.010 . 1 . . . . 37 ALA H . 17471 1 127 . 1 1 37 37 ALA CA C 13 53.557 0.250 . 1 . . . . 37 ALA CA . 17471 1 128 . 1 1 37 37 ALA CB C 13 17.558 0.250 . 1 . . . . 37 ALA CB . 17471 1 129 . 1 1 37 37 ALA N N 15 124.397 0.070 . 1 . . . . 37 ALA N . 17471 1 130 . 1 1 38 38 TYR H H 1 7.999 0.010 . 1 . . . . 38 TYR H . 17471 1 131 . 1 1 38 38 TYR CA C 13 56.770 0.250 . 1 . . . . 38 TYR CA . 17471 1 132 . 1 1 38 38 TYR CB C 13 37.213 0.250 . 1 . . . . 38 TYR CB . 17471 1 133 . 1 1 38 38 TYR N N 15 114.004 0.070 . 1 . . . . 38 TYR N . 17471 1 134 . 1 1 39 39 GLY H H 1 7.298 0.010 . 1 . . . . 39 GLY H . 17471 1 135 . 1 1 39 39 GLY CA C 13 45.149 0.250 . 1 . . . . 39 GLY CA . 17471 1 136 . 1 1 39 39 GLY N N 15 108.673 0.070 . 1 . . . . 39 GLY N . 17471 1 137 . 1 1 40 40 SER H H 1 8.096 0.010 . 1 . . . . 40 SER H . 17471 1 138 . 1 1 40 40 SER CA C 13 57.573 0.250 . 1 . . . . 40 SER CA . 17471 1 139 . 1 1 40 40 SER CB C 13 64.739 0.250 . 1 . . . . 40 SER CB . 17471 1 140 . 1 1 40 40 SER N N 15 116.281 0.070 . 1 . . . . 40 SER N . 17471 1 141 . 1 1 41 41 VAL H H 1 8.609 0.010 . 1 . . . . 41 VAL H . 17471 1 142 . 1 1 41 41 VAL CA C 13 60.973 0.250 . 1 . . . . 41 VAL CA . 17471 1 143 . 1 1 41 41 VAL CB C 13 34.210 0.250 . 1 . . . . 41 VAL CB . 17471 1 144 . 1 1 41 41 VAL N N 15 122.728 0.070 . 1 . . . . 41 VAL N . 17471 1 145 . 1 1 42 42 CYS H H 1 9.208 0.010 . 1 . . . . 42 CYS H . 17471 1 146 . 1 1 42 42 CYS CA C 13 57.573 0.250 . 1 . . . . 42 CYS CA . 17471 1 147 . 1 1 42 42 CYS CB C 13 30.593 0.250 . 1 . . . . 42 CYS CB . 17471 1 148 . 1 1 42 42 CYS N N 15 125.560 0.070 . 1 . . . . 42 CYS N . 17471 1 149 . 1 1 43 43 ALA H H 1 8.758 0.010 . 1 . . . . 43 ALA H . 17471 1 150 . 1 1 43 43 ALA CA C 13 50.263 0.250 . 1 . . . . 43 ALA CA . 17471 1 151 . 1 1 43 43 ALA CB C 13 19.810 0.250 . 1 . . . . 43 ALA CB . 17471 1 152 . 1 1 43 43 ALA N N 15 125.873 0.070 . 1 . . . . 43 ALA N . 17471 1 153 . 1 1 44 44 ALA H H 1 8.985 0.010 . 1 . . . . 44 ALA H . 17471 1 154 . 1 1 44 44 ALA CA C 13 50.263 0.250 . 1 . . . . 44 ALA CA . 17471 1 155 . 1 1 44 44 ALA CB C 13 22.327 0.250 . 1 . . . . 44 ALA CB . 17471 1 156 . 1 1 44 44 ALA N N 15 120.878 0.070 . 1 . . . . 44 ALA N . 17471 1 157 . 1 1 45 45 PHE H H 1 9.166 0.010 . 1 . . . . 45 PHE H . 17471 1 158 . 1 1 45 45 PHE CA C 13 56.743 0.250 . 1 . . . . 45 PHE CA . 17471 1 159 . 1 1 45 45 PHE CB C 13 40.353 0.250 . 1 . . . . 45 PHE CB . 17471 1 160 . 1 1 45 45 PHE N N 15 122.529 0.070 . 1 . . . . 45 PHE N . 17471 1 161 . 1 1 46 46 ASP H H 1 8.278 0.010 . 1 . . . . 46 ASP H . 17471 1 162 . 1 1 46 46 ASP CA C 13 51.549 0.250 . 1 . . . . 46 ASP CA . 17471 1 163 . 1 1 46 46 ASP CB C 13 40.694 0.250 . 1 . . . . 46 ASP CB . 17471 1 164 . 1 1 46 46 ASP N N 15 126.243 0.070 . 1 . . . . 46 ASP N . 17471 1 165 . 1 1 47 47 THR H H 1 8.883 0.010 . 1 . . . . 47 THR H . 17471 1 166 . 1 1 47 47 THR CA C 13 63.383 0.250 . 1 . . . . 47 THR CA . 17471 1 167 . 1 1 47 47 THR CB C 13 68.676 0.250 . 1 . . . . 47 THR CB . 17471 1 168 . 1 1 47 47 THR N N 15 117.609 0.070 . 1 . . . . 47 THR N . 17471 1 169 . 1 1 48 48 LYS H H 1 7.852 0.010 . 1 . . . . 48 LYS H . 17471 1 170 . 1 1 48 48 LYS CA C 13 58.215 0.250 . 1 . . . . 48 LYS CA . 17471 1 171 . 1 1 48 48 LYS CB C 13 31.685 0.250 . 1 . . . . 48 LYS CB . 17471 1 172 . 1 1 48 48 LYS N N 15 121.988 0.070 . 1 . . . . 48 LYS N . 17471 1 173 . 1 1 49 49 THR H H 1 6.545 0.010 . 1 . . . . 49 THR H . 17471 1 174 . 1 1 49 49 THR CA C 13 61.348 0.250 . 1 . . . . 49 THR CA . 17471 1 175 . 1 1 49 49 THR CB C 13 70.450 0.250 . 1 . . . . 49 THR CB . 17471 1 176 . 1 1 49 49 THR N N 15 105.262 0.070 . 1 . . . . 49 THR N . 17471 1 177 . 1 1 50 50 GLY H H 1 8.321 0.010 . 1 . . . . 50 GLY H . 17471 1 178 . 1 1 50 50 GLY CA C 13 45.566 0.250 . 1 . . . . 50 GLY CA . 17471 1 179 . 1 1 50 50 GLY N N 15 112.515 0.070 . 1 . . . . 50 GLY N . 17471 1 180 . 1 1 51 51 LEU H H 1 7.063 0.010 . 1 . . . . 51 LEU H . 17471 1 181 . 1 1 51 51 LEU CA C 13 53.289 0.250 . 1 . . . . 51 LEU CA . 17471 1 182 . 1 1 51 51 LEU CB C 13 43.083 0.250 . 1 . . . . 51 LEU CB . 17471 1 183 . 1 1 51 51 LEU N N 15 119.897 0.070 . 1 . . . . 51 LEU N . 17471 1 184 . 1 1 52 52 ARG H H 1 8.172 0.010 . 1 . . . . 52 ARG H . 17471 1 185 . 1 1 52 52 ARG CA C 13 55.565 0.250 . 1 . . . . 52 ARG CA . 17471 1 186 . 1 1 52 52 ARG CB C 13 29.501 0.250 . 1 . . . . 52 ARG CB . 17471 1 187 . 1 1 52 52 ARG N N 15 119.982 0.070 . 1 . . . . 52 ARG N . 17471 1 188 . 1 1 53 53 VAL H H 1 8.765 0.010 . 1 . . . . 53 VAL H . 17471 1 189 . 1 1 53 53 VAL CA C 13 59.019 0.250 . 1 . . . . 53 VAL CA . 17471 1 190 . 1 1 53 53 VAL CB C 13 34.347 0.250 . 1 . . . . 53 VAL CB . 17471 1 191 . 1 1 53 53 VAL N N 15 116.742 0.070 . 1 . . . . 53 VAL N . 17471 1 192 . 1 1 54 54 ALA H H 1 8.764 0.010 . 1 . . . . 54 ALA H . 17471 1 193 . 1 1 54 54 ALA CA C 13 49.674 0.250 . 1 . . . . 54 ALA CA . 17471 1 194 . 1 1 54 54 ALA CB C 13 19.537 0.250 . 1 . . . . 54 ALA CB . 17471 1 195 . 1 1 54 54 ALA N N 15 122.915 0.070 . 1 . . . . 54 ALA N . 17471 1 196 . 1 1 55 55 VAL H H 1 9.200 0.010 . 1 . . . . 55 VAL H . 17471 1 197 . 1 1 55 55 VAL CA C 13 60.224 0.250 . 1 . . . . 55 VAL CA . 17471 1 198 . 1 1 55 55 VAL CB C 13 31.753 0.250 . 1 . . . . 55 VAL CB . 17471 1 199 . 1 1 55 55 VAL N N 15 122.763 0.070 . 1 . . . . 55 VAL N . 17471 1 200 . 1 1 56 56 LYS H H 1 9.521 0.010 . 1 . . . . 56 LYS H . 17471 1 201 . 1 1 56 56 LYS CA C 13 53.717 0.250 . 1 . . . . 56 LYS CA . 17471 1 202 . 1 1 56 56 LYS CB C 13 34.142 0.250 . 1 . . . . 56 LYS CB . 17471 1 203 . 1 1 56 56 LYS N N 15 129.428 0.070 . 1 . . . . 56 LYS N . 17471 1 204 . 1 1 57 57 LYS H H 1 8.561 0.010 . 1 . . . . 57 LYS H . 17471 1 205 . 1 1 57 57 LYS CA C 13 53.985 0.250 . 1 . . . . 57 LYS CA . 17471 1 206 . 1 1 57 57 LYS CB C 13 32.914 0.250 . 1 . . . . 57 LYS CB . 17471 1 207 . 1 1 57 57 LYS N N 15 128.633 0.070 . 1 . . . . 57 LYS N . 17471 1 208 . 1 1 58 58 LEU H H 1 7.961 0.010 . 1 . . . . 58 LEU H . 17471 1 209 . 1 1 58 58 LEU CA C 13 54.869 0.250 . 1 . . . . 58 LEU CA . 17471 1 210 . 1 1 58 58 LEU CB C 13 39.192 0.250 . 1 . . . . 58 LEU CB . 17471 1 211 . 1 1 58 58 LEU N N 15 128.760 0.070 . 1 . . . . 58 LEU N . 17471 1 212 . 1 1 59 59 SER H H 1 7.980 0.010 . 1 . . . . 59 SER H . 17471 1 213 . 1 1 59 59 SER CA C 13 56.779 0.250 . 1 . . . . 59 SER CA . 17471 1 214 . 1 1 59 59 SER CB C 13 62.602 0.250 . 1 . . . . 59 SER CB . 17471 1 215 . 1 1 59 59 SER N N 15 118.104 0.070 . 1 . . . . 59 SER N . 17471 1 216 . 1 1 60 60 ARG H H 1 8.689 0.010 . 1 . . . . 60 ARG H . 17471 1 217 . 1 1 60 60 ARG CA C 13 55.672 0.250 . 1 . . . . 60 ARG CA . 17471 1 218 . 1 1 60 60 ARG CB C 13 28.614 0.250 . 1 . . . . 60 ARG CB . 17471 1 219 . 1 1 60 60 ARG N N 15 123.240 0.070 . 1 . . . . 60 ARG N . 17471 1 220 . 1 1 61 61 PRO CA C 13 63.811 0.250 . 1 . . . . 61 PRO CA . 17471 1 221 . 1 1 61 61 PRO CB C 13 30.866 0.250 . 1 . . . . 61 PRO CB . 17471 1 222 . 1 1 62 62 PHE H H 1 7.852 0.010 . 1 . . . . 62 PHE H . 17471 1 223 . 1 1 62 62 PHE CA C 13 54.146 0.250 . 1 . . . . 62 PHE CA . 17471 1 224 . 1 1 62 62 PHE CB C 13 37.281 0.250 . 1 . . . . 62 PHE CB . 17471 1 225 . 1 1 62 62 PHE N N 15 112.453 0.070 . 1 . . . . 62 PHE N . 17471 1 226 . 1 1 63 63 GLN H H 1 7.032 0.010 . 1 . . . . 63 GLN H . 17471 1 227 . 1 1 63 63 GLN CA C 13 57.184 0.250 . 1 . . . . 63 GLN CA . 17471 1 228 . 1 1 63 63 GLN CB C 13 28.682 0.250 . 1 . . . . 63 GLN CB . 17471 1 229 . 1 1 63 63 GLN N N 15 115.844 0.070 . 1 . . . . 63 GLN N . 17471 1 230 . 1 1 64 64 SER H H 1 7.382 0.010 . 1 . . . . 64 SER H . 17471 1 231 . 1 1 64 64 SER CA C 13 56.154 0.250 . 1 . . . . 64 SER CA . 17471 1 232 . 1 1 64 64 SER CB C 13 65.946 0.250 . 1 . . . . 64 SER CB . 17471 1 233 . 1 1 64 64 SER N N 15 110.593 0.070 . 1 . . . . 64 SER N . 17471 1 234 . 1 1 65 65 ILE H H 1 9.131 0.010 . 1 . . . . 65 ILE H . 17471 1 235 . 1 1 65 65 ILE CA C 13 65.257 0.250 . 1 . . . . 65 ILE CA . 17471 1 236 . 1 1 65 65 ILE CB C 13 36.872 0.250 . 1 . . . . 65 ILE CB . 17471 1 237 . 1 1 65 65 ILE N N 15 123.454 0.070 . 1 . . . . 65 ILE N . 17471 1 238 . 1 1 66 66 ILE H H 1 7.559 0.010 . 1 . . . . 66 ILE H . 17471 1 239 . 1 1 66 66 ILE CA C 13 63.811 0.250 . 1 . . . . 66 ILE CA . 17471 1 240 . 1 1 66 66 ILE CB C 13 36.736 0.250 . 1 . . . . 66 ILE CB . 17471 1 241 . 1 1 66 66 ILE N N 15 119.012 0.070 . 1 . . . . 66 ILE N . 17471 1 242 . 1 1 67 67 HIS CA C 13 60.491 0.250 . 1 . . . . 67 HIS CA . 17471 1 243 . 1 1 67 67 HIS CB C 13 29.453 0.250 . 1 . . . . 67 HIS CB . 17471 1 244 . 1 1 68 68 ALA H H 1 8.558 0.010 . 1 . . . . 68 ALA H . 17471 1 245 . 1 1 68 68 ALA CA C 13 54.761 0.250 . 1 . . . . 68 ALA CA . 17471 1 246 . 1 1 68 68 ALA CB C 13 18.513 0.250 . 1 . . . . 68 ALA CB . 17471 1 247 . 1 1 68 68 ALA N N 15 123.952 0.070 . 1 . . . . 68 ALA N . 17471 1 248 . 1 1 69 69 LYS H H 1 7.801 0.010 . 1 . . . . 69 LYS H . 17471 1 249 . 1 1 69 69 LYS CA C 13 59.153 0.250 . 1 . . . . 69 LYS CA . 17471 1 250 . 1 1 69 69 LYS CB C 13 31.412 0.250 . 1 . . . . 69 LYS CB . 17471 1 251 . 1 1 69 69 LYS N N 15 118.448 0.070 . 1 . . . . 69 LYS N . 17471 1 252 . 1 1 70 70 ARG H H 1 7.432 0.010 . 1 . . . . 70 ARG H . 17471 1 253 . 1 1 70 70 ARG CA C 13 58.809 0.250 . 1 . . . . 70 ARG CA . 17471 1 254 . 1 1 70 70 ARG CB C 13 28.630 0.250 . 1 . . . . 70 ARG CB . 17471 1 255 . 1 1 70 70 ARG N N 15 119.357 0.070 . 1 . . . . 70 ARG N . 17471 1 256 . 1 1 71 71 THR H H 1 8.346 0.010 . 