data_15945 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 15945 _Entry.Title ; MDM2 N-terminal domain ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2008-09-08 _Entry.Accession_date 2008-09-08 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.116 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details '1H, 15N, C-alpha and C-beta assignments of human MDM2 residues 17-125' _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 Christiane Riedinger . . . 15945 2 James Mcdonnell . M. . 15945 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'University of Oxford' . 15945 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 15945 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 203 15945 '15N chemical shifts' 101 15945 '1H chemical shifts' 193 15945 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 2009-03-03 2008-09-08 update BMRB 'complete entry citation' 15945 1 . . 2008-10-13 2008-09-08 original author 'original release' 15945 stop_ save_ ############### # Citations # ############### save_citation _Citation.Sf_category citations _Citation.Sf_framecode citation _Citation.Entry_ID 15945 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 18959403 _Citation.Full_citation . _Citation.Title 'Analysis of chemical shift changes reveals the binding modes of isoindolinone inhibitors of the MDM2-p53 interaction' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Am. Chem. Soc.' _Citation.Journal_name_full . _Citation.Journal_volume 130 _Citation.Journal_issue 47 _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 16038 _Citation.Page_last 16044 _Citation.Year 2008 _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 Christiane Riedinger . . . 15945 1 2 Jane Endicott . A. . 15945 1 3 Stuart Kemp . J. . 15945 1 4 Lynette Smyth . A. . 15945 1 5 Anna Watson . . . 15945 1 6 Eric Valeur . . . 15945 1 7 Bernard Golding . T. . 15945 1 8 Roger Griffin . J. . 15945 1 9 Ian Hardcastle . R. . 15945 1 10 Martin Noble . E. . 15945 1 11 James McDonnell . M. . 15945 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 15945 _Assembly.ID 1 _Assembly.Name 'MDM2 N-terminal domain, residues 17-125' _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 12931.8 _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'N-terminal domain, p53 binding domain' 1 $human_mdm2_N-terminal_domain A . yes native no no . . . 15945 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 PDB 1YCR . . 'X-ray crystallography' 2.6 'mdm2 N-terminal domain bound to a p53 peptide' . 15945 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_human_mdm2_N-terminal_domain _Entity.Sf_category entity _Entity.Sf_framecode human_mdm2_N-terminal_domain _Entity.Entry_ID 15945 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name human_mdm2_N-terminal_domain _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 ; GPLGSSQIPASEQETLVRPK PLLLKLLKSVGAQKDTYTMK EVLFYLGQYIMTKRLYDEKQ QHIVYCSNDLLGDLFGVPSF SVKEHRKIYTMIYRNLVVVN QQESSDSGTSVSEN ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq 12-125 _Entity.Polymer_author_seq_details 'residues 12-16 correspond to the remnant of a GST-tag' _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 114 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment 'mdm2 17-125' _Entity.Mutation none _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 12931.8 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-26 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1RV1 . "Crystal Structure Of Human Mdm2 With An Imidazoline Inhibitor" . . . . . 74.56 85 98.82 98.82 7.68e-53 . . . . 15945 1 2 no PDB 1T4E . "Structure Of Human Mdm2 In Complex With A Benzodiazepine Inhibitor" . . . . . 83.33 96 100.00 100.00 9.48e-62 . . . . 15945 1 3 no PDB 1T4F . "Structure Of Human Mdm2 In Complex With An Optimized P53 Peptide" . . . . . 95.61 110 100.00 100.00 2.79e-72 . . . . 15945 1 4 no PDB 1YCR . "Mdm2 Bound To The Transactivation Domain Of P53" . . . . . 95.61 109 100.00 100.00 1.93e-72 . . . . 15945 1 5 no PDB 2AXI . "Hdm2 In Complex With A Beta-hairpin" . . . . . 95.61 115 100.00 100.00 1.79e-72 . . . . 15945 1 6 no PDB 2GV2 . "Mdm2 In Complex With An 8-Mer P53 Peptide Analogue" . . . . . 95.61 110 100.00 100.00 2.79e-72 . . . . 