1 . . . . 71 THR H . 17471 1 257 . 1 1 71 71 THR CA C 13 66.246 0.250 . 1 . . . . 71 THR CA . 17471 1 258 . 1 1 71 71 THR CB C 13 67.480 0.250 . 1 . . . . 71 THR CB . 17471 1 259 . 1 1 71 71 THR N N 15 119.966 0.070 . 1 . . . . 71 THR N . 17471 1 260 . 1 1 72 72 TYR H H 1 7.554 0.010 . 1 . . . . 72 TYR H . 17471 1 261 . 1 1 72 72 TYR CA C 13 62.205 0.250 . 1 . . . . 72 TYR CA . 17471 1 262 . 1 1 72 72 TYR CB C 13 37.469 0.250 . 1 . . . . 72 TYR CB . 17471 1 263 . 1 1 72 72 TYR N N 15 121.675 0.070 . 1 . . . . 72 TYR N . 17471 1 264 . 1 1 81 81 MET CA C 13 55.190 0.250 . 1 . . . . 81 MET CA . 17471 1 265 . 1 1 81 81 MET CB C 13 33.187 0.250 . 1 . . . . 81 MET CB . 17471 1 266 . 1 1 82 82 LYS H H 1 8.448 0.010 . 1 . . . . 82 LYS H . 17471 1 267 . 1 1 82 82 LYS CA C 13 54.119 0.250 . 1 . . . . 82 LYS CA . 17471 1 268 . 1 1 82 82 LYS CB C 13 31.753 0.250 . 1 . . . . 82 LYS CB . 17471 1 269 . 1 1 82 82 LYS N N 15 128.850 0.070 . 1 . . . . 82 LYS N . 17471 1 270 . 1 1 83 83 HIS H H 1 8.657 0.010 . 1 . . . . 83 HIS H . 17471 1 271 . 1 1 83 83 HIS CA C 13 56.957 0.250 . 1 . . . . 83 HIS CA . 17471 1 272 . 1 1 83 83 HIS CB C 13 32.641 0.250 . 1 . . . . 83 HIS CB . 17471 1 273 . 1 1 83 83 HIS N N 15 124.208 0.070 . 1 . . . . 83 HIS N . 17471 1 274 . 1 1 84 84 GLU H H 1 8.009 0.010 . 1 . . . . 84 GLU H . 17471 1 275 . 1 1 84 84 GLU CA C 13 59.179 0.250 . 1 . . . . 84 GLU CA . 17471 1 276 . 1 1 84 84 GLU CB C 13 29.365 0.250 . 1 . . . . 84 GLU CB . 17471 1 277 . 1 1 84 84 GLU N N 15 125.802 0.070 . 1 . . . . 84 GLU N . 17471 1 278 . 1 1 85 85 ASN H H 1 11.288 0.010 . 1 . . . . 85 ASN H . 17471 1 279 . 1 1 85 85 ASN CA C 13 53.236 0.250 . 1 . . . . 85 ASN CA . 17471 1 280 . 1 1 85 85 ASN CB C 13 40.507 0.250 . 1 . . . . 85 ASN CB . 17471 1 281 . 1 1 85 85 ASN N N 15 118.168 0.070 . 1 . . . . 85 ASN N . 17471 1 282 . 1 1 86 86 VAL H H 1 7.644 0.010 . 1 . . . . 86 VAL H . 17471 1 283 . 1 1 86 86 VAL CA C 13 61.134 0.250 . 1 . . . . 86 VAL CA . 17471 1 284 . 1 1 86 86 VAL CB C 13 35.071 0.250 . 1 . . . . 86 VAL CB . 17471 1 285 . 1 1 86 86 VAL N N 15 119.943 0.070 . 1 . . . . 86 VAL N . 17471 1 286 . 1 1 87 87 ILE H H 1 8.311 0.010 . 1 . . . . 87 ILE H . 17471 1 287 . 1 1 87 87 ILE CA C 13 61.134 0.250 . 1 . . . . 87 ILE CA . 17471 1 288 . 1 1 87 87 ILE CB C 13 37.880 0.250 . 1 . . . . 87 ILE CB . 17471 1 289 . 1 1 87 87 ILE N N 15 129.638 0.070 . 1 . . . . 87 ILE N . 17471 1 290 . 1 1 88 88 GLY H H 1 7.590 0.010 . 1 . . . . 88 GLY H . 17471 1 291 . 1 1 88 88 GLY CA C 13 43.088 0.250 . 1 . . . . 88 GLY CA . 17471 1 292 . 1 1 88 88 GLY N N 15 109.828 0.070 . 1 . . . . 88 GLY N . 17471 1 293 . 1 1 89 89 LEU H H 1 8.183 0.010 . 1 . . . . 89 LEU H . 17471 1 294 . 1 1 89 89 LEU CA C 13 54.226 0.250 . 1 . . . . 89 LEU CA . 17471 1 295 . 1 1 89 89 LEU CB C 13 42.265 0.250 . 1 . . . . 89 LEU CB . 17471 1 296 . 1 1 89 89 LEU N N 15 121.321 0.070 . 1 . . . . 89 LEU N . 17471 1 297 . 1 1 90 90 LEU H H 1 8.925 0.010 . 1 . . . . 90 LEU H . 17471 1 298 . 1 1 90 90 LEU CA C 13 55.431 0.250 . 1 . . . . 90 LEU CA . 17471 1 299 . 1 1 90 90 LEU CB C 13 42.167 0.250 . 1 . . . . 90 LEU CB . 17471 1 300 . 1 1 90 90 LEU N N 15 126.816 0.070 . 1 . . . . 90 LEU N . 17471 1 301 . 1 1 91 91 ASP CA C 13 52.619 0.250 . 1 . . . . 91 ASP CA . 17471 1 302 . 1 1 91 91 ASP CB C 13 41.717 0.250 . 1 . . . . 91 ASP CB . 17471 1 303 . 1 1 92 92 VAL H H 1 7.797 0.010 . 1 . . . . 92 VAL H . 17471 1 304 . 1 1 92 92 VAL CA C 13 59.153 0.250 . 1 . . . . 92 VAL CA . 17471 1 305 . 1 1 92 92 VAL CB C 13 32.504 0.250 . 1 . . . . 92 VAL CB . 17471 1 306 . 1 1 92 92 VAL N N 15 120.603 0.070 . 1 . . . . 92 VAL N . 17471 1 307 . 1 1 93 93 PHE H H 1 8.203 0.010 . 1 . . . . 93 PHE H . 17471 1 308 . 1 1 93 93 PHE CA C 13 55.565 0.250 . 1 . . . . 93 PHE CA . 17471 1 309 . 1 1 93 93 PHE CB C 13 40.964 0.250 . 1 . . . . 93 PHE CB . 17471 1 310 . 1 1 93 93 PHE N N 15 119.140 0.070 . 1 . . . . 93 PHE N . 17471 1 311 . 1 1 94 94 THR H H 1 8.891 0.010 . 1 . . . . 94 THR H . 17471 1 312 . 1 1 94 94 THR CA C 13 56.957 0.250 . 1 . . . . 94 THR CA . 17471 1 313 . 1 1 94 94 THR CB C 13 71.679 0.250 . 1 . . . . 94 THR CB . 17471 1 314 . 1 1 94 94 THR N N 15 113.768 0.070 . 1 . . . . 94 THR N . 17471 1 315 . 1 1 95 95 PRO CA C 13 62.151 0.250 . 1 . . . . 95 PRO CA . 17471 1 316 . 1 1 95 95 PRO CB C 13 30.320 0.250 . 1 . . . . 95 PRO CB . 17471 1 317 . 1 1 96 96 ALA H H 1 7.658 0.010 . 1 . . . . 96 ALA H . 17471 1 318 . 1 1 96 96 ALA CA C 13 52.405 0.250 . 1 . . . . 96 ALA CA . 17471 1 319 . 1 1 96 96 ALA CB C 13 19.878 0.250 . 1 . . . . 96 ALA CB . 17471 1 320 . 1 1 96 96 ALA N N 15 122.543 0.070 . 1 . . . . 96 ALA N . 17471 1 321 . 1 1 97 97 ARG H H 1 9.219 0.010 . 1 . . . . 97 ARG H . 17471 1 322 . 1 1 97 97 ARG CA C 13 55.591 0.250 . 1 . . . . 97 ARG CA . 17471 1 323 . 1 1 97 97 ARG CB C 13 29.706 0.250 . 1 . . . . 97 ARG CB . 17471 1 324 . 1 1 97 97 ARG N N 15 121.436 0.070 . 1 . . . . 97 ARG N . 17471 1 325 . 1 1 98 98 SER H H 1 7.335 0.010 . 1 . . . . 98 SER H . 17471 1 326 . 1 1 98 98 SER CA C 13 56.207 0.250 . 1 . . . . 98 SER CA . 17471 1 327 . 1 1 98 98 SER CB C 13 65.127 0.250 . 1 . . . . 98 SER CB . 17471 1 328 . 1 1 98 98 SER N N 15 111.570 0.070 . 1 . . . . 98 SER N . 17471 1 329 . 1 1 99 99 LEU H H 1 8.411 0.010 . 1 . . . . 99 LEU H . 17471 1 330 . 1 1 99 99 LEU CA C 13 56.582 0.250 . 1 . . . . 99 LEU CA . 17471 1 331 . 1 1 99 99 LEU CB C 13 40.278 0.250 . 1 . . . . 99 LEU CB . 17471 1 332 . 1 1 99 99 LEU N N 15 122.712 0.070 . 1 . . . . 99 LEU N . 17471 1 333 . 1 1 100 100 GLU H H 1 8.256 0.010 . 1 . . . . 100 GLU H . 17471 1 334 . 1 1 100 100 GLU CA C 13 58.992 0.250 . 1 . . . . 100 GLU CA . 17471 1 335 . 1 1 100 100 GLU CB C 13 28.068 0.250 . 1 . . . . 100 GLU CB . 17471 1 336 . 1 1 100 100 GLU N N 15 117.561 0.070 . 1 . . . . 100 GLU N . 17471 1 337 . 1 1 101 101 GLU H H 1 6.979 0.010 . 1 . . . . 101 GLU H . 17471 1 338 . 1 1 101 101 GLU CA C 13 54.467 0.250 . 1 . . . . 101 GLU CA . 17471 1 339 . 1 1 101 101 GLU CB C 13 30.115 0.250 . 1 . . . . 101 GLU CB . 17471 1 340 . 1 1 101 101 GLU N N 15 115.634 0.070 . 1 . . . . 101 GLU N . 17471 1 341 . 1 1 102 102 PHE H H 1 7.248 0.010 . 1 . . . . 102 PHE H . 17471 1 342 . 1 1 102 102 PHE CA C 13 56.540 0.250 . 1 . . . . 102 PHE CA . 17471 1 343 . 1 1 102 102 PHE CB C 13 37.964 0.250 . 1 . . . . 102 PHE CB . 17471 1 344 . 1 1 102 102 PHE N N 15 122.415 0.070 . 1 . . . . 102 PHE N . 17471 1 345 . 1 1 103 103 ASN H H 1 8.490 0.010 . 1 . . . . 103 ASN H . 17471 1 346 . 1 1 103 103 ASN CA C 13 53.776 0.250 . 1 . . . . 103 ASN CA . 17471 1 347 . 1 1 103 103 ASN CB C 13 41.581 0.250 . 1 . . . . 103 ASN CB . 17471 1 348 . 1 1 103 103 ASN N N 15 125.658 0.070 . 1 . . . . 103 ASN N . 17471 1 349 . 1 1 104 104 ASP H H 1 7.575 0.010 . 1 . . . . 104 ASP H . 17471 1 350 . 1 1 104 104 ASP CA C 13 52.860 0.250 . 1 . . . . 104 ASP CA . 17471 1 351 . 1 1 104 104 ASP CB C 13 43.833 0.250 . 1 . . . . 104 ASP CB . 17471 1 352 . 1 1 104 104 ASP N N 15 116.118 0.070 . 1 . . . . 104 ASP N . 17471 1 353 . 1 1 105 105 VAL H H 1 8.412 0.010 . 1 . . . . 105 VAL H . 17471 1 354 . 1 1 105 105 VAL CA C 13 61.214 0.250 . 1 . . . . 105 VAL CA . 17471 1 355 . 1 1 105 105 VAL CB C 13 34.620 0.250 . 1 . . . . 105 VAL CB . 17471 1 356 . 1 1 105 105 VAL N N 15 121.405 0.070 . 1 . . . . 105 VAL N . 17471 1 357 . 1 1 106 106 TYR H H 1 8.047 0.010 . 1 . . . . 106 TYR H . 17471 1 358 . 1 1 106 106 TYR CA C 13 54.595 0.250 . 1 . . . . 106 TYR CA . 17471 1 359 . 1 1 106 106 TYR CB C 13 39.182 0.250 . 1 . . . . 106 TYR CB . 17471 1 360 . 1 1 106 106 TYR N N 15 124.881 0.070 . 1 . . . . 106 TYR N . 17471 1 361 . 1 1 107 107 LEU H H 1 8.790 0.010 . 1 . . . . 107 LEU H . 17471 1 362 . 1 1 107 107 LEU CA C 13 53.101 0.250 . 1 . . . . 107 LEU CA . 17471 1 363 . 1 1 107 107 LEU CB C 13 43.560 0.250 . 1 . . . . 107 LEU CB . 17471 1 364 . 1 1 107 107 LEU N N 15 119.729 0.070 . 1 . . . . 107 LEU N . 17471 1 365 . 1 1 108 108 VAL CA C 13 60.518 0.250 . 1 . . . . 108 VAL CA . 17471 1 366 . 1 1 108 108 VAL CB C 13 31.753 0.250 . 1 . . . . 108 VAL CB . 17471 1 367 . 1 1 109 109 THR H H 1 8.970 0.010 . 1 . . . . 109 THR H . 17471 1 368 . 1 1 109 109 THR CA C 13 59.153 0.250 . 1 . . . . 109 THR CA . 17471 1 369 . 1 1 109 109 THR CB C 13 72.839 0.250 . 1 . . . . 109 THR CB . 17471 1 370 . 1 1 109 109 THR N N 15 118.292 0.070 . 1 . . . . 109 THR N . 17471 1 371 . 1 1 110 110 HIS H H 1 8.849 0.010 . 1 . . . . 110 HIS H . 17471 1 372 . 1 1 110 110 HIS CA C 13 58.537 0.250 . 1 . . . . 110 HIS CA . 17471 1 373 . 1 1 110 110 HIS CB C 13 31.029 0.250 . 1 . . . . 110 HIS CB . 17471 1 374 . 1 1 110 110 HIS N N 15 119.612 0.070 . 1 . . . . 110 HIS N . 17471 1 375 . 1 1 111 111 LEU H H 1 8.153 0.010 . 1 . . . . 111 LEU H . 17471 1 376 . 1 1 111 111 LEU CA C 13 54.119 0.250 . 1 . . . . 111 LEU CA . 17471 1 377 . 1 1 111 111 LEU CB C 13 41.376 0.250 . 1 . . . . 111 LEU CB . 17471 1 378 . 1 1 111 111 LEU N N 15 125.617 0.070 . 1 . . . . 111 LEU N . 17471 1 379 . 1 1 112 112 MET H H 1 8.633 0.010 . 1 . . . . 112 MET H . 17471 1 380 . 1 1 112 112 MET CA C 13 54.949 0.250 . 1 . . . . 112 MET CA . 17471 1 381 . 1 1 112 112 MET CB C 13 31.440 0.250 . 1 . . . . 112 MET CB . 17471 1 382 . 1 1 112 112 MET N N 15 126.200 0.070 . 1 . . . . 112 MET N . 17471 1 383 . 1 1 113 113 GLY H H 1 8.075 0.010 . 1 . . . . 113 GLY H . 17471 1 384 . 1 1 113 113 GLY CA C 13 45.417 0.250 . 1 . . . . 113 GLY CA . 17471 1 385 . 1 1 113 113 GLY N N 15 108.863 0.070 . 1 . . . . 113 GLY N . 17471 1 386 . 1 1 114 114 ALA H H 1 7.825 0.010 . 1 . . . . 114 ALA H . 17471 1 387 . 1 1 114 114 ALA CA C 13 51.013 0.250 . 1 . . . . 114 ALA CA . 17471 1 388 . 1 1 114 114 ALA CB C 13 20.203 0.250 . 1 . . . . 114 ALA CB . 17471 1 389 . 1 1 114 114 ALA N N 15 124.052 0.070 . 1 . . . . 114 ALA N . 17471 1 390 . 1 1 115 115 ASP H H 1 7.932 0.010 . 1 . . . . 115 ASP H . 17471 1 391 . 1 1 115 115 ASP CA C 13 52.030 0.250 . 1 . . . . 115 ASP CA . 17471 1 392 . 1 1 115 115 ASP CB C 13 41.854 0.250 . 1 . . . . 115 ASP CB . 17471 1 393 . 1 1 115 115 ASP N N 15 118.747 0.070 . 1 . . . . 115 ASP N . 17471 1 394 . 1 1 116 116 LEU H H 1 7.769 0.010 . 1 . . . . 116 LEU H . 17471 1 395 . 1 1 116 116 LEU CA C 13 56.850 0.250 . 1 . . . . 116 LEU CA . 17471 1 396 . 1 1 116 116 LEU CB C 13 41.240 0.250 . 1 . . . . 116 LEU CB . 17471 1 397 . 1 1 116 116 LEU N N 15 117.746 0.070 . 1 . . . . 116 LEU N . 17471 1 398 . 1 1 117 117 ASN H H 1 7.634 0.010 . 1 . . . . 117 ASN H . 17471 1 399 . 1 1 117 117 ASN CA C 13 55.565 0.250 . 1 . . . . 117 ASN CA . 17471 1 400 . 1 1 117 117 ASN CB C 13 37.554 0.250 . 1 . . . . 117 ASN CB . 17471 1 401 . 1 1 117 117 ASN N N 15 115.928 0.070 . 1 . . . . 117 ASN N . 17471 1 402 . 1 1 118 118 ASN H H 1 7.927 0.010 . 1 . . . . 118 ASN H . 17471 1 403 . 1 1 118 118 ASN CA C 13 55.966 0.250 . 1 . . . . 118 ASN CA . 17471 1 404 . 1 1 118 118 ASN CB C 13 39.056 0.250 . 1 . . . . 118 ASN CB . 17471 1 405 . 1 1 118 118 ASN N N 15 118.374 0.070 . 1 . . . . 118 ASN N . 17471 1 406 . 1 1 119 119 ILE H H 1 7.449 0.010 . 1 . . . . 119 ILE H . 17471 1 407 . 1 1 119 119 ILE CA C 13 62.847 0.250 . 1 . . . . 119 ILE CA . 17471 1 408 . 1 1 119 119 ILE CB C 13 36.190 0.250 . 1 . . . . 119 ILE CB . 17471 1 409 . 1 1 119 119 ILE N N 15 118.978 0.070 . 1 . . . . 119 ILE N . 17471 1 410 . 1 1 120 120 VAL H H 1 7.482 0.010 . 1 . . . . 120 VAL H . 17471 1 411 . 1 1 120 120 VAL CA C 13 64.106 0.250 . 1 . . . . 120 VAL CA . 17471 1 412 . 1 1 120 120 VAL CB C 13 30.661 0.250 . 1 . . . . 120 VAL CB . 17471 1 413 . 1 1 120 120 VAL N N 15 116.779 0.070 . 1 . . . . 120 VAL N . 17471 1 414 . 1 1 121 121 LYS H H 1 7.343 0.010 . 1 . . . . 121 LYS H . 17471 1 415 . 1 1 121 121 LYS CA C 13 57.359 0.250 . 1 . . . . 121 LYS CA . 17471 1 416 . 1 1 121 121 LYS CB C 13 31.753 0.250 . 1 . . . . 121 LYS CB . 17471 1 417 . 1 1 121 121 LYS N N 15 117.668 0.070 . 1 . . . . 121 LYS N . 17471 1 418 . 1 1 122 122 CYS H H 1 7.612 0.010 . 1 . . . . 122 CYS H . 17471 1 419 . 1 1 122 122 CYS CA C 13 59.340 0.250 . 1 . . . . 122 CYS CA . 17471 1 420 . 1 1 122 122 CYS CB C 13 28.614 0.250 . 1 . . . . 122 CYS CB . 17471 1 421 . 1 1 122 122 CYS N N 15 114.705 0.070 . 1 . . . . 122 CYS N . 17471 1 422 . 1 1 123 123 GLN H H 1 7.948 0.010 . 1 . . . . 123 GLN H . 17471 1 423 . 1 1 123 123 GLN CA C 13 54.547 0.250 . 1 . . . . 123 GLN CA . 17471 1 424 . 1 1 123 123 GLN CB C 13 30.115 0.250 . 1 . . . . 123 GLN CB . 17471 1 425 . 1 1 123 123 GLN N N 15 119.718 0.070 . 1 . . . . 123 GLN N . 17471 1 426 . 1 1 124 124 LYS H H 1 8.169 0.010 . 1 . . . . 124 LYS H . 17471 1 427 . 1 1 124 124 LYS CA C 13 54.815 0.250 . 1 . . . . 124 LYS CA . 17471 1 428 . 1 1 124 124 LYS CB C 13 30.934 0.250 . 1 . . . . 124 LYS CB . 17471 1 429 . 1 1 124 124 LYS N N 15 122.116 0.070 . 1 . . . . 124 LYS N . 17471 1 430 . 1 1 125 125 LEU H H 1 8.508 0.010 . 1 . . . . 125 LEU H . 17471 1 431 . 1 1 125 125 LEU CA C 13 54.039 0.250 . 1 . . . . 125 LEU CA . 17471 1 432 . 1 1 125 125 LEU CB C 13 41.649 0.250 . 1 . . . . 125 LEU CB . 17471 1 433 . 1 1 125 125 LEU N N 15 127.011 0.070 . 1 . . . . 125 LEU N . 17471 1 434 . 1 1 126 126 THR CA C 13 60.170 0.250 . 1 . . . . 126 THR CA . 17471 1 435 . 1 1 126 126 THR CB C 13 70.928 0.250 . 1 . . . . 126 THR CB . 17471 1 436 . 1 1 127 127 ASP H H 1 8.910 0.010 . 1 . . . . 127 ASP H . 17471 1 437 . 1 1 127 127 ASP CA C 13 58.055 0.250 . 1 . . . . 127 ASP CA . 17471 1 438 . 1 1 127 127 ASP CB C 13 42.127 0.250 . 1 . . . . 127 ASP CB . 17471 1 439 . 1 1 127 127 ASP N N 15 121.220 0.070 . 1 . . . . 127 ASP N . 17471 1 440 . 1 1 128 128 ASP H H 1 7.987 0.010 . 1 . . . . 128 ASP H . 17471 1 441 . 1 1 128 128 ASP CA C 13 56.957 0.250 . 1 . . . . 128 ASP CA . 17471 1 442 . 1 1 128 128 ASP CB C 13 39.807 0.250 . 1 . . . . 128 ASP CB . 17471 1 443 . 1 1 128 128 ASP N N 15 115.626 0.070 . 1 . . . . 128 ASP N . 17471 1 444 . 1 1 129 129 HIS H H 1 7.477 0.010 . 1 . . . . 129 HIS H . 17471 1 445 . 1 1 129 129 HIS CA C 13 59.527 0.250 . 1 . . . . 129 HIS CA . 17471 1 446 . 1 1 129 129 HIS CB C 13 31.207 0.250 . 1 . . . . 129 HIS CB . 17471 1 447 . 1 1 129 129 HIS N N 15 119.357 0.070 . 1 . . . . 129 HIS N . 17471 1 448 . 1 1 130 130 VAL H H 1 8.115 0.010 . 1 . . . . 130 VAL H . 17471 1 449 . 1 1 130 130 VAL CA C 13 68.023 0.250 . 1 . . . . 130 VAL CA . 17471 1 450 . 1 1 130 130 VAL CB C 13 29.842 0.250 . 1 . . . . 130 VAL CB . 17471 1 451 . 1 1 130 130 VAL N N 15 120.595 0.070 . 1 . . . . 130 VAL N . 17471 1 452 . 1 1 131 131 GLN H H 1 8.365 0.010 . 1 . . . . 131 GLN H . 17471 1 453 . 1 1 131 131 GLN CA C 13 58.965 0.250 . 1 . . . . 131 GLN CA . 17471 1 454 . 1 1 131 131 GLN CB C 13 29.365 0.250 . 1 . . . . 131 GLN CB . 17471 1 455 . 1 1 131 131 GLN N N 15 118.481 0.070 . 1 . . . . 131 GLN N . 17471 1 456 . 1 1 132 132 PHE H H 1 7.398 0.010 . 1 . . . . 132 PHE H . 17471 1 457 . 1 1 132 132 PHE CA C 13 58.135 0.250 . 1 . . . . 132 PHE CA . 17471 1 458 . 1 1 132 132 PHE CB C 13 38.988 0.250 . 1 . . . . 132 PHE CB . 17471 1 459 . 1 1 132 132 PHE N N 15 116.511 0.070 . 1 . . . . 132 PHE N . 17471 1 460 . 1 1 133 133 LEU H H 1 8.705 0.010 . 1 . . . . 133 LEU H . 17471 1 461 . 1 1 133 133 LEU CA C 13 58.165 0.250 . 1 . . . . 133 LEU CA . 17471 1 462 . 1 1 133 133 LEU CB C 13 41.581 0.250 . 1 . . . . 133 LEU CB . 17471 1 463 . 1 1 133 133 LEU N N 15 120.915 0.070 . 1 . . . . 133 LEU N . 17471 1 464 . 1 1 134 134 ILE CA C 13 55.645 0.250 . 1 . . . . 134 ILE CA . 17471 1 465 . 1 1 135 135 TYR H H 1 8.862 0.010 . 1 . . . . 135 TYR H . 17471 1 466 . 1 1 135 135 TYR CA C 13 51.388 0.250 . 1 . . . . 135 TYR CA . 17471 1 467 . 1 1 135 135 TYR CB C 13 39.124 0.250 . 1 . . . . 135 TYR CB . 17471 1 468 . 1 1 135 135 TYR N N 15 120.118 0.070 . 1 . . . . 135 TYR N . 17471 1 469 . 1 1 136 136 GLN H H 1 8.519 0.010 . 1 . . . . 136 GLN H . 17471 1 470 . 1 1 136 136 GLN CA C 13 51.388 0.250 . 1 . . . . 136 GLN CA . 17471 1 471 . 1 1 136 136 GLN CB C 13 25.890 0.250 . 1 . . . . 136 GLN CB . 17471 1 472 . 1 1 136 136 GLN N N 15 116.659 0.070 . 1 . . . . 136 GLN N . 17471 1 473 . 1 1 139 139 ARG CA C 13 59.956 0.250 . 1 . . . . 139 ARG CA . 17471 1 474 . 1 1 140 140 GLY H H 1 8.089 0.010 . 1 . . . . 140 GLY H . 17471 1 475 . 1 1 140 140 GLY CA C 13 46.595 0.250 . 1 . . . . 140 GLY CA . 17471 1 476 . 1 1 140 140 GLY N N 15 107.443 0.070 . 1 . . . . 140 GLY N . 17471 1 477 . 1 1 141 141 LEU H H 1 8.633 0.010 . 1 . . . . 141 LEU H . 17471 1 478 . 1 1 141 141 LEU CA C 13 56.368 0.250 . 1 . . . . 141 LEU CA . 17471 1 479 . 1 1 141 141 LEU CB C 13 40.347 0.250 . 1 . . . . 141 LEU CB . 17471 1 480 . 1 1 141 141 LEU N N 15 121.832 0.070 . 1 . . . . 141 LEU N . 17471 1 481 . 1 1 142 142 LYS H H 1 8.625 0.010 . 1 . . . . 142 LYS H . 17471 1 482 . 1 1 142 142 LYS CA C 13 59.447 0.250 . 1 . . . . 142 LYS CA . 17471 1 483 . 1 1 142 142 LYS CB C 13 31.412 0.250 . 1 . . . . 142 LYS CB . 17471 1 484 . 1 1 142 142 LYS N N 15 119.584 0.070 . 1 . . . . 142 LYS N . 17471 1 485 . 1 1 143 143 TYR H H 1 6.781 0.010 . 1 . . . . 143 TYR H . 17471 1 486 . 1 1 143 143 TYR CA C 13 61.428 0.250 . 1 . . . . 143 TYR CA . 17471 1 487 . 1 1 143 143 TYR CB C 13 37.350 0.250 . 1 . . . . 143 TYR CB . 17471 1 488 . 1 1 143 143 TYR N N 15 118.435 0.070 . 1 . . . . 143 TYR N . 17471 1 489 . 1 1 144 144 ILE H H 1 8.398 0.010 . 1 . . . . 144 ILE H . 17471 1 490 . 1 1 144 144 ILE CA C 13 66.315 0.250 . 1 . . . . 144 ILE CA . 17471 1 491 . 1 1 144 144 ILE CB C 13 37.469 0.250 . 1 . . . . 144 ILE CB . 17471 1 492 . 1 1 144 144 ILE N N 15 120.323 0.070 . 1 . . . . 144 ILE N . 17471 1 493 . 1 1 145 145 HIS H H 1 9.463 0.010 . 1 . . . . 145 HIS H . 17471 1 494 . 1 1 145 145 HIS CA C 13 56.850 0.250 . 1 . . . . 145 HIS CA . 17471 1 495 . 1 1 145 145 HIS CB C 13 30.184 0.250 . 1 . . . . 145 HIS CB . 17471 1 496 . 1 1 145 145 HIS N N 15 119.879 0.070 . 1 . . . . 145 HIS N . 17471 1 497 . 1 1 146 146 SER H H 1 7.824 0.010 . 1 . . . . 146 SER H . 17471 1 498 . 1 1 146 146 SER CA C 13 60.920 0.250 . 1 . . . . 146 SER CA . 17471 1 499 . 1 1 146 146 SER CB C 13 61.861 0.250 . 1 . . . . 146 SER CB . 17471 1 500 . 1 1 146 146 SER N N 15 116.726 0.070 . 1 . . . . 146 SER N . 17471 1 501 . 1 1 147 147 ALA H H 1 7.364 0.010 . 1 . . . . 147 ALA H . 17471 1 502 . 1 1 147 147 ALA CA C 13 51.013 0.250 . 1 . . . . 147 ALA CA . 17471 1 503 . 1 1 147 147 ALA CB C 13 17.257 0.250 . 1 . . . . 147 ALA CB . 17471 1 504 . 1 1 147 147 ALA N N 15 126.542 0.070 . 1 . . . . 147 ALA N . 17471 1 505 . 1 1 148 148 ASP H H 1 8.147 0.010 . 1 . . . . 148 ASP H . 17471 1 506 . 1 1 148 148 ASP CA C 13 55.190 0.250 . 1 . . . . 148 ASP CA . 17471 1 507 . 1 1 148 148 ASP CB C 13 38.510 0.250 . 1 . . . . 148 ASP CB . 17471 1 508 . 1 1 148 148 ASP N N 15 115.457 0.070 . 1 . . . . 148 ASP N . 17471 1 509 . 1 1 149 149 ILE H H 1 7.192 0.010 . 