15945 1 7 no PDB 2M86 . "Solution Structure Of Hdm2 With Engineered Cyclotide" . . . . . 100.88 129 97.39 97.39 9.72e-73 . . . . 15945 1 8 no PDB 3EQS . "Crystal Structure Of Human Mdm2 In Complex With A 12-Mer Peptide Inhibitor" . . . . . 74.56 85 100.00 100.00 5.63e-54 . . . . 15945 1 9 no PDB 3G03 . "Structure Of Human Mdm2 In Complex With High Affinity Peptide" . . . . . 94.74 109 100.00 100.00 8.24e-72 . . . . 15945 1 10 no PDB 3IUX . "Crystal Structure Of Human Mdm2 In Complex With A Potent Miniature Protein Inhibitor (18-Residues)" . . . . . 74.56 85 100.00 100.00 5.63e-54 . . . . 15945 1 11 no PDB 3IWY . "Crystal Structure Of Human Mdm2 Complexed With D-peptide (12 Residues)" . . . . . 74.56 85 100.00 100.00 5.63e-54 . . . . 15945 1 12 no PDB 3JZK . "Crystal Structure Of Mdm2 With Chromenotriazolopyrimidine 1" . . . . . 83.33 96 100.00 100.00 9.48e-62 . . . . 15945 1 13 no PDB 3JZR . "Human Mdm2 Liganded With A 12mer Peptide Inhibitor (Pdi6w)" . . . . . 95.61 110 100.00 100.00 2.79e-72 . . . . 15945 1 14 no PDB 3JZS . "Human Mdm2 Liganded With A 12mer Peptide Inhibitor (Pdiq)" . . . . . 75.44 86 100.00 100.00 9.83e-55 . . . . 15945 1 15 no PDB 3LBK . "Structure Of Human Mdm2 Protein In Complex With A Small Molecule Inhibitor" . . . . . 82.46 95 98.94 98.94 3.95e-60 . . . . 15945 1 16 no PDB 3LBL . "Structure Of Human Mdm2 Protein In Complex With Mi-63-Analog" . . . . . 82.46 95 100.00 100.00 3.05e-61 . . . . 15945 1 17 no PDB 3LNJ . "Crystal Structure Of Human Mdm2 In Complex With D-Peptide Inhibitor (Dpmi-Alpha)" . . . . . 74.56 85 100.00 100.00 5.63e-54 . . . . 15945 1 18 no PDB 3LNZ . "Crystal Structure Of Human Mdm2 With A 12-Mer Peptide Inhibitor Pmi (N8a Mutant)" . . . . . 74.56 85 100.00 100.00 5.63e-54 . . . . 15945 1 19 no PDB 3TJ2 . "Structure Of A Novel Submicromolar Mdm2 Inhibitor" . . . . . 82.46 95 100.00 100.00 3.05e-61 . . . . 15945 1 20 no PDB 3TPX . "Crystal Structure Of Human Mdm2 In Complex With A Trifluoromethylated D-peptide Inhibitor" . . . . . 74.56 85 100.00 100.00 5.63e-54 . . . . 15945 1 21 no PDB 3TU1 . "Exhaustive Fluorine Scanning Towards Potent P53-Mdm2 Antagonist" . . . . . 94.74 108 100.00 100.00 1.13e-71 . . . . 15945 1 22 no PDB 3V3B . "Structure Of The Stapled P53 Peptide Bound To Mdm2" . . . . . 76.32 88 100.00 100.00 1.93e-55 . . . . 15945 1 23 no PDB 3VBG . "Structure Of Hdm2 With Dimer Inducing Indolyl Hydantoin Ro-2443" . . . . . 74.56 85 98.82 98.82 7.68e-53 . . . . 15945 1 24 no PDB 3VZV . "Crystal Structure Of Human Mdm2 With A Dihydroimidazothiazole Inhibitor" . . . . . 74.56 87 98.82 98.82 7.79e-53 . . . . 15945 1 25 no PDB 3W69 . "Crystal Structure Of Human Mdm2 With A Dihydroimidazothiazole Inhibitor" . . . . . 74.56 87 98.82 98.82 7.79e-53 . . . . 15945 1 26 no PDB 4DIJ . "The Central Valine Concept Provides An Entry In A New Class Of Non Peptide Inhibitors Of The P53-Mdm2 Interaction" . . . . . 83.33 96 98.95 98.95 1.28e-60 . . . . 15945 1 27 no PDB 4ERE . "Crystal Structure Of Mdm2 (17-111) In Complex With Compound 23" . . . . . 83.33 96 100.00 100.00 9.48e-62 . . . . 15945 1 28 no PDB 4ERF . "Crystal Structure Of Mdm2 (17-111) In Complex With Compound 29 (Am- 8553)" . . . . . 83.33 96 100.00 100.00 9.48e-62 . . . . 15945 1 29 no PDB 4HFZ . "Crystal Structure Of An Mdm2/p53 Peptide Complex" . . . . . 95.61 109 98.17 98.17 5.44e-71 . . . . 15945 1 30 no PDB 4HG7 . "Crystal Structure Of An Mdm2/nutlin-3a Complex" . . . . . 85.09 97 97.94 97.94 3.51e-62 . . . . 15945 1 31 no PDB 4JV7 . "Co-crystal Structure Of Mdm2 With Inhibitor (2s,5r,6s)-2-benzyl-5,6- Bis(4-bromophenyl)-4-methylmorpholin-3-one" . . . . . 82.46 96 100.00 100.00 3.87e-61 . . . . 15945 1 32 no PDB 4JV9 . "Co-crystal Structure Of Mdm2 With Inhibitor (2s,5r,6s)-2-benzyl-5,6- Bis(4-chlorophenyl)-4-methylmorpholin-3-one" . . . . . 82.46 96 100.00 100.00 3.87e-61 . . . . 15945 1 33 no PDB 4JVE . "Co-crystal Structure Of Mdm2 With Inhibitor (2r,3e)-2-[(2s,3r,6s)-2,3- Bis(4-chlorophenyl)-6-(4-fluorobenzyl)-5-oxomorpholin-4-" . . . . . 82.46 96 100.00 100.00 3.87e-61 . . . . 15945 1 34 no PDB 4JVR . "Co-crystal Structure Of Mdm2 With Inhibitor (2's,3r,4's,5'r)-n-(2- Aminoethyl)-6-chloro-4'-(3-chloro-2-fluorophenyl)-2'-(2,2- D" . . . . . 