1 . . . . 149 ILE H . 17471 1 510 . 1 1 149 149 ILE CA C 13 58.965 0.250 . 1 . . . . 149 ILE CA . 17471 1 511 . 1 1 149 149 ILE CB C 13 38.419 0.250 . 1 . . . . 149 ILE CB . 17471 1 512 . 1 1 149 149 ILE N N 15 119.258 0.070 . 1 . . . . 149 ILE N . 17471 1 513 . 1 1 150 150 ILE H H 1 7.792 0.010 . 1 . . . . 150 ILE H . 17471 1 514 . 1 1 150 150 ILE CA C 13 59.688 0.250 . 1 . . . . 150 ILE CA . 17471 1 515 . 1 1 150 150 ILE CB C 13 39.730 0.250 . 1 . . . . 150 ILE CB . 17471 1 516 . 1 1 150 150 ILE N N 15 123.300 0.070 . 1 . . . . 150 ILE N . 17471 1 517 . 1 1 151 151 HIS H H 1 7.360 0.010 . 1 . . . . 151 HIS H . 17471 1 518 . 1 1 151 151 HIS CA C 13 62.473 0.250 . 1 . . . . 151 HIS CA . 17471 1 519 . 1 1 151 151 HIS CB C 13 35.423 0.250 . 1 . . . . 151 HIS CB . 17471 1 520 . 1 1 151 151 HIS N N 15 121.123 0.070 . 1 . . . . 151 HIS N . 17471 1 521 . 1 1 157 157 SER H H 1 7.484 0.010 . 1 . . . . 157 SER H . 17471 1 522 . 1 1 157 157 SER CA C 13 59.313 0.250 . 1 . . . . 157 SER CA . 17471 1 523 . 1 1 157 157 SER CB C 13 62.125 0.250 . 1 . . . . 157 SER CB . 17471 1 524 . 1 1 157 157 SER N N 15 106.345 0.070 . 1 . . . . 157 SER N . 17471 1 525 . 1 1 158 158 ASN H H 1 7.742 0.010 . 1 . . . . 158 ASN H . 17471 1 526 . 1 1 158 158 ASN CA C 13 52.352 0.250 . 1 . . . . 158 ASN CA . 17471 1 527 . 1 1 158 158 ASN CB C 13 37.829 0.250 . 1 . . . . 158 ASN CB . 17471 1 528 . 1 1 158 158 ASN N N 15 119.241 0.070 . 1 . . . . 158 ASN N . 17471 1 529 . 1 1 159 159 LEU H H 1 7.010 0.010 . 1 . . . . 159 LEU H . 17471 1 530 . 1 1 159 159 LEU CA C 13 52.566 0.250 . 1 . . . . 159 LEU CA . 17471 1 531 . 1 1 159 159 LEU CB C 13 42.059 0.250 . 1 . . . . 159 LEU CB . 17471 1 532 . 1 1 159 159 LEU N N 15 119.484 0.070 . 1 . . . . 159 LEU N . 17471 1 533 . 1 1 160 160 ALA H H 1 8.497 0.010 . 1 . . . . 160 ALA H . 17471 1 534 . 1 1 160 160 ALA CA C 13 50.290 0.250 . 1 . . . . 160 ALA CA . 17471 1 535 . 1 1 160 160 ALA CB C 13 20.834 0.250 . 1 . . . . 160 ALA CB . 17471 1 536 . 1 1 160 160 ALA N N 15 125.759 0.070 . 1 . . . . 160 ALA N . 17471 1 537 . 1 1 161 161 VAL H H 1 8.123 0.010 . 1 . . . . 161 VAL H . 17471 1 538 . 1 1 161 161 VAL CA C 13 59.045 0.250 . 1 . . . . 161 VAL CA . 17471 1 539 . 1 1 161 161 VAL CB C 13 34.961 0.250 . 1 . . . . 161 VAL CB . 17471 1 540 . 1 1 161 161 VAL N N 15 118.135 0.070 . 1 . . . . 161 VAL N . 17471 1 541 . 1 1 162 162 ASN H H 1 7.844 0.010 . 1 . . . . 162 ASN H . 17471 1 542 . 1 1 162 162 ASN CA C 13 50.129 0.250 . 1 . . . . 162 ASN CA . 17471 1 543 . 1 1 162 162 ASN CB C 13 39.261 0.250 . 1 . . . . 162 ASN CB . 17471 1 544 . 1 1 162 162 ASN N N 15 122.501 0.070 . 1 . . . . 162 ASN N . 17471 1 545 . 1 1 163 163 GLU H H 1 8.798 0.010 . 1 . . . . 163 GLU H . 17471 1 546 . 1 1 163 163 GLU CA C 13 58.762 0.250 . 1 . . . . 163 GLU CA . 17471 1 547 . 1 1 163 163 GLU CB C 13 28.136 0.250 . 1 . . . . 163 GLU CB . 17471 1 548 . 1 1 163 163 GLU N N 15 117.831 0.070 . 1 . . . . 163 GLU N . 17471 1 549 . 1 1 164 164 ASP H H 1 7.470 0.010 . 1 . . . . 164 ASP H . 17471 1 550 . 1 1 164 164 ASP CA C 13 53.985 0.250 . 1 . . . . 164 ASP CA . 17471 1 551 . 1 1 164 164 ASP CB C 13 40.557 0.250 . 1 . . . . 164 ASP CB . 17471 1 552 . 1 1 164 164 ASP N N 15 118.914 0.070 . 1 . . . . 164 ASP N . 17471 1 553 . 1 1 165 165 CYS H H 1 8.248 0.010 . 1 . . . . 165 CYS H . 17471 1 554 . 1 1 165 165 CYS CA C 13 62.125 0.250 . 1 . . . . 165 CYS CA . 17471 1 555 . 1 1 165 165 CYS CB C 13 24.382 0.250 . 1 . . . . 165 CYS CB . 17471 1 556 . 1 1 165 165 CYS N N 15 111.527 0.070 . 1 . . . . 165 CYS N . 17471 1 557 . 1 1 166 166 GLU H H 1 7.622 0.010 . 1 . . . . 166 GLU H . 17471 1 558 . 1 1 166 166 GLU CA C 13 55.806 0.250 . 1 . . . . 166 GLU CA . 17471 1 559 . 1 1 166 166 GLU CB C 13 28.273 0.250 . 1 . . . . 166 GLU CB . 17471 1 560 . 1 1 166 166 GLU N N 15 117.983 0.070 . 1 . . . . 166 GLU N . 17471 1 561 . 1 1 167 167 LEU H H 1 7.924 0.010 . 1 . . . . 167 LEU H . 17471 1 562 . 1 1 167 167 LEU CA C 13 53.289 0.250 . 1 . . . . 167 LEU CA . 17471 1 563 . 1 1 167 167 LEU CB C 13 45.335 0.250 . 1 . . . . 167 LEU CB . 17471 1 564 . 1 1 167 167 LEU N N 15 125.603 0.070 . 1 . . . . 167 LEU N . 17471 1 565 . 1 1 168 168 LYS H H 1 8.931 0.010 . 1 . . . . 168 LYS H . 17471 1 566 . 1 1 168 168 LYS CB C 13 37.213 0.250 . 1 . . . . 168 LYS CB . 17471 1 567 . 1 1 168 168 LYS N N 15 122.956 0.070 . 1 . . . . 168 LYS N . 17471 1 568 . 1 1 169 169 ILE H H 1 8.167 0.010 . 1 . . . . 169 ILE H . 17471 1 569 . 1 1 169 169 ILE CA C 13 62.124 0.250 . 1 . . . . 169 ILE CA . 17471 1 570 . 1 1 169 169 ILE CB C 13 38.908 0.250 . 1 . . . . 169 ILE CB . 17471 1 571 . 1 1 169 169 ILE N N 15 122.261 0.070 . 1 . . . . 169 ILE N . 17471 1 572 . 1 1 170 170 LEU H H 1 8.403 0.010 . 1 . . . . 170 LEU H . 17471 1 573 . 1 1 170 170 LEU CA C 13 54.146 0.250 . 1 . . . . 170 LEU CA . 17471 1 574 . 1 1 170 170 LEU CB C 13 43.156 0.250 . 1 . . . . 170 LEU CB . 17471 1 575 . 1 1 170 170 LEU N N 15 125.543 0.070 . 1 . . . . 170 LEU N . 17471 1 576 . 1 1 174 174 LEU CA C 13 54.440 0.250 . 1 . . . . 174 LEU CA . 17471 1 577 . 1 1 174 174 LEU CB C 13 40.484 0.250 . 1 . . . . 174 LEU CB . 17471 1 578 . 1 1 175 175 ALA H H 1 8.028 0.010 . 1 . . . . 175 ALA H . 17471 1 579 . 1 1 175 175 ALA CA C 13 59.665 0.250 . 1 . . . . 175 ALA CA . 17471 1 580 . 1 1 175 175 ALA CB C 13 18.010 0.250 . 1 . . . . 175 ALA CB . 17471 1 581 . 1 1 175 175 ALA N N 15 119.416 0.070 . 1 . . . . 175 ALA N . 17471 1 582 . 1 1 176 176 ARG H H 1 8.348 0.010 . 1 . . . . 176 ARG H . 17471 1 583 . 1 1 176 176 ARG CA C 13 55.270 0.250 . 1 . . . . 176 ARG CA . 17471 1 584 . 1 1 176 176 ARG CB C 13 37.264 0.250 . 1 . . . . 176 ARG CB . 17471 1 585 . 1 1 176 176 ARG N N 15 117.319 0.070 . 1 . . . . 176 ARG N . 17471 1 586 . 1 1 177 177 HIS CA C 13 59.340 0.250 . 1 . . . . 177 HIS CA . 17471 1 587 . 1 1 177 177 HIS CB C 13 27.277 0.250 . 1 . . . . 177 HIS CB . 17471 1 588 . 1 1 178 178 THR H H 1 7.248 0.010 . 1 . . . . 178 THR H . 17471 1 589 . 1 1 178 178 THR CA C 13 55.940 0.250 . 1 . . . . 178 THR CA . 17471 1 590 . 1 1 178 178 THR CB C 13 62.942 0.250 . 1 . . . . 178 THR CB . 17471 1 591 . 1 1 178 178 THR N N 15 115.565 0.070 . 1 . . . . 178 THR N . 17471 1 592 . 1 1 179 179 ASP CA C 13 54.654 0.250 . 1 . . . . 179 ASP CA . 17471 1 593 . 1 1 179 179 ASP CB C 13 40.284 0.250 . 1 . . . . 179 ASP CB . 17471 1 594 . 1 1 180 180 ASP H H 1 8.043 0.010 . 1 . . . . 180 ASP H . 17471 1 595 . 1 1 180 180 ASP CA C 13 54.547 0.250 . 1 . . . . 180 ASP CA . 17471 1 596 . 1 1 180 180 ASP CB C 13 40.454 0.250 . 1 . . . . 180 ASP CB . 17471 1 597 . 1 1 180 180 ASP N N 15 120.257 0.070 . 1 . . . . 180 ASP N . 17471 1 598 . 1 1 181 181 GLU H H 1 8.083 0.010 . 1 . . . . 181 GLU H . 17471 1 599 . 1 1 181 181 GLU CA C 13 56.745 0.250 . 1 . . . . 181 GLU CA . 17471 1 600 . 1 1 181 181 GLU CB C 13 29.160 0.250 . 1 . . . . 181 GLU CB . 17471 1 601 . 1 1 181 181 GLU N N 15 120.550 0.070 . 1 . . . . 181 GLU N . 17471 1 602 . 1 1 182 182 MET H H 1 8.108 0.010 . 1 . . . . 182 MET H . 17471 1 603 . 1 1 182 182 MET CA C 13 55.511 0.250 . 1 . . . . 182 MET CA . 17471 1 604 . 1 1 182 182 MET CB C 13 31.549 0.250 . 1 . . . . 182 MET CB . 17471 1 605 . 1 1 182 182 MET N N 15 120.172 0.070 . 1 . . . . 182 MET N . 17471 1 606 . 1 1 183 183 THR H H 1 7.878 0.010 . 1 . . . . 183 THR H . 17471 1 607 . 1 1 183 183 THR CA C 13 62.151 0.250 . 1 . . . . 183 THR CA . 17471 1 608 . 1 1 183 183 THR CB C 13 69.017 0.250 . 1 . . . . 183 THR CB . 17471 1 609 . 1 1 183 183 THR N N 15 114.220 0.070 . 1 . . . . 183 THR N . 17471 1 610 . 1 1 184 184 GLY H H 1 8.208 0.010 . 1 . . . . 184 GLY H . 17471 1 611 . 1 1 184 184 GLY CA C 13 44.908 0.250 . 1 . . . . 184 GLY CA . 17471 1 612 . 1 1 184 184 GLY N N 15 111.449 0.070 . 1 . . . . 184 GLY N . 17471 1 613 . 1 1 185 185 TYR H H 1 7.809 0.010 . 1 . . . . 185 TYR H . 17471 1 614 . 1 1 185 185 TYR CA C 13 57.733 0.250 . 1 . . . . 185 TYR CA . 17471 1 615 . 1 1 185 185 TYR CB C 13 37.812 0.250 . 1 . . . . 185 TYR CB . 17471 1 616 . 1 1 185 185 TYR N N 15 121.106 0.070 . 1 . . . . 185 TYR N . 17471 1 617 . 1 1 186 186 VAL H H 1 7.726 0.010 . 1 . . . . 186 VAL H . 17471 1 618 . 1 1 186 186 VAL CA C 13 61.937 0.250 . 1 . . . . 186 VAL CA . 17471 1 619 . 1 1 186 186 VAL CB C 13 31.420 0.250 . 1 . . . . 186 VAL CB . 17471 1 620 . 1 1 186 186 VAL N N 15 123.303 0.070 . 1 . . . . 186 VAL N . 17471 1 621 . 1 1 191 191 TYR CA C 13 56.743 0.250 . 1 . . . . 191 TYR CA . 17471 1 622 . 1 1 191 191 TYR CB C 13 37.896 0.250 . 1 . . . . 191 TYR CB . 17471 1 623 . 1 1 192 192 ARG H H 1 7.292 0.010 . 1 . . . . 192 ARG H . 17471 1 624 . 1 1 192 192 ARG CA C 13 55.431 0.250 . 1 . . . . 192 ARG CA . 17471 1 625 . 1 1 192 192 ARG CB C 13 30.798 0.250 . 1 . . . . 192 ARG CB . 17471 1 626 . 1 1 192 192 ARG N N 15 122.671 0.070 . 1 . . . . 192 ARG N . 17471 1 627 . 1 1 193 193 ALA H H 1 8.794 0.010 . 1 . . . . 193 ALA H . 17471 1 628 . 1 1 193 193 ALA CA C 13 49.674 0.250 . 1 . . . . 193 ALA CA . 17471 1 629 . 1 1 193 193 ALA CB C 13 16.777 0.250 . 1 . . . . 193 ALA CB . 17471 1 630 . 1 1 193 193 ALA N N 15 126.460 0.070 . 1 . . . . 193 ALA N . 17471 1 631 . 1 1 197 197 MET CA C 13 59.286 0.250 . 1 . . . . 197 MET CA . 17471 1 632 . 1 1 197 197 MET CB C 13 33.733 0.250 . 1 . . . . 197 MET CB . 17471 1 633 . 1 1 198 198 LEU H H 1 9.162 0.010 . 1 . . . . 198 LEU H . 17471 1 634 . 1 1 198 198 LEU CA C 13 57.707 0.250 . 