82.46 96 100.00 100.00 3.87e-61 . . . . 15945 1 35 no PDB 4JWR . "Co-crystal Structure Of Mdm2 With Inhibitor {(2s,5r,6s)-6-(3- Chlorophenyl)-5-(4-chlorophenyl)-4-[(2s)-1-hydroxybutan-2-yl]-3- " . . . . . 83.33 95 100.00 100.00 7.08e-62 . . . . 15945 1 36 no PDB 4MDN . "Structure Of A Novel Submicromolar Mdm2 Inhibitor" . . . . . 81.58 94 100.00 100.00 2.86e-60 . . . . 15945 1 37 no PDB 4MDQ . "Structure Of A Novel Submicromolar Mdm2 Inhibitor" . . . . . 75.44 86 100.00 100.00 1.54e-54 . . . . 15945 1 38 no PDB 4OAS . "Co-crystal Structure Of Mdm2 (17-111) In Complex With Compound 25" . . . . . 83.33 96 100.00 100.00 9.48e-62 . . . . 15945 1 39 no PDB 4OBA . "Co-crystal Structure Of Mdm2 With Inhibitor Compound 4" . . . . . 83.33 96 100.00 100.00 9.48e-62 . . . . 15945 1 40 no PDB 4OCC . "Co-crystal Structure Of Mdm2(17-111) In Complex With Compound 48" . . . . . 83.33 96 100.00 100.00 9.48e-62 . . . . 15945 1 41 no PDB 4OGV . "Co-crystal Structure Of Mdm2 With Inhibitor Compound 49" . . . . . 83.33 95 100.00 100.00 7.08e-62 . . . . 15945 1 42 no PDB 4OQ3 . "Tetra-substituted Imidazoles As A New Class Of Inhibitors Of The P53- Mdm2 Interaction" . . . . . 83.33 96 98.95 98.95 1.28e-60 . . . . 15945 1 43 no PDB 4QO4 . "Co-crystal Structure Of Mdm2 (17-111) With Compound 16, {(3r,5r,6s)-5- (3-chlorophenyl)-6-(4-chlorophenyl)-1-[(1s)-1-(6-cyclopr" . . . . . 83.33 96 100.00 100.00 9.48e-62 . . . . 15945 1 44 no PDB 4QOC . "Crystal Structure Of Compound 16 Bound To Mdm2(17-111), {(3r,5r,6s)-5- (3-chlorophenyl)-6-(4-chlorophenyl)-1-[(1s)-1-cyclopropy" . . . . . 83.33 96 100.00 100.00 9.48e-62 . . . . 15945 1 45 no PDB 4ZYC . "Discovery Of Dihydroisoquinolinone Derivatives As Novel Inhibitors Of The P53-mdm2 Interaction With A Distinct Binding Mode: Hd" . . . . . 83.33 96 98.95 98.95 1.28e-60 . . . . 15945 1 46 no PDB 4ZYF . "Discovery Of Nvp-cgm097 - A Highly Potent And Selective Mdm2 Inhibitor Undergoing Phase 1 Clinical Trials In P53wt Tumors: Hdm2" . . . . . 83.33 96 100.00 100.00 9.48e-62 . . . . 15945 1 47 no PDB 4ZYI . "Discovery Of Nvp-cgm097 - A Highly Potent And Selective Mdm2 Inhibitor Undergoing Phase 1 Clinical Trials In P53wt Tumors: Hdm2" . . . . . 83.33 96 100.00 100.00 9.48e-62 . . . . 15945 1 48 no REF XP_006719462 . "PREDICTED: E3 ubiquitin-protein ligase Mdm2 isoform X2 [Homo sapiens]" . . . . . 56.14 430 100.00 100.00 2.03e-35 . . . . 15945 1 49 no REF XP_012911529 . "PREDICTED: E3 ubiquitin-protein ligase Mdm2 isoform X2 [Mustela putorius furo]" . . . . . 56.14 426 98.44 98.44 1.25e-34 . . . . 15945 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'p53-binding domain' 15945 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 12 GLY . 15945 1 2 13 PRO . 15945 1 3 14 LEU . 15945 1 4 15 GLY . 15945 1 5 16 SER . 15945 1 6 17 SER . 15945 1 7 18 GLN . 15945 1 8 19 ILE . 15945 1 9 20 PRO . 15945 1 10 21 ALA . 15945 1 11 22 SER . 15945 1 12 23 GLU . 15945 1 13 24 GLN . 15945 1 14 25 GLU . 15945 1 15 26 THR . 15945 1 16 27 LEU . 15945 1 17 28 VAL . 15945 1 18 29 ARG . 15945 1 19 30 PRO . 15945 1 20 31 LYS . 15945 1 21 32 PRO . 15945 1 22 33 LEU . 15945 1 23 34 LEU . 15945 1 24 35 LEU . 15945 1 25 36 LYS . 15945 1 26 37 LEU . 15945 1 27 38 LEU . 15945 1 28 39 LYS . 15945 1 29 40 SER . 15945 1 30 41 VAL . 15945 1 31 42 GLY . 15945 1 32 43 ALA . 15945 1 33 44 GLN . 15945 1 34 45 LYS . 15945 1 35 46 ASP . 15945 1 36 47 THR . 15945 1 37 48 TYR . 15945 1 38 49 THR . 15945 1 39 50 MET . 15945 1 40 51 LYS . 15945 1 41 52 GLU . 15945 1 42 53 VAL . 15945 1 43 54 LEU . 15945 1 44 55 PHE . 15945 1 45 56 TYR . 15945 1 46 57 LEU . 15945 1 47 58 GLY . 15945 1 48 59 GLN . 15945 1 49 60 TYR . 15945 1 50 61 ILE . 15945 1 51 62 MET . 15945 1 52 63 THR . 15945 1 53 64 LYS . 15945 1 54 65 ARG . 15945 1 55 66 LEU . 15945 1 56 67 TYR . 15945 1 57 68 ASP . 15945 1 58 69 GLU . 15945 1 59 70 LYS . 15945 1 60 71 GLN . 15945 1 61 72 GLN . 15945 1 62 73 HIS . 15945 1 63 74 ILE . 15945 1 64 75 VAL . 15945 1 65 76 TYR . 15945 1 66 77 CYS . 15945 1 67 78 SER . 15945 1 68 79 ASN . 15945 1 69 80 ASP . 15945 1 70 81 LEU . 15945 1 71 82 LEU . 15945 1 72 83 GLY . 15945 1 73 84 ASP . 15945 1 74 85 LEU . 15945 1 75 86 PHE . 15945 1 76 87 GLY . 15945 1 77 88 VAL . 15945 1 78 89 PRO . 15945 1 79 90 SER . 15945 1 80 91 PHE . 15945 1 81 92 SER . 15945 1 82 93 VAL . 15945 1 83 94 LYS . 15945 1 84 95 GLU . 15945 1 85 96 HIS . 15945 1 86 97 ARG . 15945 1 87 98 LYS . 15945 1 88 99 ILE . 15945 1 89 100 TYR . 15945 1 90 101 THR . 15945 1 91 102 MET . 15945 1 92 103 ILE . 15945 1 93 104 TYR . 15945 1 94 105 ARG . 15945 1 95 106 ASN . 15945 1 96 107 LEU . 15945 1 97 108 VAL . 15945 1 98 109 VAL . 15945 1 99 110 VAL . 15945 1 100 111 ASN . 15945 1 101 112 GLN . 15945 1 102 113 GLN . 15945 1 103 114 GLU . 15945 1 104 115 SER . 15945 1 105 116 SER . 15945 1 106 117 ASP . 15945 1 107 118 SER . 15945 1 108 119 GLY . 15945 1 109 120 THR . 15945 1 110 121 SER . 15945 1 111 122 VAL . 15945 1 112 123 SER . 15945 1 113 124 GLU . 15945 1 114 125 ASN . 15945 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 15945 1 . PRO 2 2 15945 1 . LEU 3 3 15945 1 . GLY 4 4 15945 1 . SER 5 5 15945 1 . SER 6 6 15945 1 . GLN 7 7 15945 1 . ILE 8 8 15945 1 . PRO 9 9 15945 1 . ALA 10 10 15945 1 . SER 11 11 15945 1 . GLU 12 12 15945 1 . GLN 13 13 15945 1 . GLU 14 14 15945 1 . THR 15 15 15945 1 . LEU 16 16 15945 1 . VAL 17 17 15945 1 . ARG 18 18 15945 1 . PRO 19 19 15945 1 . LYS 20 20 15945 1 . PRO 21 21 15945 1 . LEU 22 22 15945 1 . LEU 23 23 15945 1 . LEU 24 24 15945 1 . LYS 25 25 15945 1 . LEU 26 26 15945 1 . LEU 27 27 15945 1 . LYS 28 28 15945 1 . SER 29 29 15945 1 . VAL 30 30 15945 1 . GLY 31 31 15945 1 . ALA 32 32 15945 1 . GLN 33 33 15945 1 . LYS 34 34 15945 1 . ASP 35 35 15945 1 . THR 36 36 15945 1 . TYR 37 37 15945 1 . THR 38 38 15945 1 . MET 39 39 15945 1 . LYS 40 40 15945 1 . GLU 41 41 15945 1 . VAL 42 42 15945 1 . LEU 43 43 15945 1 . PHE 44 44 15945 1 . TYR 45 45 15945 1 . LEU 46 46 15945 1 . GLY 47 47 15945 1 . GLN 48 48 15945 1 . TYR 49 49 15945 1 . ILE 50 50 15945 1 . MET 51 51 15945 1 . THR 52 52 15945 1 . LYS 53 53 15945 1 . ARG 54 54 15945 1 . LEU 55 55 15945 1 . TYR 56 56 15945 1 . ASP 57 57 15945 1 . GLU 58 58 15945 1 . LYS 59 59 15945 1 . GLN 60 60 15945 1 . GLN 61 61 15945 1 . HIS 62 62 15945 1 . ILE 63 63 15945 1 . VAL 64 64 15945 1 . TYR 65 65 15945 1 . CYS 66 66 15945 1 . SER 67 67 15945 1 . ASN 68 68 15945 1 . ASP 69 69 15945 1 . LEU 70 70 15945 1 . LEU 71 71 15945 1 . GLY 72 72 15945 1 . ASP 73 73 15945 1 . LEU 74 74 15945 1 . PHE 75 75 15945 1 . GLY 76 76 15945 1 . VAL 77 77 15945 1 . PRO 78 78 15945 1 . SER 79 79 15945 1 . PHE 80 80 15945 1 . SER 81 81 15945 1 . VAL 82 82 15945 1 . LYS 83 83 15945 1 . GLU 84 84 15945 1 . HIS 85 85 15945 1 . ARG 86 86 15945 1 . LYS 87 87 15945 1 . ILE 88 88 15945 1 . TYR 89 89 15945 1 . THR 90 90 15945 1 . MET 91 91 15945 1 . ILE 92 92 15945 1 . TYR 93 93 15945 1 . ARG 94 94 15945 1 . ASN 95 95 15945 1 . LEU 96 96 15945 1 . VAL 97 97 15945 1 . VAL 98 98 15945 1 . VAL 99 99 15945 1 . ASN 100 100 15945 1 . GLN 101 101 15945 1 . GLN 102 102 15945 1 . GLU 103 103 15945 1 . SER 104 104 15945 1 . SER 105 105 15945 1 . ASP 106 106 15945 1 . SER 107 107 15945 1 . GLY 108 108 15945 1 . THR 109 109 15945 1 . SER 110 110 15945 1 . VAL 111 111 15945 1 . SER 112 112 15945 1 . GLU 113 113 15945 1 . ASN 114 114 15945 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 15945 _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 $human_mdm2_N-terminal_domain . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 15945 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 15945 _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 $human_mdm2_N-terminal_domain . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli BL21 DE3 . . . . . . . . . . . . . . 'pGEX 6P1' . . . 'GST-tagged, 3C precision protease cleavable' . . 15945 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_mdm2_17-125 _Sample.Sf_category sample _Sample.Sf_framecode mdm2_17-125 _Sample.Entry_ID 15945 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'prepared as GST-fusion in a 3-step purification procedure comprising affinity chromatography, 3C precision protease cleavage and a final gel filtration step.' _Sample.Aggregate_sample_number . _Sample.Solvent_system '5% D20, 5% glycerol, 90% water' _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 H2O 'natural abundance' . . . . . . 