1 . . . . 198 LEU CA . 17471 1 635 . 1 1 198 198 LEU CB C 13 41.240 0.250 . 1 . . . . 198 LEU CB . 17471 1 636 . 1 1 198 198 LEU N N 15 126.842 0.070 . 1 . . . . 198 LEU N . 17471 1 637 . 1 1 199 199 ASN H H 1 7.819 0.010 . 1 . . . . 199 ASN H . 17471 1 638 . 1 1 199 199 ASN CA C 13 53.342 0.250 . 1 . . . . 199 ASN CA . 17471 1 639 . 1 1 199 199 ASN CB C 13 40.284 0.250 . 1 . . . . 199 ASN CB . 17471 1 640 . 1 1 199 199 ASN N N 15 115.457 0.070 . 1 . . . . 199 ASN N . 17471 1 641 . 1 1 200 200 TRP H H 1 8.500 0.010 . 1 . . . . 200 TRP H . 17471 1 642 . 1 1 200 200 TRP CA C 13 54.226 0.250 . 1 . . . . 200 TRP CA . 17471 1 643 . 1 1 200 200 TRP CB C 13 27.727 0.250 . 1 . . . . 200 TRP CB . 17471 1 644 . 1 1 200 200 TRP N N 15 125.361 0.070 . 1 . . . . 200 TRP N . 17471 1 645 . 1 1 201 201 MET H H 1 8.619 0.010 . 1 . . . . 201 MET H . 17471 1 646 . 1 1 201 201 MET CA C 13 61.803 0.250 . 1 . . . . 201 MET CA . 17471 1 647 . 1 1 201 201 MET CB C 13 36.990 0.250 . 1 . . . . 201 MET CB . 17471 1 648 . 1 1 201 201 MET N N 15 120.188 0.070 . 1 . . . . 201 MET N . 17471 1 649 . 1 1 202 202 HIS H H 1 7.172 0.010 . 1 . . . . 202 HIS H . 17471 1 650 . 1 1 202 202 HIS CA C 13 59.260 0.250 . 1 . . . . 202 HIS CA . 17471 1 651 . 1 1 202 202 HIS CB C 13 32.380 0.250 . 1 . . . . 202 HIS CB . 17471 1 652 . 1 1 202 202 HIS N N 15 115.369 0.070 . 1 . . . . 202 HIS N . 17471 1 653 . 1 1 203 203 TYR H H 1 10.038 0.010 . 1 . . . . 203 TYR H . 17471 1 654 . 1 1 203 203 TYR CA C 13 52.539 0.250 . 1 . . . . 203 TYR CA . 17471 1 655 . 1 1 203 203 TYR CB C 13 41.376 0.250 . 1 . . . . 203 TYR CB . 17471 1 656 . 1 1 203 203 TYR N N 15 127.109 0.070 . 1 . . . . 203 TYR N . 17471 1 657 . 1 1 204 204 ASN H H 1 8.718 0.010 . 1 . . . . 204 ASN H . 17471 1 658 . 1 1 204 204 ASN CA C 13 56.100 0.250 . 1 . . . . 204 ASN CA . 17471 1 659 . 1 1 204 204 ASN CB C 13 41.376 0.250 . 1 . . . . 204 ASN CB . 17471 1 660 . 1 1 204 204 ASN N N 15 125.076 0.070 . 1 . . . . 204 ASN N . 17471 1 661 . 1 1 205 205 GLN H H 1 7.150 0.010 . 1 . . . . 205 GLN H . 17471 1 662 . 1 1 205 205 GLN CA C 13 57.252 0.250 . 1 . . . . 205 GLN CA . 17471 1 663 . 1 1 205 205 GLN CB C 13 28.151 0.250 . 1 . . . . 205 GLN CB . 17471 1 664 . 1 1 205 205 GLN N N 15 118.612 0.070 . 1 . . . . 205 GLN N . 17471 1 665 . 1 1 206 206 THR H H 1 8.296 0.010 . 1 . . . . 206 THR H . 17471 1 666 . 1 1 206 206 THR CA C 13 58.965 0.250 . 1 . . . . 206 THR CA . 17471 1 667 . 1 1 206 206 THR CB C 13 64.328 0.250 . 1 . . . . 206 THR CB . 17471 1 668 . 1 1 206 206 THR N N 15 115.664 0.070 . 1 . . . . 206 THR N . 17471 1 669 . 1 1 208 208 ASP CA C 13 56.448 0.250 . 1 . . . . 208 ASP CA . 17471 1 670 . 1 1 209 209 ILE H H 1 7.227 0.010 . 1 . . . . 209 ILE H . 17471 1 671 . 1 1 209 209 ILE CA C 13 60.679 0.250 . 1 . . . . 209 ILE CA . 17471 1 672 . 1 1 209 209 ILE CB C 13 34.210 0.250 . 1 . . . . 209 ILE CB . 17471 1 673 . 1 1 209 209 ILE N N 15 119.502 0.070 . 1 . . . . 209 ILE N . 17471 1 674 . 1 1 210 210 TRP H H 1 7.476 0.010 . 1 . . . . 210 TRP H . 17471 1 675 . 1 1 210 210 TRP CA C 13 61.054 0.250 . 1 . . . . 210 TRP CA . 17471 1 676 . 1 1 210 210 TRP CB C 13 27.931 0.250 . 1 . . . . 210 TRP CB . 17471 1 677 . 1 1 210 210 TRP N N 15 121.120 0.070 . 1 . . . . 210 TRP N . 17471 1 678 . 1 1 211 211 SER H H 1 7.554 0.010 . 1 . . . . 211 SER H . 17471 1 679 . 1 1 211 211 SER CA C 13 61.995 0.250 . 1 . . . . 211 SER CA . 17471 1 680 . 1 1 211 211 SER CB C 13 62.752 0.250 . 1 . . . . 211 SER CB . 17471 1 681 . 1 1 211 211 SER N N 15 112.846 0.070 . 1 . . . . 211 SER N . 17471 1 682 . 1 1 212 212 VAL H H 1 7.952 0.010 . 1 . . . . 212 VAL H . 17471 1 683 . 1 1 212 212 VAL CA C 13 67.206 0.250 . 1 . . . . 212 VAL CA . 17471 1 684 . 1 1 212 212 VAL CB C 13 29.453 0.250 . 1 . . . . 212 VAL CB . 17471 1 685 . 1 1 212 212 VAL N N 15 120.112 0.070 . 1 . . . . 212 VAL N . 17471 1 686 . 1 1 213 213 GLY H H 1 8.473 0.010 . 1 . . . . 213 GLY H . 17471 1 687 . 1 1 213 213 GLY CA C 13 47.666 0.250 . 1 . . . . 213 GLY CA . 17471 1 688 . 1 1 213 213 GLY N N 15 110.547 0.070 . 1 . . . . 213 GLY N . 17471 1 689 . 1 1 214 214 CYS H H 1 7.846 0.010 . 1 . . . . 214 CYS H . 17471 1 690 . 1 1 214 214 CYS CA C 13 63.624 0.250 . 1 . . . . 214 CYS CA . 17471 1 691 . 1 1 214 214 CYS CB C 13 27.329 0.250 . 1 . . . . 214 CYS CB . 17471 1 692 . 1 1 214 214 CYS N N 15 119.526 0.070 . 1 . . . . 214 CYS N . 17471 1 693 . 1 1 215 215 ILE H H 1 8.390 0.010 . 1 . . . . 215 ILE H . 17471 1 694 . 1 1 215 215 ILE CA C 13 65.471 0.250 . 1 . . . . 215 ILE CA . 17471 1 695 . 1 1 215 215 ILE CB C 13 37.691 0.250 . 1 . . . . 215 ILE CB . 17471 1 696 . 1 1 215 215 ILE N N 15 124.407 0.070 . 1 . . . . 215 ILE N . 17471 1 697 . 1 1 216 216 MET H H 1 9.256 0.010 . 1 . . . . 216 MET H . 17471 1 698 . 1 1 216 216 MET CA C 13 60.036 0.250 . 1 . . . . 216 MET CA . 17471 1 699 . 1 1 216 216 MET CB C 13 30.934 0.250 . 1 . . . . 216 MET CB . 17471 1 700 . 1 1 216 216 MET N N 15 120.794 0.070 . 1 . . . . 216 MET N . 17471 1 701 . 1 1 217 217 ALA H H 1 8.104 0.010 . 1 . . . . 217 ALA H . 17471 1 702 . 1 1 217 217 ALA CA C 13 55.136 0.250 . 1 . . . . 217 ALA CA . 17471 1 703 . 1 1 217 217 ALA CB C 13 19.537 0.250 . 1 . . . . 217 ALA CB . 17471 1 704 . 1 1 217 217 ALA N N 15 118.722 0.070 . 1 . . . . 217 ALA N . 17471 1 705 . 1 1 218 218 GLU H H 1 7.090 0.010 . 1 . . . . 218 GLU H . 17471 1 706 . 1 1 218 218 GLU CA C 13 57.760 0.250 . 1 . . . . 218 GLU CA . 17471 1 707 . 1 1 218 218 GLU CB C 13 29.160 0.250 . 1 . . . . 218 GLU CB . 17471 1 708 . 1 1 218 218 GLU N N 15 120.110 0.070 . 1 . . . . 218 GLU N . 17471 1 709 . 1 1 219 219 LEU H H 1 7.245 0.010 . 1 . . . . 219 LEU H . 17471 1 710 . 1 1 219 219 LEU CA C 13 56.850 0.250 . 1 . . . . 219 LEU CA . 17471 1 711 . 1 1 219 219 LEU CB C 13 42.127 0.250 . 1 . . . . 219 LEU CB . 17471 1 712 . 1 1 219 219 LEU N N 15 116.669 0.070 . 1 . . . . 219 LEU N . 17471 1 713 . 1 1 220 220 LEU H H 1 8.456 0.010 . 1 . . . . 220 LEU H . 17471 1 714 . 1 1 220 220 LEU CA C 13 56.770 0.250 . 1 . . . . 220 LEU CA . 17471 1 715 . 1 1 220 220 LEU CB C 13 39.875 0.250 . 1 . . . . 220 LEU CB . 17471 1 716 . 1 1 220 220 LEU N N 15 118.670 0.070 . 1 . . . . 220 LEU N . 17471 1 717 . 1 1 221 221 THR H H 1 7.913 0.010 . 1 . . . . 221 THR H . 17471 1 718 . 1 1 221 221 THR CA C 13 61.803 0.250 . 1 . . . . 221 THR CA . 17471 1 719 . 1 1 221 221 THR CB C 13 71.201 0.250 . 1 . . . . 221 THR CB . 17471 1 720 . 1 1 221 221 THR N N 15 106.254 0.070 . 1 . . . . 221 THR N . 17471 1 721 . 1 1 222 222 GLY H H 1 8.377 0.010 . 1 . . . . 222 GLY H . 17471 1 722 . 1 1 222 222 GLY CA C 13 45.203 0.250 . 1 . . . . 222 GLY CA . 17471 1 723 . 1 1 222 222 GLY N N 15 112.899 0.070 . 1 . . . . 222 GLY N . 17471 1 724 . 1 1 223 223 ARG H H 1 7.962 0.010 . 1 . . . . 223 ARG H . 17471 1 725 . 1 1 223 223 ARG CA C 13 53.610 0.250 . 1 . . . . 223 ARG CA . 17471 1 726 . 1 1 223 223 ARG CB C 13 32.056 0.250 . 1 . . . . 223 ARG CB . 17471 1 727 . 1 1 223 223 ARG N N 15 119.277 0.070 . 1 . . . . 223 ARG N . 17471 1 728 . 1 1 224 224 THR H H 1 7.889 0.010 . 1 . . . . 224 THR H . 17471 1 729 . 1 1 224 224 THR CA C 13 63.142 0.250 . 1 . . . . 224 THR CA . 17471 1 730 . 1 1 224 224 THR CB C 13 68.471 0.250 . 1 . . . . 224 THR CB . 17471 1 731 . 1 1 224 224 THR N N 15 120.136 0.070 . 1 . . . . 224 THR N . 17471 1 732 . 1 1 225 225 LEU H H 1 7.808 0.010 . 1 . . . . 225 LEU H . 17471 1 733 . 1 1 225 225 LEU CA C 13 52.673 0.250 . 1 . . . . 225 LEU CA . 17471 1 734 . 1 1 225 225 LEU CB C 13 40.626 0.250 . 1 . . . . 225 LEU CB . 17471 1 735 . 1 1 225 225 LEU N N 15 118.038 0.070 . 1 . . . . 225 LEU N . 17471 1 736 . 1 1 227 227 PRO CA C 13 60.625 0.250 . 1 . . . . 227 PRO CA . 17471 1 737 . 1 1 227 227 PRO CB C 13 26.157 0.250 . 1 . . . . 227 PRO CB . 17471 1 738 . 1 1 228 228 GLY H H 1 8.300 0.010 . 1 . . . . 228 GLY H . 17471 1 739 . 1 1 228 228 GLY CA C 13 45.116 0.250 . 1 . . . . 228 GLY CA . 17471 1 740 . 1 1 228 228 GLY N N 15 113.787 0.070 . 1 . . . . 228 GLY N . 17471 1 741 . 1 1 229 229 THR H H 1 10.053 0.010 . 1 . . . . 229 THR H . 17471 1 742 . 1 1 229 229 THR CA C 13 63.276 0.250 . 1 . . . . 229 THR CA . 17471 1 743 . 1 1 229 229 THR CB C 13 68.644 0.250 . 1 . . . . 229 THR CB . 17471 1 744 . 1 1 229 229 THR N N 15 116.820 0.070 . 1 . . . . 229 THR N . 17471 1 745 . 1 1 230 230 ASP H H 1 8.590 0.010 . 1 . . . . 230 ASP H . 17471 1 746 . 1 1 230 230 ASP CA C 13 57.653 0.250 . 1 . . . . 230 ASP CA . 17471 1 747 . 1 1 230 230 ASP CB C 13 39.730 0.250 . 1 . . . . 230 ASP CB . 17471 1 748 . 1 1 230 230 ASP N N 15 130.939 0.070 . 1 . . . . 230 ASP N . 17471 1 749 . 1 1 231 231 HIS H H 1 8.516 0.010 . 1 . . . . 231 HIS H . 17471 1 750 . 1 1 231 231 HIS CA C 13 51.789 0.250 . 1 . . . . 231 HIS CA . 17471 1 751 . 1 1 231 231 HIS CB C 13 39.807 0.250 . 1 . . . . 231 HIS CB . 17471 1 752 . 1 1 231 231 HIS N N 15 114.572 0.070 . 1 . . . . 231 HIS N . 17471 1 753 . 1 1 239 239 LEU CA C 13 57.252 0.250 . 1 . . . . 239 LEU CA . 17471 1 754 . 1 1 239 239 LEU CB C 13 41.308 0.250 . 1 . . . . 239 LEU CB . 17471 1 755 . 1 1 240 240 ARG H H 1 8.174 0.010 . 1 . . . . 240 ARG H . 17471 1 756 . 1 1 240 240 ARG CA C 13 58.938 0.250 . 1 . . . . 240 ARG CA . 17471 1 757 . 1 1 240 240 ARG CB C 13 31.958 0.250 . 1 . . . . 240 ARG CB . 17471 1 758 . 1 1 240 240 ARG N N 15 117.568 0.070 . 1 . . . . 240 ARG N . 17471 1 759 . 