90 . . % . . . . 15945 1 2 D2O 'natural abundance' . . . . . . 5 . . % . . . . 15945 1 3 DMSO 'natural abundance' . . . . . . 5 . . % . . . . 15945 1 4 NaCl 'natural abundance' . . . . . . 50 . . mM . . . . 15945 1 5 'Sodium Phosphate pH 6.5' 'natural abundance' . . . . . . 25 . . mM . . . . 15945 1 6 Mono-Thioglycerol 'natural abundance' . . . . . . 0.02 . . % . . . . 15945 1 7 'Sodium Azide' 'natural abundance' . . . . . . 0.02 . . % . . . . 15945 1 8 glycerol 'natural abundance' . . . . . . 5 . . % . . . . 15945 1 9 human_mdm2_N-terminal_domain 'natural abundance' . . 1 $human_mdm2_N-terminal_domain . . . . . . . . . . 15945 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions _Sample_condition_list.Entry_ID 15945 _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' 125 . mM 15945 1 pH 6.5 . pH 15945 1 pressure 1 . atm 15945 1 temperature 293.15 . K 15945 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 15945 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 15945 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 15945 1 stop_ save_ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 15945 _Software.ID 2 _Software.Name NMRView _Software.Version 5.2.2 _Software.Details 'tcl version' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'bruce johnson, onemoonscientific' . . 15945 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 15945 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 15945 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'a GE/Oxford instruments magnet fitted with a bruker cryogenic probe and console.' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 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 15945 _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 DMX . 500 'a GE/Oxford instruments magnet fitted with a bruker cryogenic probe and console.' . . 15945 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 15945 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $mdm2_17-125 isotropic . . 1 $sample_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15945 1 2 '3D HNCA' no . . . . . . . . . . 1 $mdm2_17-125 isotropic . . 1 $sample_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15945 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_DSS _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode DSS _Chem_shift_reference.Entry_ID 15945 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0 internal direct 1.0 . . . . . . . . . 15945 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 15945 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $DSS _Assigned_chem_shift_list.Chem_shift_1H_err 0.00425 _Assigned_chem_shift_list.Chem_shift_13C_err 0.087 _Assigned_chem_shift_list.Chem_shift_15N_err 0.07 _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 '1/2 the digital resolution error stated in ppm/pt.' _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '3D CBCA(CO)NH' . . . 15945 1 2 '3D HNCA' . . . 15945 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 LEU CA C 13 54.9110 0.087 . 1 . . . . 14 LEU CA . 15945 1 2 . 1 1 3 3 LEU CB C 13 42.0810 0.087 . 1 . . . . 14 LEU CB . 15945 1 3 . 1 1 4 4 GLY H H 1 8.4230 0.00425 . 1 . . . . 15 GLY HN . 15945 1 4 . 1 1 4 4 GLY CA C 13 45.3620 0.087 . 1 . . . . 15 GLY CA . 15945 1 5 . 1 1 4 4 GLY N N 15 109.6860 0.07 . 1 . . . . 15 GLY N . 15945 1 6 . 1 1 5 5 SER H H 1 8.2650 0.00425 . 1 . . . . 16 SER HN . 15945 1 7 . 1 1 5 5 SER CA C 13 58.9600 0.087 . 1 . . . . 16 SER CA . 15945 1 8 . 1 1 5 5 SER CB C 13 63.5400 0.087 . 1 . . . . 16 SER CB . 15945 1 9 . 1 1 5 5 SER N N 15 114.4660 0.07 . 1 . . . . 16 SER N . 15945 1 10 . 1 1 6 6 SER H H 1 8.6100 0.00425 . 1 . . . . 17 SER HN . 15945 1 11 . 1 1 6 6 SER CA C 13 57.9270 0.087 . 1 . . . . 17 SER CA . 15945 1 12 . 1 1 6 6 SER CB C 13 63.2310 0.087 . 1 . . . . 17 SER CB . 15945 1 13 . 1 1 6 6 SER N N 15 121.1110 0.07 . 1 . . . . 17 SER N . 15945 1 14 . 1 1 7 7 GLN H H 1 9.2520 0.00425 . 1 . . . . 18 GLN HN . 15945 1 15 . 1 1 7 7 GLN CA C 13 56.1160 0.087 . 1 . . . . 18 GLN CA . 15945 1 16 . 1 1 7 7 GLN CB C 13 29.2090 0.087 . 1 . . . . 18 GLN CB . 15945 1 17 . 1 1 7 7 GLN N N 15 121.6550 0.07 . 1 . . . . 18 GLN N . 15945 1 18 . 1 1 8 8 ILE H H 1 7.9390 0.00425 . 