1 1 241 241 LEU H H 1 7.556 0.010 . 1 . . . . 241 LEU H . 17471 1 760 . 1 1 241 241 LEU CA C 13 57.225 0.250 . 1 . . . . 241 LEU CA . 17471 1 761 . 1 1 241 241 LEU CB C 13 40.278 0.250 . 1 . . . . 241 LEU CB . 17471 1 762 . 1 1 241 241 LEU N N 15 117.984 0.070 . 1 . . . . 241 LEU N . 17471 1 763 . 1 1 242 242 VAL H H 1 8.532 0.010 . 1 . . . . 242 VAL H . 17471 1 764 . 1 1 242 242 VAL CA C 13 59.956 0.250 . 1 . . . . 242 VAL CA . 17471 1 765 . 1 1 242 242 VAL CB C 13 40.284 0.250 . 1 . . . . 242 VAL CB . 17471 1 766 . 1 1 242 242 VAL N N 15 122.708 0.070 . 1 . . . . 242 VAL N . 17471 1 767 . 1 1 243 243 GLY CA C 13 44.775 0.250 . 1 . . . . 243 GLY CA . 17471 1 768 . 1 1 244 244 THR H H 1 7.756 0.010 . 1 . . . . 244 THR H . 17471 1 769 . 1 1 244 244 THR CA C 13 59.554 0.250 . 1 . . . . 244 THR CA . 17471 1 770 . 1 1 244 244 THR CB C 13 64.122 0.250 . 1 . . . . 244 THR CB . 17471 1 771 . 1 1 244 244 THR N N 15 121.804 0.070 . 1 . . . . 244 THR N . 17471 1 772 . 1 1 245 245 PRO CA C 13 62.339 0.250 . 1 . . . . 245 PRO CA . 17471 1 773 . 1 1 245 245 PRO CB C 13 32.026 0.250 . 1 . . . . 245 PRO CB . 17471 1 774 . 1 1 246 246 GLY H H 1 8.218 0.010 . 1 . . . . 246 GLY H . 17471 1 775 . 1 1 246 246 GLY CA C 13 43.347 0.250 . 1 . . . . 246 GLY CA . 17471 1 776 . 1 1 246 246 GLY N N 15 108.873 0.070 . 1 . . . . 246 GLY N . 17471 1 777 . 1 1 247 247 ALA H H 1 8.313 0.010 . 1 . . . . 247 ALA H . 17471 1 778 . 1 1 247 247 ALA CA C 13 55.029 0.250 . 1 . . . . 247 ALA CA . 17471 1 779 . 1 1 247 247 ALA CB C 13 18.010 0.250 . 1 . . . . 247 ALA CB . 17471 1 780 . 1 1 247 247 ALA N N 15 121.547 0.070 . 1 . . . . 247 ALA N . 17471 1 781 . 1 1 248 248 GLU H H 1 8.521 0.010 . 1 . . . . 248 GLU H . 17471 1 782 . 1 1 248 248 GLU CA C 13 58.778 0.250 . 1 . . . . 248 GLU CA . 17471 1 783 . 1 1 248 248 GLU CB C 13 27.931 0.250 . 1 . . . . 248 GLU CB . 17471 1 784 . 1 1 248 248 GLU N N 15 116.456 0.070 . 1 . . . . 248 GLU N . 17471 1 785 . 1 1 249 249 LEU H H 1 7.410 0.010 . 1 . . . . 249 LEU H . 17471 1 786 . 1 1 249 249 LEU CA C 13 56.395 0.250 . 1 . . . . 249 LEU CA . 17471 1 787 . 1 1 249 249 LEU CB C 13 40.353 0.250 . 1 . . . . 249 LEU CB . 17471 1 788 . 1 1 249 249 LEU N N 15 120.565 0.070 . 1 . . . . 249 LEU N . 17471 1 789 . 1 1 250 250 LEU H H 1 7.826 0.010 . 1 . . . . 250 LEU H . 17471 1 790 . 1 1 250 250 LEU CA C 13 57.588 0.250 . 1 . . . . 250 LEU CA . 17471 1 791 . 1 1 250 250 LEU CB C 13 41.308 0.250 . 1 . . . . 250 LEU CB . 17471 1 792 . 1 1 250 250 LEU N N 15 118.242 0.070 . 1 . . . . 250 LEU N . 17471 1 793 . 1 1 251 251 LYS H H 1 7.572 0.010 . 1 . . . . 251 LYS H . 17471 1 794 . 1 1 251 251 LYS CA C 13 55.601 0.250 . 1 . . . . 251 LYS CA . 17471 1 795 . 1 1 251 251 LYS CB C 13 36.326 0.250 . 1 . . . . 251 LYS CB . 17471 1 796 . 1 1 251 251 LYS N N 15 120.278 0.070 . 1 . . . . 251 LYS N . 17471 1 797 . 1 1 252 252 LYS H H 1 7.408 0.010 . 1 . . . . 252 LYS H . 17471 1 798 . 1 1 252 252 LYS CA C 13 55.538 0.250 . 1 . . . . 252 LYS CA . 17471 1 799 . 1 1 252 252 LYS CB C 13 38.840 0.250 . 1 . . . . 252 LYS CB . 17471 1 800 . 1 1 252 252 LYS N N 15 120.693 0.070 . 1 . . . . 252 LYS N . 17471 1 801 . 1 1 256 256 GLU CA C 13 59.286 0.250 . 1 . . . . 256 GLU CA . 17471 1 802 . 1 1 257 257 SER H H 1 8.312 0.010 . 1 . . . . 257 SER H . 17471 1 803 . 1 1 257 257 SER CA C 13 60.526 0.250 . 1 . . . . 257 SER CA . 17471 1 804 . 1 1 257 257 SER CB C 13 61.450 0.250 . 1 . . . . 257 SER CB . 17471 1 805 . 1 1 257 257 SER N N 15 114.084 0.070 . 1 . . . . 257 SER N . 17471 1 806 . 1 1 258 258 ALA H H 1 7.642 0.010 . 1 . . . . 258 ALA H . 17471 1 807 . 1 1 258 258 ALA CA C 13 54.387 0.250 . 1 . . . . 258 ALA CA . 17471 1 808 . 1 1 258 258 ALA CB C 13 17.914 0.250 . 1 . . . . 258 ALA CB . 17471 1 809 . 1 1 258 258 ALA N N 15 126.001 0.070 . 1 . . . . 258 ALA N . 17471 1 810 . 1 1 259 259 ARG H H 1 8.792 0.010 . 1 . . . . 259 ARG H . 17471 1 811 . 1 1 259 259 ARG CA C 13 55.163 0.250 . 1 . . . . 259 ARG CA . 17471 1 812 . 1 1 259 259 ARG CB C 13 29.658 0.250 . 1 . . . . 259 ARG CB . 17471 1 813 . 1 1 259 259 ARG N N 15 126.420 0.070 . 1 . . . . 259 ARG N . 17471 1 814 . 1 1 262 262 ILE CA C 13 63.329 0.250 . 1 . . . . 262 ILE CA . 17471 1 815 . 1 1 263 263 GLN H H 1 7.966 0.010 . 1 . . . . 263 GLN H . 17471 1 816 . 1 1 263 263 GLN CA C 13 57.733 0.250 . 1 . . . . 263 GLN CA . 17471 1 817 . 1 1 263 263 GLN CB C 13 28.204 0.250 . 1 . . . . 263 GLN CB . 17471 1 818 . 1 1 263 263 GLN N N 15 118.349 0.070 . 1 . . . . 263 GLN N . 17471 1 819 . 1 1 264 264 SER H H 1 7.371 0.010 . 1 . . . . 264 SER H . 17471 1 820 . 1 1 264 264 SER CA C 13 58.848 0.250 . 1 . . . . 264 SER CA . 17471 1 821 . 1 1 264 264 SER CB C 13 63.421 0.250 . 1 . . . . 264 SER CB . 17471 1 822 . 1 1 264 264 SER N N 15 113.958 0.070 . 1 . . . . 264 SER N . 17471 1 823 . 1 1 265 265 LEU H H 1 6.815 0.010 . 1 . . . . 265 LEU H . 17471 1 824 . 1 1 265 265 LEU CA C 13 54.039 0.250 . 1 . . . . 265 LEU CA . 17471 1 825 . 1 1 265 265 LEU CB C 13 41.376 0.250 . 1 . . . . 265 LEU CB . 17471 1 826 . 1 1 265 265 LEU N N 15 123.112 0.070 . 1 . . . . 265 LEU N . 17471 1 827 . 1 1 266 266 THR H H 1 9.158 0.010 . 1 . . . . 266 THR H . 17471 1 828 . 1 1 266 266 THR CA C 13 63.356 0.250 . 1 . . . . 266 THR CA . 17471 1 829 . 1 1 266 266 THR CB C 13 71.522 0.250 . 1 . . . . 266 THR CB . 17471 1 830 . 1 1 266 266 THR N N 15 122.017 0.070 . 1 . . . . 266 THR N . 17471 1 831 . 1 1 267 267 GLN H H 1 8.436 0.010 . 1 . . . . 267 GLN H . 17471 1 832 . 1 1 267 267 GLN CA C 13 56.261 0.250 . 1 . . . . 267 GLN CA . 17471 1 833 . 1 1 267 267 GLN CB C 13 27.658 0.250 . 1 . . . . 267 GLN CB . 17471 1 834 . 1 1 267 267 GLN N N 15 127.025 0.070 . 1 . . . . 267 GLN N . 17471 1 835 . 1 1 268 268 MET H H 1 8.673 0.010 . 1 . . . . 268 MET H . 17471 1 836 . 1 1 268 268 MET CA C 13 51.709 0.250 . 1 . . . . 268 MET CA . 17471 1 837 . 1 1 268 268 MET N N 15 124.057 0.070 . 1 . . . . 268 MET N . 17471 1 838 . 1 1 269 269 PRO CA C 13 61.187 0.250 . 1 . . . . 269 PRO CA . 17471 1 839 . 1 1 269 269 PRO CB C 13 31.207 0.250 . 1 . . . . 269 PRO CB . 17471 1 840 . 1 1 270 270 LYS H H 1 8.209 0.010 . 1 . . . . 270 LYS H . 17471 1 841 . 1 1 270 270 LYS CA C 13 56.395 0.250 . 1 . . . . 270 LYS CA . 17471 1 842 . 1 1 270 270 LYS CB C 13 32.026 0.250 . 1 . . . . 270 LYS CB . 17471 1 843 . 1 1 270 270 LYS N N 15 120.637 0.070 . 1 . . . . 270 LYS N . 17471 1 844 . 1 1 271 271 MET H H 1 8.342 0.010 . 1 . . . . 271 MET H . 17471 1 845 . 1 1 271 271 MET CA C 13 55.538 0.250 . 1 . . . . 271 MET CA . 17471 1 846 . 1 1 271 271 MET CB C 13 32.504 0.250 . 1 . . . . 271 MET CB . 17471 1 847 . 1 1 271 271 MET N N 15 126.456 0.070 . 1 . . . . 271 MET N . 17471 1 848 . 1 1 272 272 ASN H H 1 8.518 0.010 . 1 . . . . 272 ASN H . 17471 1 849 . 1 1 272 272 ASN CA C 13 52.432 0.250 . 1 . . . . 272 ASN CA . 17471 1 850 . 1 1 272 272 ASN CB C 13 37.418 0.250 . 1 . . . . 272 ASN CB . 17471 1 851 . 1 1 272 272 ASN N N 15 120.679 0.070 . 1 . . . . 272 ASN N . 17471 1 852 . 1 1 273 273 PHE H H 1 9.355 0.010 . 1 . . . . 273 PHE H . 17471 1 853 . 1 1 273 273 PHE CA C 13 59.420 0.250 . 1 . . . . 273 PHE CA . 17471 1 854 . 1 1 273 273 PHE CB C 13 36.667 0.250 . 1 . . . . 273 PHE CB . 17471 1 855 . 1 1 273 273 PHE N N 15 130.170 0.070 . 1 . . . . 273 PHE N . 17471 1 856 . 1 1 274 274 ALA H H 1 8.505 0.010 . 1 . . . . 274 ALA H . 17471 1 857 . 1 1 274 274 ALA CA C 13 54.280 0.250 . 1 . . . . 274 ALA CA . 17471 1 858 . 1 1 274 274 ALA CB C 13 17.012 0.250 . 1 . . . . 274 ALA CB . 17471 1 859 . 1 1 274 274 ALA N N 15 122.572 0.070 . 1 . . . . 274 ALA N . 17471 1 860 . 1 1 275 275 ASN H H 1 7.417 0.010 . 1 . . . . 275 ASN H . 17471 1 861 . 1 1 275 275 ASN CA C 13 53.316 0.250 . 1 . . . . 275 ASN CA . 17471 1 862 . 1 1 275 275 ASN CB C 13 38.017 0.250 . 1 . . . . 275 ASN CB . 17471 1 863 . 1 1 275 275 ASN N N 15 113.227 0.070 . 1 . . . . 275 ASN N . 17471 1 864 . 1 1 276 276 VAL H H 1 7.157 0.010 . 1 . . . . 276 VAL H . 17471 1 865 . 1 1 276 276 VAL CA C 13 63.892 0.250 . 1 . . . . 276 VAL CA . 17471 1 866 . 1 1 276 276 VAL CB C 13 32.163 0.250 . 1 . . . . 276 VAL CB . 17471 1 867 . 1 1 276 276 VAL N N 15 120.181 0.070 . 1 . . . . 276 VAL N . 17471 1 868 . 1 1 277 277 PHE H H 1 7.570 0.010 . 1 . . . . 277 PHE H . 17471 1 869 . 1 1 277 277 PHE CA C 13 55.672 0.250 . 1 . . . . 277 PHE CA . 17471 1 870 . 1 1 277 277 PHE CB C 13 36.190 0.250 . 1 . . . . 277 PHE CB . 17471 1 871 . 1 1 277 277 PHE N N 15 120.992 0.070 . 1 . . . . 277 PHE N . 17471 1 872 . 1 1 278 278 ILE H H 1 6.842 0.010 . 1 . . . . 278 ILE H . 17471 1 873 . 1 1 278 278 ILE CA C 13 61.964 0.250 . 1 . . . . 278 ILE CA . 17471 1 874 . 1 1 278 278 ILE CB C 13 36.463 0.250 . 1 . . . . 278 ILE CB . 17471 1 875 . 1 1 278 278 ILE N N 15 121.106 0.070 . 1 . . . . 278 ILE N . 17471 1 876 . 1 1 279 279 GLY H H 1 8.944 0.010 . 1 . . . . 279 GLY H . 17471 1 877 . 1 1 279 279 GLY CA C 13 44.614 0.250 . 1 . . . . 279 GLY CA . 17471 1 878 . 1 1 279 279 GLY N N 15 116.481 0.070 . 1 . . . . 279 GLY N . 17471 1 879 . 1 1 280 280 ALA H H 1 7.348 0.010 . 1 . . . . 280 ALA H . 17471 1 880 . 1 1 280 280 ALA CA C 13 50.780 0.250 . 1 . . . . 280 ALA CA . 17471 1 881 . 1 1 280 280 ALA CB C 13 18.970 0.250 . 1 . . . . 280 ALA CB . 17471 1 882 . 1 1 280 280 ALA N N 15 122.202 0.070 . 1 . . . . 280 ALA N . 17471 1 883 . 1 1 281 281 ASN H H 1 9.033 0.010 . 1 . . . . 281 ASN H . 17471 1 884 . 1 1 281 281 ASN CA C 13 50.959 0.250 . 1 . . . . 281 ASN CA . 17471 1 885 . 1 1 281 281 ASN CB C 13 38.578 0.250 . 1 . . . . 281 ASN CB . 17471 1 886 . 1 1 281 281 ASN N N 15 122.728 0.070 . 1 . . . . 281 ASN N . 17471 1 887 . 1 1 282 282 PRO CA C 13 64.775 0.250 . 1 . . . . 282 PRO CA . 17471 1 888 . 1 1 283 283 LEU H H 1 8.378 0.010 . 1 . . . . 283 LEU H . 17471 1 889 . 1 1 283 283 LEU CA C 13 56.770 0.250 . 1 . . . . 283 LEU CA . 17471 1 890 . 1 1 283 283 LEU CB C 13 41.718 0.250 . 1 . . . . 283 LEU CB . 17471 1 891 . 1 1 283 283 LEU N N 15 117.304 0.070 . 1 . . . . 283 LEU N . 17471 1 892 . 1 1 284 284 ALA H H 1 7.067 0.010 . 1 . . . . 284 ALA H . 17471 1 893 . 1 1 284 284 ALA CA C 13 53.591 0.250 . 1 . . . . 284 ALA CA . 17471 1 894 . 1 1 284 284 ALA CB C 13 17.148 0.250 . 1 . . . . 284 ALA CB . 17471 1 895 . 1 1 284 284 ALA N N 15 121.254 0.070 . 1 . . . . 284 ALA N . 17471 1 896 . 1 1 285 285 VAL H H 1 7.040 0.010 . 1 . . . . 285 VAL H . 17471 1 897 . 1 1 285 285 VAL CA C 13 66.383 0.250 . 1 . . . . 285 VAL CA . 17471 1 898 . 1 1 285 285 VAL CB C 13 30.388 0.250 . 1 . . . . 285 VAL CB . 17471 1 899 . 1 1 285 285 VAL N N 15 116.679 0.070 . 1 . . . . 285 VAL N . 17471 1 900 . 1 1 286 286 ASP H H 1 7.441 0.010 . 1 . . . . 286 ASP H . 17471 1 901 . 1 1 286 286 ASP CA C 13 57.530 0.250 . 1 . . . . 286 ASP CA . 17471 1 902 . 1 1 286 286 ASP CB C 13 42.676 0.250 . 1 . . . . 286 ASP CB . 17471 1 903 . 1 1 286 286 ASP N N 15 118.168 0.070 . 1 . . . . 286 ASP N . 17471 1 904 . 1 1 287 287 LEU H H 1 7.060 0.010 . 1 . . . . 287 LEU H . 17471 1 905 . 1 1 287 287 LEU CA C 13 57.385 0.250 . 1 . . . . 287 LEU CA . 17471 1 906 . 1 1 287 287 LEU CB C 13 38.988 0.250 . 1 . . . . 287 LEU CB . 17471 1 907 . 1 1 287 287 LEU N N 15 117.793 0.070 . 1 . . . . 287 LEU N . 17471 1 908 . 1 1 288 288 LEU H H 1 8.083 0.010 . 1 . . . . 288 LEU H . 17471 1 909 . 1 1 288 288 LEU CA C 13 58.483 0.250 . 1 . . . . 288 LEU CA . 17471 1 910 . 1 1 288 288 LEU CB C 13 40.537 0.250 . 1 . . . . 288 LEU CB . 17471 1 911 . 1 1 288 288 LEU N N 15 120.497 0.070 . 1 . . . . 288 LEU N . 17471 1 912 . 1 1 289 289 GLU H H 1 7.929 0.010 . 1 . . . . 289 GLU H . 17471 1 913 . 1 1 289 289 GLU CA C 13 58.349 0.250 . 1 . . . . 289 GLU CA . 17471 1 914 . 1 1 289 289 GLU CB C 13 28.356 0.250 . 1 . . . . 289 GLU CB . 17471 1 915 . 1 1 289 289 GLU N N 15 117.728 0.070 . 1 . . . . 289 GLU N . 17471 1 916 . 1 1 290 290 LYS H H 1 7.290 0.010 . 1 . . . . 290 LYS H . 17471 1 917 . 1 1 290 290 LYS CA C 13 56.930 0.250 . 1 . . . . 290 LYS CA . 17471 1 918 . 1 1 290 290 LYS CB C 13 31.958 0.250 . 1 . . . . 290 LYS CB . 17471 1 919 . 1 1 290 290 LYS N N 15 116.504 0.070 . 1 . . . . 290 LYS N . 17471 1 920 . 1 1 291 291 MET H H 1 7.520 0.010 . 1 . . . . 291 MET H . 17471 1 921 . 1 1 291 291 MET CA C 13 58.269 0.250 . 1 . . . . 291 MET CA . 17471 1 922 . 1 1 291 291 MET CB C 13 34.112 0.250 . 1 . . . . 291 MET CB . 17471 1 923 . 1 1 291 291 MET N N 15 118.499 0.070 . 1 . . . . 291 MET N . 17471 1 924 . 1 1 292 292 LEU H H 1 7.795 0.010 . 1 . . . . 292 LEU H . 17471 1 925 . 1 1 292 292 LEU CA C 13 59.208 0.250 . 1 . . . . 292 LEU CA . 17471 1 926 . 1 1 292 292 LEU CB C 13 38.154 0.250 . 1 . . . . 292 LEU CB . 17471 1 927 . 1 1 292 292 LEU N N 15 119.026 0.070 . 1 . . . . 292 LEU N . 17471 1 928 . 1 1 296 296 SER CA C 13 60.946 0.250 . 1 . . . . 296 SER CA . 17471 1 929 . 1 1 296 296 SER CB C 13 62.192 0.250 . 1 . . . . 296 SER CB . 17471 1 930 . 1 1 297 297 ASP H H 1 8.414 0.010 . 1 . . . . 297 ASP H . 17471 1 931 . 1 1 297 297 ASP CA C 13 56.073 0.250 . 1 . . . . 297 ASP CA . 17471 1 932 . 1 1 297 297 ASP CB C 13 40.216 0.250 . 1 . . . . 297 ASP CB . 17471 1 933 . 1 1 297 297 ASP N N 15 121.163 0.070 . 1 . . . . 297 ASP N . 17471 1 934 . 1 1 298 298 LYS H H 1 7.584 0.010 . 1 . . . . 298 LYS H . 17471 1 935 . 1 1 298 298 LYS CA C 13 54.521 0.250 . 1 . . . . 298 LYS CA . 17471 1 936 . 1 1 298 298 LYS CB C 13 32.845 0.250 . 1 . . . . 298 LYS CB . 17471 1 937 . 1 1 298 298 LYS N N 15 117.606 0.070 . 1 . . . . 298 LYS N . 17471 1 938 . 1 1 299 299 ARG H H 1 7.013 0.010 . 1 . . . . 299 ARG H . 17471 1 939 . 1 1 299 299 ARG CA C 13 56.955 0.250 . 1 . . . . 299 ARG CA . 17471 1 940 . 1 1 299 299 ARG CB C 13 29.638 0.250 . 1 . . . . 299 ARG CB . 17471 1 941 . 1 1 299 299 ARG N N 15 122.742 0.070 . 1 . . . . 299 ARG N . 17471 1 942 . 1 1 300 300 ILE H H 1 7.047 0.010 . 1 . . . . 300 ILE H . 17471 1 943 . 1 1 300 300 ILE CA C 13 61.937 0.250 . 1 . . . . 300 ILE CA . 17471 1 944 . 1 1 300 300 ILE CB C 13 38.988 0.250 . 1 . . . . 300 ILE CB . 17471 1 945 . 1 1 300 300 ILE N N 15 125.275 0.070 . 1 . . . . 300 ILE N . 17471 1 946 . 1 1 301 301 THR H H 1 7.321 0.010 . 1 . . . . 301 THR H . 17471 1 947 . 1 1 301 301 THR CA C 13 59.929 0.250 . 1 . . . . 301 THR CA . 17471 1 948 . 1 1 301 301 THR CB C 13 70.723 0.250 . 1 . . . . 301 THR CB . 17471 1 949 . 1 1 301 301 THR N N 15 109.543 0.070 . 1 . . . . 301 THR N . 17471 1 950 . 1 1 302 302 ALA H H 1 9.459 0.010 . 1 . . . . 302 ALA H . 17471 1 951 . 1 1 302 302 ALA CA C 13 55.940 0.250 . 1 . . . . 302 ALA CA . 17471 1 952 . 1 1 302 302 ALA CB C 13 15.920 0.250 . 1 . . . . 302 ALA CB . 17471 1 953 . 1 1 302 302 ALA N N 15 122.372 0.070 . 1 . . . . 302 ALA N . 17471 1 954 . 1 1 303 303 ALA H H 1 8.582 0.010 . 1 . . . . 303 ALA H . 17471 1 955 . 1 1 303 303 ALA CA C 13 54.869 0.250 . 1 . . . . 303 ALA CA . 17471 1 956 . 1 1 303 303 ALA CB C 13 17.558 0.250 . 1 . . . . 303 ALA CB . 17471 1 957 . 1 1 303 303 ALA N N 15 116.407 0.070 . 1 . . . . 303 ALA N . 17471 1 958 . 1 1 304 304 GLN H H 1 7.371 0.010 . 1 . . . . 304 GLN H . 17471 1 959 . 1 1 304 304 GLN CA C 13 57.747 0.250 . 1 . . . . 304 GLN CA . 17471 1 960 . 1 1 304 304 GLN CB C 13 27.863 0.250 . 1 . . . . 304 GLN CB . 17471 1 961 . 1 1 304 304 GLN N N 15 116.005 0.070 . 1 . . . . 304 GLN N . 17471 1 962 . 1 1 305 305 ALA H H 1 8.647 0.010 . 1 . . . . 305 ALA H . 17471 1 963 . 1 1 305 305 ALA CA C 13 54.708 0.250 . 1 . . . . 305 ALA CA . 17471 1 964 . 1 1 305 305 ALA CB C 13 18.513 0.250 . 1 . . . . 305 ALA CB . 17471 1 965 . 1 1 305 305 ALA N N 15 124.028 0.070 . 1 . . . . 305 ALA N . 17471 1 966 . 1 1 306 306 LEU H H 1 7.606 0.010 . 1 . . . . 306 LEU H . 17471 1 967 . 1 1 306 306 LEU CA C 13 57.359 0.250 . 1 . . . . 306 LEU CA . 17471 1 968 . 1 1 306 306 LEU CB C 13 41.035 0.250 . 1 . . . . 306 LEU CB . 17471 1 969 . 1 1 306 306 LEU N N 15 116.445 0.070 . 1 . . . . 306 LEU N . 17471 1 970 . 1 1 307 307 ALA H H 1 6.617 0.010 . 1 . . . . 307 ALA H . 17471 1 971 . 1 1 307 307 ALA CA C 13 50.611 0.250 . 1 . . . . 307 ALA CA . 17471 1 972 . 1 1 307 307 ALA CB C 13 18.079 0.250 . 1 . . . . 307 ALA CB . 17471 1 973 . 1 1 307 307 ALA N N 15 115.594 0.070 . 1 . . . . 307 ALA N . 17471 1 974 . 1 1 308 308 HIS H H 1 7.919 0.010 . 1 . . . . 308 HIS H . 17471 1 975 . 1 1 308 308 HIS CA C 13 58.483 0.250 . 1 . . . . 308 HIS CA . 17471 1 976 . 1 1 308 308 HIS CB C 13 32.163 0.250 . 1 . . . . 308 HIS CB . 17471 1 977 . 1 1 308 308 HIS N N 15 122.927 0.070 . 1 . . . . 308 HIS N . 17471 1 978 . 1 1 309 309 ALA H H 1 8.292 0.010 . 1 . . . . 309 ALA H . 17471 1 979 . 1 1 309 309 ALA CA C 13 54.865 0.250 . 1 . . . . 309 ALA CA . 17471 1 980 . 1 1 309 309 ALA CB C 13 18.151 0.250 . 1 . . . . 309 ALA CB . 17471 1 981 . 1 1 309 309 ALA N N 15 132.975 0.070 . 1 . . . . 309 ALA N . 17471 1 982 . 1 1 310 310 TYR H H 1 11.592 0.010 . 1 . . . . 310 TYR H . 17471 1 983 . 1 1 310 310 TYR CA C 13 59.962 0.250 . 1 . . . . 310 TYR CA . 17471 1 984 . 1 1 310 310 TYR CB C 13 38.075 0.250 . 1 . . . . 310 TYR CB . 17471 1 985 . 1 1 310 310 TYR N N 15 125.286 0.070 . 1 . . . . 310 TYR N . 17471 1 986 . 1 1 311 311 PHE H H 1 7.617 0.010 . 1 . . . . 311 PHE H . 17471 1 987 . 1 1 311 311 PHE CA C 13 55.832 0.250 . 1 . . . . 311 PHE CA . 17471 1 988 . 1 1 311 311 PHE CB C 13 38.100 0.250 . 1 . . . . 311 PHE CB . 17471 1 989 . 1 1 311 311 PHE N N 15 110.659 0.070 . 1 . . . . 311 PHE N . 17471 1 990 . 1 1 312 312 ALA H H 1 7.487 0.010 . 1 . . . . 312 ALA H . 17471 1 991 . 1 1 312 312 ALA CA C 13 55.565 0.250 . 1 . . . . 312 ALA CA . 17471 1 992 . 1 1 312 312 ALA CB C 13 18.104 0.250 . 1 . . . . 312 ALA CB . 17471 1 993 . 1 1 312 312 ALA N N 15 123.854 0.070 . 1 . . . . 312 ALA N . 17471 1 994 . 1 1 313 313 GLN H H 1 8.606 0.010 . 1 . . . . 313 GLN H . 17471 1 995 . 1 1 313 313 GLN CA C 13 56.957 0.250 . 1 . . . . 313 GLN CA . 17471 1 996 . 1 1 313 313 GLN CB C 13 27.522 0.250 . 1 . . . . 313 GLN CB . 17471 1 997 . 1 1 313 313 GLN N N 15 114.214 0.070 . 1 . . . . 313 GLN N . 17471 1 998 . 1 1 314 314 TYR H H 1 7.395 0.010 . 1 . . . . 314 TYR H . 17471 1 999 . 1 1 314 314 TYR CA C 13 58.172 0.250 . 1 . . . . 314 TYR CA . 17471 1 1000 . 1 1 314 314 TYR CB C 13 39.134 0.250 . 1 . . . . 314 TYR CB . 17471 1 1001 . 1 1 314 314 TYR N N 15 116.170 0.070 . 1 . . . . 314 TYR N . 17471 1 1002 . 1 1 315 315 HIS H H 1 7.780 0.010 . 1 . . . . 315 HIS H . 17471 1 1003 . 1 1 315 315 HIS CA C 13 55.719 0.250 . 1 . . . . 315 HIS CA . 17471 1 1004 . 1 1 315 315 HIS CB C 13 28.819 0.250 . 1 . . . . 315 HIS CB . 17471 1 1005 . 1 1 315 315 HIS N N 15 115.759 0.070 . 1 . . . . 315 HIS N . 17471 1 1006 . 1 1 316 316 ASP H H 1 7.367 0.010 . 1 . . . . 316 ASP H . 17471 1 1007 . 1 1 316 316 ASP CA C 13 50.611 0.250 . 1 . . . . 316 ASP CA . 17471 1 1008 . 1 1 316 316 ASP CB C 13 41.103 0.250 . 1 . . . . 316 ASP CB . 