1 . . . . 19 ILE HN . 15945 1 19 . 1 1 8 8 ILE HA H 1 4.3070 0.00425 . 1 . . . . 19 ILE HA . 15945 1 20 . 1 1 8 8 ILE HB H 1 1.7700 0.00425 . 1 . . . . 19 ILE HB . 15945 1 21 . 1 1 8 8 ILE CA C 13 56.9460 0.087 . 1 . . . . 19 ILE CA . 15945 1 22 . 1 1 8 8 ILE N N 15 122.6140 0.07 . 1 . . . . 19 ILE N . 15945 1 23 . 1 1 9 9 PRO CA C 13 63.5450 0.087 . 1 . . . . 20 PRO CA . 15945 1 24 . 1 1 9 9 PRO CB C 13 32.4930 0.087 . 1 . . . . 20 PRO CB . 15945 1 25 . 1 1 10 10 ALA H H 1 8.8350 0.00425 . 1 . . . . 21 ALA HN . 15945 1 26 . 1 1 10 10 ALA CA C 13 55.5420 0.087 . 1 . . . . 21 ALA CA . 15945 1 27 . 1 1 10 10 ALA CB C 13 18.4230 0.087 . 1 . . . . 21 ALA CB . 15945 1 28 . 1 1 10 10 ALA N N 15 126.9740 0.07 . 1 . . . . 21 ALA N . 15945 1 29 . 1 1 11 11 SER H H 1 8.5820 0.00425 . 1 . . . . 22 SER HN . 15945 1 30 . 1 1 11 11 SER CA C 13 60.5210 0.087 . 1 . . . . 22 SER CA . 15945 1 31 . 1 1 11 11 SER CB C 13 62.1500 0.087 . 1 . . . . 22 SER CB . 15945 1 32 . 1 1 11 11 SER N N 15 111.1830 0.07 . 1 . . . . 22 SER N . 15945 1 33 . 1 1 12 12 GLU H H 1 7.5520 0.00425 . 1 . . . . 23 GLU HN . 15945 1 34 . 1 1 12 12 GLU CA C 13 58.0990 0.087 . 1 . . . . 23 GLU CA . 15945 1 35 . 1 1 12 12 GLU CB C 13 29.9790 0.087 . 1 . . . . 23 GLU CB . 15945 1 36 . 1 1 12 12 GLU N N 15 122.9790 0.07 . 1 . . . . 23 GLU N . 15945 1 37 . 1 1 13 13 GLN H H 1 7.9260 0.00425 . 1 . . . . 24 GLN HN . 15945 1 38 . 1 1 13 13 GLN CA C 13 58.6730 0.087 . 1 . . . . 24 GLN CA . 15945 1 39 . 1 1 13 13 GLN CB C 13 29.1900 0.087 . 1 . . . . 24 GLN CB . 15945 1 40 . 1 1 13 13 GLN N N 15 118.9380 0.07 . 1 . . . . 24 GLN N . 15945 1 41 . 1 1 14 14 GLU H H 1 7.6430 0.00425 . 1 . . . . 25 GLU HN . 15945 1 42 . 1 1 14 14 GLU CA C 13 55.7850 0.087 . 1 . . . . 25 GLU CA . 15945 1 43 . 1 1 14 14 GLU CB C 13 29.8210 0.087 . 1 . . . . 25 GLU CB . 15945 1 44 . 1 1 14 14 GLU N N 15 114.6480 0.07 . 1 . . . . 25 GLU N . 15945 1 45 . 1 1 15 15 THR H H 1 7.4970 0.00425 . 1 . . . . 26 THR HN . 15945 1 46 . 1 1 15 15 THR HA H 1 4.0230 0.00425 . 1 . . . . 26 THR HA . 15945 1 47 . 1 1 15 15 THR CA C 13 64.8870 0.087 . 1 . . . . 26 THR CA . 15945 1 48 . 1 1 15 15 THR CB C 13 70.2140 0.087 . 1 . . . . 26 THR CB . 15945 1 49 . 1 1 15 15 THR N N 15 117.4120 0.07 . 1 . . . . 26 THR N . 15945 1 50 . 1 1 16 16 LEU H H 1 8.4840 0.00425 . 1 . . . . 27 LEU HN . 15945 1 51 . 1 1 16 16 LEU CA C 13 54.6710 0.087 . 1 . . . . 27 LEU CA . 15945 1 52 . 1 1 16 16 LEU CB C 13 43.2660 0.087 . 1 . . . . 27 LEU CB . 15945 1 53 . 1 1 16 16 LEU N N 15 128.2150 0.07 . 1 . . . . 27 LEU N . 15945 1 54 . 1 1 17 17 VAL H H 1 9.8030 0.00425 . 1 . . . . 28 VAL HN . 15945 1 55 . 1 1 17 17 VAL CA C 13 59.1520 0.087 . 1 . . . . 28 VAL CA . 15945 1 56 . 1 1 17 17 VAL CB C 13 36.5240 0.087 . 1 . . . . 28 VAL CB . 15945 1 57 . 1 1 17 17 VAL N N 15 116.9750 0.07 . 1 . . . . 28 VAL N . 15945 1 58 . 1 1 18 18 ARG H H 1 9.2500 0.00425 . 1 . . . . 29 ARG HN . 15945 1 59 . 1 1 18 18 ARG CA C 13 52.4880 0.087 . 1 . . . . 29 ARG CA . 15945 1 60 . 1 1 18 18 ARG N N 15 121.6550 0.07 . 1 . . . . 29 ARG N . 15945 1 61 . 1 1 19 19 PRO CA C 13 62.9490 0.087 . 1 . . . . 30 PRO CA . 15945 1 62 . 1 1 19 19 PRO CB C 13 32.6750 0.087 . 1 . . . . 30 PRO CB . 15945 1 63 . 1 1 20 20 LYS H H 1 8.3120 0.00425 . 1 . . . . 31 LYS HN . 15945 1 64 . 1 1 20 20 LYS CA C 13 56.7750 0.087 . 1 . . . . 31 LYS CA . 15945 1 65 . 1 1 20 20 LYS N N 15 123.2810 0.07 . 1 . . . . 31 LYS N . 15945 1 66 . 1 1 21 21 PRO CA C 13 67.5880 0.087 . 1 . . . . 32 PRO CA . 15945 1 67 . 1 1 21 21 PRO CB C 13 32.6510 0.087 . 1 . . . . 32 PRO CB . 15945 1 68 . 1 1 22 22 LEU H H 1 8.9210 0.00425 . 1 . . . . 33 LEU HN . 15945 1 69 . 1 1 22 22 LEU CA C 13 58.3380 0.087 . 1 . . . . 33 LEU CA . 15945 1 70 . 1 1 22 22 LEU CB C 13 41.4550 0.087 . 1 . . . . 33 LEU CB . 15945 1 71 . 1 1 22 22 LEU N N 15 118.4450 0.07 . 1 . . . . 33 LEU N . 15945 1 72 . 1 1 23 23 LEU H H 1 7.4390 0.00425 . 1 . . . . 34 LEU HN . 15945 1 73 . 1 1 23 23 LEU HA H 1 4.0760 0.00425 . 1 . . . . 34 LEU HA . 15945 1 74 . 1 1 23 23 LEU CA C 13 56.7990 0.087 . 1 . . . . 34 LEU CA . 15945 1 75 . 1 1 23 23 LEU CB C 13 40.7980 0.087 . 1 . . . . 34 LEU CB . 15945 1 76 . 1 1 23 23 LEU N N 15 118.2640 0.07 . 1 . . . . 34 LEU N . 15945 1 77 . 1 1 24 24 LEU H H 1 8.5920 0.00425 . 1 . . . . 35 LEU HN . 15945 1 78 . 1 1 24 24 LEU CA C 13 58.1860 0.087 . 1 . . . . 35 LEU CA . 15945 1 79 . 1 1 24 24 LEU CB C 13 41.4150 0.087 . 1 . . . . 35 LEU CB . 15945 1 80 . 1 1 24 24 LEU N N 15 120.1010 0.07 . 1 . . . . 35 LEU N . 15945 1 81 . 1 1 25 25 LYS H H 1 7.9480 0.00425 . 1 . . . . 36 LYS HN . 15945 1 82 . 1 1 25 25 LYS HA H 1 3.8420 0.00425 . 1 . . . . 36 LYS HA . 15945 1 83 . 1 1 25 25 LYS CA C 13 59.7300 0.087 . 1 . . . . 36 LYS CA . 15945 1 84 . 1 1 25 25 LYS CB C 13 32.2680 0.087 . 1 . . . . 36 LYS CB . 15945 1 85 . 1 1 25 25 LYS N N 15 118.2050 0.07 . 1 . . . . 36 LYS N . 15945 1 86 . 1 1 26 26 LEU H H 1 7.3380 0.00425 . 1 . . . . 37 LEU HN . 15945 1 87 . 1 1 26 26 LEU CA C 13 59.6420 0.087 . 1 . . . . 37 LEU CA . 15945 1 88 . 1 1 26 26 LEU CB C 13 41.1600 0.087 . 1 . . . . 37 LEU CB . 15945 1 89 . 1 1 26 26 LEU N N 15 121.0970 0.07 . 1 . . . . 37 LEU N . 15945 1 90 . 1 1 27 27 LEU H H 1 8.1990 0.00425 . 1 . . . . 38 LEU HN . 15945 1 91 . 1 1 27 27 LEU CA C 13 57.9800 0.087 . 1 . . . . 38 LEU CA . 15945 1 92 . 1 1 27 27 LEU CB C 13 39.1310 0.087 . 1 . . . . 38 LEU CB . 15945 1 93 . 1 1 27 27 LEU N N 15 120.4260 0.07 . 1 . . . . 38 LEU N . 15945 1 94 . 1 1 28 28 LYS H H 1 8.8530 0.00425 . 1 . . . . 39 LYS HN . 15945 1 95 . 1 1 28 28 LYS CA C 13 59.3680 0.087 . 1 . . . . 39 LYS CA . 15945 1 96 . 1 1 28 28 LYS N N 15 118.1960 0.07 . 1 . . . . 39 LYS N . 15945 1 97 . 1 1 29 29 SER H H 1 7.8690 0.00425 . 1 . . . . 40 SER HN . 15945 1 98 . 1 1 29 29 SER HA H 1 4.4340 0.00425 . 1 . . . . 40 SER HA . 15945 1 99 . 1 1 29 29 SER CA C 13 61.9030 0.087 . 1 . . . . 40 SER CA . 15945 1 100 . 1 1 29 29 SER CB C 13 63.0050 0.087 . 1 . . . . 40 SER CB . 15945 1 101 . 1 1 29 29 SER N N 15 116.7260 0.07 . 1 . . . . 40 SER N . 15945 1 102 . 1 1 30 30 VAL H H 1 7.2900 0.00425 . 1 . . . . 41 VAL HN . 15945 1 103 . 1 1 30 30 VAL HA H 1 4.8130 0.00425 . 1 . . . . 41 VAL HA . 15945 1 104 . 1 1 30 30 VAL CA C 13 60.4970 0.087 . 1 . . . . 41 VAL CA . 15945 1 105 . 1 1 30 30 VAL CB C 13 30.8010 0.087 . 1 . . . . 41 VAL CB . 15945 1 106 . 1 1 30 30 VAL N N 15 112.5690 0.07 . 1 . . . . 41 VAL N . 15945 1 107 . 1 1 31 31 GLY H H 1 7.5510 0.00425 . 1 . . . . 42 GLY HN . 15945 1 108 . 1 1 31 31 GLY HA2 H 1 4.4400 0.00425 . 2 . . . . 42 GLY HA1 . 15945 1 109 . 1 1 31 31 GLY HA3 H 1 3.7800 0.00425 . 2 . . . . 42 GLY HA2 . 15945 1 110 . 1 1 31 31 GLY CA C 13 45.5990 0.087 . 1 . . . . 42 GLY CA . 15945 1 111 . 1 1 31 31 GLY N N 15 106.2630 0.07 . 1 . . . . 42 GLY N . 15945 1 112 . 1 1 32 32 ALA H H 1 7.3800 0.00425 . 1 . . . . 43 ALA HN . 15945 1 113 . 1 1 32 32 ALA HA H 1 4.0530 0.00425 . 1 . . . . 43 ALA HA . 15945 1 114 . 1 1 32 32 ALA CA C 13 53.2060 0.087 . 1 . . . . 43 ALA CA . 15945 1 115 . 1 1 32 32 ALA CB C 13 18.4730 0.087 . 1 . . . . 43 ALA CB . 15945 1 116 . 1 1 32 32 ALA N N 15 124.9500 0.07 . 1 . . . . 43 ALA N . 15945 1 117 . 1 1 33 33 GLN H H 1 8.7780 0.00425 . 1 . . . . 44 GLN HN . 15945 1 118 . 1 1 33 33 GLN HA H 1 4.5920 0.00425 . 1 . . . . 44 GLN HA . 15945 1 119 . 1 1 33 33 GLN CA C 13 55.7290 0.087 . 1 . . . . 44 GLN CA . 15945 1 120 . 1 1 33 33 GLN CB C 13 31.0640 0.087 . 1 . . . . 44 GLN CB . 15945 1 121 . 1 1 33 33 GLN N N 15 118.1150 0.07 . 1 . . . . 44 GLN N . 15945 1 122 . 1 1 34 34 LYS H H 1 7.3830 0.00425 . 1 . . . . 45 LYS HN . 15945 1 123 . 1 1 34 34 LYS HA H 1 4.6990 0.00425 . 1 . . . . 45 LYS HA . 15945 1 124 . 1 1 34 34 LYS CA C 13 63.3850 0.087 . 1 . . . . 45 LYS CA . 15945 1 125 . 1 1 34 34 LYS CB C 13 32.4550 0.087 . 1 . . . . 45 LYS CB . 15945 1 126 . 1 1 34 34 LYS N N 15 118.1590 0.07 . 1 . . . . 45 LYS N . 15945 1 127 . 1 1 35 35 ASP H H 1 8.3750 0.00425 . 1 . . . . 46 ASP HN . 15945 1 128 . 1 1 35 35 ASP CA C 13 55.1780 0.087 . 1 . . . . 46 ASP CA . 15945 1 129 . 1 1 35 35 ASP N N 15 120.8770 0.07 . 1 . . . . 46 ASP N . 15945 1 130 . 1 1 36 36 THR H H 1 6.9960 0.00425 . 1 . . . . 47 THR HN . 15945 1 131 . 1 1 36 36 THR HA H 1 5.0100 0.00425 . 1 . . . . 47 THR HA . 15945 1 132 . 1 1 36 36 THR HB H 1 3.9130 0.00425 . 1 . . . . 47 THR HB . 15945 1 133 . 1 1 36 36 THR CA C 13 60.6660 0.087 . 1 . . . . 47 THR CA . 15945 1 134 . 1 1 36 36 THR CB C 13 71.7840 0.087 . 1 . . . . 