17471 1 1009 . 1 1 316 316 ASP N N 15 125.289 0.070 . 1 . . . . 316 ASP N . 17471 1 1010 . 1 1 317 317 PRO CA C 13 63.702 0.250 . 1 . . . . 317 PRO CA . 17471 1 1011 . 1 1 317 317 PRO CB C 13 31.029 0.250 . 1 . . . . 317 PRO CB . 17471 1 1012 . 1 1 318 318 ASP H H 1 7.924 0.010 . 1 . . . . 318 ASP H . 17471 1 1013 . 1 1 318 318 ASP CA C 13 54.963 0.250 . 1 . . . . 318 ASP CA . 17471 1 1014 . 1 1 318 318 ASP CB C 13 40.013 0.250 . 1 . . . . 318 ASP CB . 17471 1 1015 . 1 1 318 318 ASP N N 15 117.625 0.070 . 1 . . . . 318 ASP N . 17471 1 1016 . 1 1 319 319 ASP H H 1 7.940 0.010 . 1 . . . . 319 ASP H . 17471 1 1017 . 1 1 319 319 ASP CA C 13 52.379 0.250 . 1 . . . . 319 ASP CA . 17471 1 1018 . 1 1 319 319 ASP CB C 13 41.581 0.250 . 1 . . . . 319 ASP CB . 17471 1 1019 . 1 1 319 319 ASP N N 15 121.362 0.070 . 1 . . . . 319 ASP N . 17471 1 1020 . 1 1 320 320 GLU H H 1 7.743 0.010 . 1 . . . . 320 GLU H . 17471 1 1021 . 1 1 320 320 GLU CA C 13 53.262 0.250 . 1 . . . . 320 GLU CA . 17471 1 1022 . 1 1 320 320 GLU CB C 13 28.905 0.250 . 1 . . . . 320 GLU CB . 17471 1 1023 . 1 1 320 320 GLU N N 15 121.547 0.070 . 1 . . . . 320 GLU N . 17471 1 1024 . 1 1 321 321 PRO CA C 13 63.169 0.250 . 1 . . . . 321 PRO CA . 17471 1 1025 . 1 1 321 321 PRO CB C 13 32.777 0.250 . 1 . . . . 321 PRO CB . 17471 1 1026 . 1 1 322 322 VAL H H 1 7.793 0.010 . 1 . . . . 322 VAL H . 17471 1 1027 . 1 1 322 322 VAL CA C 13 59.206 0.250 . 1 . . . . 322 VAL CA . 17471 1 1028 . 1 1 322 322 VAL CB C 13 33.118 0.250 . 1 . . . . 322 VAL CB . 17471 1 1029 . 1 1 322 322 VAL N N 15 109.357 0.070 . 1 . . . . 322 VAL N . 17471 1 1030 . 1 1 323 323 ALA H H 1 8.393 0.010 . 1 . . . . 323 ALA H . 17471 1 1031 . 1 1 323 323 ALA CA C 13 50.585 0.250 . 1 . . . . 323 ALA CA . 17471 1 1032 . 1 1 323 323 ALA CB C 13 19.381 0.250 . 1 . . . . 323 ALA CB . 17471 1 1033 . 1 1 323 323 ALA N N 15 123.753 0.070 . 1 . . . . 323 ALA N . 17471 1 1034 . 1 1 324 324 ASP H H 1 8.027 0.010 . 1 . . . . 324 ASP H . 17471 1 1035 . 1 1 324 324 ASP CA C 13 52.780 0.250 . 1 . . . . 324 ASP CA . 17471 1 1036 . 1 1 324 324 ASP CB C 13 38.988 0.250 . 1 . . . . 324 ASP CB . 17471 1 1037 . 1 1 324 324 ASP N N 15 121.100 0.070 . 1 . . . . 324 ASP N . 17471 1 1038 . 1 1 326 326 TYR CA C 13 59.153 0.250 . 1 . . . . 326 TYR CA . 17471 1 1039 . 1 1 327 327 ASP H H 1 6.931 0.010 . 1 . . . . 327 ASP H . 17471 1 1040 . 1 1 327 327 ASP CA C 13 54.039 0.250 . 1 . . . . 327 ASP CA . 17471 1 1041 . 1 1 327 327 ASP CB C 13 41.033 0.250 . 1 . . . . 327 ASP CB . 17471 1 1042 . 1 1 327 327 ASP N N 15 123.144 0.070 . 1 . . . . 327 ASP N . 17471 1 1043 . 1 1 328 328 GLN H H 1 8.076 0.010 . 1 . . . . 328 GLN H . 17471 1 1044 . 1 1 328 328 GLN CA C 13 55.940 0.250 . 1 . . . . 328 GLN CA . 17471 1 1045 . 1 1 328 328 GLN CB C 13 31.685 0.250 . 1 . . . . 328 GLN CB . 17471 1 1046 . 1 1 328 328 GLN N N 15 121.360 0.070 . 1 . . . . 328 GLN N . 17471 1 1047 . 1 1 330 330 PHE CA C 13 63.945 0.250 . 1 . . . . 330 PHE CA . 17471 1 1048 . 1 1 331 331 GLU H H 1 9.845 0.010 . 1 . . . . 331 GLU H . 17471 1 1049 . 1 1 331 331 GLU CA C 13 58.215 0.250 . 1 . . . . 331 GLU CA . 17471 1 1050 . 1 1 331 331 GLU CB C 13 27.181 0.250 . 1 . . . . 331 GLU CB . 17471 1 1051 . 1 1 331 331 GLU N N 15 115.089 0.070 . 1 . . . . 331 GLU N . 17471 1 1052 . 1 1 332 332 SER H H 1 7.405 0.010 . 1 . . . . 332 SER H . 17471 1 1053 . 1 1 332 332 SER CA C 13 57.760 0.250 . 1 . . . . 332 SER CA . 17471 1 1054 . 1 1 332 332 SER CB C 13 62.958 0.250 . 1 . . . . 332 SER CB . 17471 1 1055 . 1 1 332 332 SER N N 15 112.114 0.070 . 1 . . . . 332 SER N . 17471 1 1056 . 1 1 333 333 ARG H H 1 7.556 0.010 . 1 . . . . 333 ARG H . 17471 1 1057 . 1 1 333 333 ARG CA C 13 55.832 0.250 . 1 . . . . 333 ARG CA . 17471 1 1058 . 1 1 333 333 ARG CB C 13 30.388 0.250 . 1 . . . . 333 ARG CB . 17471 1 1059 . 1 1 333 333 ARG N N 15 122.059 0.070 . 1 . . . . 333 ARG N . 17471 1 1060 . 1 1 334 334 ASP H H 1 8.505 0.010 . 1 . . . . 334 ASP H . 17471 1 1061 . 1 1 334 334 ASP CA C 13 53.128 0.250 . 1 . . . . 334 ASP CA . 17471 1 1062 . 1 1 334 334 ASP CB C 13 40.353 0.250 . 1 . . . . 334 ASP CB . 17471 1 1063 . 1 1 334 334 ASP N N 15 124.848 0.070 . 1 . . . . 334 ASP N . 17471 1 1064 . 1 1 335 335 LEU H H 1 7.761 0.010 . 1 . . . . 335 LEU H . 17471 1 1065 . 1 1 335 335 LEU CA C 13 52.512 0.250 . 1 . . . . 335 LEU CA . 17471 1 1066 . 1 1 335 335 LEU CB C 13 41.172 0.250 . 1 . . . . 335 LEU CB . 17471 1 1067 . 1 1 335 335 LEU N N 15 123.340 0.070 . 1 . . . . 335 LEU N . 17471 1 1068 . 1 1 336 336 LEU H H 1 8.718 0.010 . 1 . . . . 336 LEU H . 17471 1 1069 . 1 1 336 336 LEU CA C 13 53.717 0.250 . 1 . . . . 336 LEU CA . 17471 1 1070 . 1 1 336 336 LEU CB C 13 41.358 0.250 . 1 . . . . 336 LEU CB . 17471 1 1071 . 1 1 336 336 LEU N N 15 120.110 0.070 . 1 . . . . 336 LEU N . 17471 1 1072 . 1 1 337 337 ILE H H 1 8.912 0.010 . 1 . . . . 337 ILE H . 17471 1 1073 . 1 1 337 337 ILE CA C 13 66.452 0.250 . 1 . . . . 337 ILE CA . 17471 1 1074 . 1 1 337 337 ILE CB C 13 37.350 0.250 . 1 . . . . 337 ILE CB . 17471 1 1075 . 1 1 337 337 ILE N N 15 121.975 0.070 . 1 . . . . 337 ILE N . 17471 1 1076 . 1 1 338 338 ASP H H 1 8.333 0.010 . 1 . . . . 338 ASP H . 17471 1 1077 . 1 1 338 338 ASP CA C 13 56.903 0.250 . 1 . . . . 338 ASP CA . 17471 1 1078 . 1 1 338 338 ASP CB C 13 39.319 0.250 . 1 . . . . 338 ASP CB . 17471 1 1079 . 1 1 338 338 ASP N N 15 116.168 0.070 . 1 . . . . 338 ASP N . 17471 1 1080 . 1 1 339 339 GLU H H 1 7.065 0.010 . 1 . . . . 339 GLU H . 17471 1 1081 . 1 1 339 339 GLU CA C 13 58.323 0.250 . 1 . . . . 339 GLU CA . 17471 1 1082 . 1 1 339 339 GLU CB C 13 29.110 0.250 . 1 . . . . 339 GLU CB . 17471 1 1083 . 1 1 339 339 GLU N N 15 120.722 0.070 . 1 . . . . 339 GLU N . 17471 1 1084 . 1 1 340 340 TRP H H 1 7.658 0.010 . 1 . . . . 340 TRP H . 17471 1 1085 . 1 1 340 340 TRP CA C 13 59.742 0.250 . 1 . . . . 340 TRP CA . 17471 1 1086 . 1 1 340 340 TRP CB C 13 30.252 0.250 . 1 . . . . 340 TRP CB . 17471 1 1087 . 1 1 340 340 TRP N N 15 119.775 0.070 . 1 . . . . 340 TRP N . 17471 1 1088 . 1 1 341 341 LYS H H 1 8.705 0.010 . 1 . . . . 341 LYS H . 17471 1 1089 . 1 1 341 341 LYS CA C 13 60.009 0.250 . 1 . . . . 341 LYS CA . 17471 1 1090 . 1 1 341 341 LYS CB C 13 31.412 0.250 . 1 . . . . 341 LYS CB . 17471 1 1091 . 1 1 341 341 LYS N N 15 121.618 0.070 . 1 . . . . 341 LYS N . 17471 1 1092 . 1 1 342 342 SER H H 1 7.583 0.010 . 1 . . . . 342 SER H . 17471 1 1093 . 1 1 342 342 SER CA C 13 60.902 0.250 . 1 . . . . 342 SER CA . 17471 1 1094 . 1 1 342 342 SER CB C 13 61.987 0.250 . 1 . . . . 342 SER CB . 17471 1 1095 . 1 1 342 342 SER N N 15 114.776 0.070 . 1 . . . . 342 SER N . 17471 1 1096 . 1 1 343 343 LEU H H 1 7.887 0.010 . 1 . . . . 343 LEU H . 17471 1 1097 . 1 1 343 343 LEU CA C 13 57.439 0.250 . 1 . . . . 343 LEU CA . 17471 1 1098 . 1 1 343 343 LEU CB C 13 41.392 0.250 . 1 . . . . 343 LEU CB . 17471 1 1099 . 1 1 343 343 LEU N N 15 120.634 0.070 . 1 . . . . 343 LEU N . 17471 1 1100 . 1 1 345 345 TYR H H 1 8.774 0.010 . 1 . . . . 345 TYR H . 17471 1 1101 . 1 1 345 345 TYR CA C 13 61.643 0.250 . 1 . . . . 345 TYR CA . 17471 1 1102 . 1 1 345 345 TYR CB C 13 37.332 0.250 . 1 . . . . 345 TYR CB . 17471 1 1103 . 1 1 345 345 TYR N N 15 125.005 0.070 . 1 . . . . 345 TYR N . 17471 1 1104 . 1 1 346 346 ASP H H 1 8.011 0.010 . 1 . . . . 346 ASP H . 17471 1 1105 . 1 1 346 346 ASP CA C 13 56.930 0.250 . 1 . . . . 346 ASP CA . 17471 1 1106 . 1 1 346 346 ASP CB C 13 39.534 0.250 . 1 . . . . 346 ASP CB . 17471 1 1107 . 1 1 346 346 ASP N N 15 117.510 0.070 . 1 . . . . 346 ASP N . 17471 1 1108 . 1 1 347 347 GLU H H 1 7.454 0.010 . 1 . . . . 347 GLU H . 17471 1 1109 . 1 1 347 347 GLU CA C 13 57.690 0.250 . 1 . . . . 347 GLU CA . 17471 1 1110 . 1 1 347 347 GLU CB C 13 28.887 0.250 . 1 . . . . 347 GLU CB . 17471 1 1111 . 1 1 347 347 GLU N N 15 118.513 0.070 . 1 . . . . 347 GLU N . 17471 1 1112 . 1 1 348 348 VAL H H 1 8.028 0.010 . 1 . . . . 348 VAL H . 17471 1 1113 . 1 1 348 348 VAL CA C 13 65.739 0.250 . 1 . . . . 348 VAL CA . 17471 1 1114 . 1 1 348 348 VAL CB C 13 30.661 0.250 . 1 . . . . 348 VAL CB . 17471 1 1115 . 1 1 348 348 VAL N N 15 121.295 0.070 . 1 . . . . 348 VAL N . 17471 1 1116 . 1 1 349 349 ILE H H 1 8.058 0.010 . 1 . . . . 349 ILE H . 17471 1 1117 . 1 1 349 349 ILE CA C 13 62.874 0.250 . 1 . . . . 349 ILE CA . 17471 1 1118 . 1 1 349 349 ILE CB C 13 36.053 0.250 . 1 . . . . 349 ILE CB . 17471 1 1119 . 1 1 349 349 ILE N N 15 114.770 0.070 . 1 . . . . 349 ILE N . 17471 1 1120 . 1 1 350 350 SER H H 1 7.349 0.010 . 1 . . . . 350 SER H . 17471 1 1121 . 1 1 350 350 SER CA C 13 57.841 0.250 . 1 . . . . 350 SER CA . 17471 1 1122 . 1 1 350 350 SER CB C 13 63.284 0.250 . 1 . . . . 350 SER CB . 17471 1 1123 . 1 1 350 350 SER N N 15 113.552 0.070 . 1 . . . . 350 SER N . 17471 1 1124 . 1 1 351 351 PHE H H 1 7.252 0.010 . 1 . . . . 351 PHE H . 17471 1 1125 . 1 1 351 351 PHE CA C 13 60.170 0.250 . 1 . . . . 351 PHE CA . 17471 1 1126 . 1 1 351 351 PHE CB C 13 39.056 0.250 . 1 . . . . 351 PHE CB . 17471 1 1127 . 1 1 351 351 PHE N N 15 125.133 0.070 . 1 . . . . 351 PHE N . 17471 1 1128 . 1 1 352 352 VAL H H 1 6.862 0.010 . 1 . . . . 352 VAL H . 17471 1 1129 . 1 1 352 352 VAL CA C 13 63.225 0.250 . 1 . . . . 352 VAL CA . 17471 1 1130 . 1 1 352 352 VAL CB C 13 33.136 0.250 . 1 . . . . 352 VAL CB . 17471 1 1131 . 1 1 352 352 VAL N N 15 130.112 0.070 . 1 . . . . 352 VAL N . 17471 1 stop_ save_