47 THR CB . 15945 1 135 . 1 1 36 36 THR N N 15 111.2880 0.07 . 1 . . . . 47 THR N . 15945 1 136 . 1 1 37 37 TYR H H 1 8.7630 0.00425 . 1 . . . . 48 TYR HN . 15945 1 137 . 1 1 37 37 TYR HA H 1 4.8230 0.00425 . 1 . . . . 48 TYR HA . 15945 1 138 . 1 1 37 37 TYR CA C 13 57.2970 0.087 . 1 . . . . 48 TYR CA . 15945 1 139 . 1 1 37 37 TYR CB C 13 45.6810 0.087 . 1 . . . . 48 TYR CB . 15945 1 140 . 1 1 37 37 TYR N N 15 120.0200 0.07 . 1 . . . . 48 TYR N . 15945 1 141 . 1 1 38 38 THR H H 1 9.0050 0.00425 . 1 . . . . 49 THR HN . 15945 1 142 . 1 1 38 38 THR HA H 1 5.3990 0.00425 . 1 . . . . 49 THR HA . 15945 1 143 . 1 1 38 38 THR CA C 13 61.0680 0.087 . 1 . . . . 49 THR CA . 15945 1 144 . 1 1 38 38 THR CB C 13 70.8700 0.087 . 1 . . . . 49 THR CB . 15945 1 145 . 1 1 38 38 THR N N 15 110.5870 0.07 . 1 . . . . 49 THR N . 15945 1 146 . 1 1 39 39 MET H H 1 8.2610 0.00425 . 1 . . . . 50 MET HN . 15945 1 147 . 1 1 39 39 MET CA C 13 57.5000 0.087 . 1 . . . . 50 MET CA . 15945 1 148 . 1 1 39 39 MET CB C 13 30.4630 0.087 . 1 . . . . 50 MET CB . 15945 1 149 . 1 1 39 39 MET N N 15 121.7140 0.07 . 1 . . . . 50 MET N . 15945 1 150 . 1 1 40 40 LYS H H 1 8.6180 0.00425 . 1 . . . . 51 LYS HN . 15945 1 151 . 1 1 40 40 LYS HA H 1 4.0160 0.00425 . 1 . . . . 51 LYS HA . 15945 1 152 . 1 1 40 40 LYS CA C 13 59.7380 0.087 . 1 . . . . 51 LYS CA . 15945 1 153 . 1 1 40 40 LYS CB C 13 32.7750 0.087 . 1 . . . . 51 LYS CB . 15945 1 154 . 1 1 40 40 LYS N N 15 117.7770 0.07 . 1 . . . . 51 LYS N . 15945 1 155 . 1 1 41 41 GLU H H 1 7.9570 0.00425 . 1 . . . . 52 GLU HN . 15945 1 156 . 1 1 41 41 GLU HA H 1 4.1270 0.00425 . 1 . . . . 52 GLU HA . 15945 1 157 . 1 1 41 41 GLU CA C 13 59.5420 0.087 . 1 . . . . 52 GLU CA . 15945 1 158 . 1 1 41 41 GLU CB C 13 31.7390 0.087 . 1 . . . . 52 GLU CB . 15945 1 159 . 1 1 41 41 GLU N N 15 120.5100 0.07 . 1 . . . . 52 GLU N . 15945 1 160 . 1 1 42 42 VAL H H 1 8.3100 0.00425 . 1 . . . . 53 VAL HN . 15945 1 161 . 1 1 42 42 VAL HA H 1 3.3420 0.00425 . 1 . . . . 53 VAL HA . 15945 1 162 . 1 1 42 42 VAL CA C 13 68.0980 0.087 . 1 . . . . 53 VAL CA . 15945 1 163 . 1 1 42 42 VAL CB C 13 30.5200 0.087 . 1 . . . . 53 VAL CB . 15945 1 164 . 1 1 42 42 VAL N N 15 119.6920 0.07 . 1 . . . . 53 VAL N . 15945 1 165 . 1 1 43 43 LEU H H 1 8.2930 0.00425 . 1 . . . . 54 LEU HN . 15945 1 166 . 1 1 43 43 LEU HA H 1 3.9720 0.00425 . 1 . . . . 54 LEU HA . 15945 1 167 . 1 1 43 43 LEU CA C 13 58.1040 0.087 . 1 . . . . 54 LEU CA . 15945 1 168 . 1 1 43 43 LEU CB C 13 40.8290 0.087 . 1 . . . . 54 LEU CB . 15945 1 169 . 1 1 43 43 LEU N N 15 118.8360 0.07 . 1 . . . . 54 LEU N . 15945 1 170 . 1 1 44 44 PHE H H 1 8.0610 0.00425 . 1 . . . . 55 PHE HN . 15945 1 171 . 1 1 44 44 PHE HA H 1 3.9040 0.00425 . 1 . . . . 55 PHE HA . 15945 1 172 . 1 1 44 44 PHE CA C 13 61.5350 0.087 . 1 . . . . 55 PHE CA . 15945 1 173 . 1 1 44 44 PHE CB C 13 38.4080 0.087 . 1 . . . . 55 PHE CB . 15945 1 174 . 1 1 44 44 PHE N N 15 121.8260 0.07 . 1 . . . . 55 PHE N . 15945 1 175 . 1 1 45 45 TYR H H 1 8.6110 0.00425 . 1 . . . . 56 TYR HN . 15945 1 176 . 1 1 45 45 TYR CA C 13 63.0010 0.087 . 1 . . . . 56 TYR CA . 15945 1 177 . 1 1 45 45 TYR CB C 13 38.8580 0.087 . 1 . . . . 56 TYR CB . 15945 1 178 . 1 1 45 45 TYR N N 15 120.1010 0.07 . 1 . . . . 56 TYR N . 15945 1 179 . 1 1 46 46 LEU H H 1 8.9270 0.00425 . 1 . . . . 57 LEU HN . 15945 1 180 . 1 1 46 46 LEU HA H 1 4.0010 0.00425 . 1 . . . . 57 LEU HA . 15945 1 181 . 1 1 46 46 LEU CA C 13 58.3290 0.087 . 1 . . . . 57 LEU CA . 15945 1 182 . 1 1 46 46 LEU CB C 13 41.8170 0.087 . 1 . . . . 57 LEU CB . 15945 1 183 . 1 1 46 46 LEU N N 15 121.1520 0.07 . 1 . . . . 57 LEU N . 15945 1 184 . 1 1 47 47 GLY H H 1 8.2530 0.00425 . 1 . . . . 58 GLY HN . 15945 1 185 . 1 1 47 47 GLY CA C 13 47.5570 0.087 . 1 . . . . 58 GLY CA . 15945 1 186 . 1 1 47 47 GLY N N 15 106.1730 0.07 . 1 . . . . 58 GLY N . 15945 1 187 . 1 1 48 48 GLN H H 1 7.7460 0.00425 . 1 . . . . 59 GLN HN . 15945 1 188 . 1 1 48 48 GLN CA C 13 59.1980 0.087 . 1 . . . . 59 GLN CA . 15945 1 189 . 1 1 48 48 GLN CB C 13 28.6150 0.087 . 1 . . . . 59 GLN CB . 15945 1 190 . 1 1 48 48 GLN N N 15 120.6310 0.07 . 1 . . . . 59 GLN N . 15945 1 191 . 1 1 49 49 TYR H H 1 8.7810 0.00425 . 1 . . . . 60 TYR HN . 15945 1 192 . 1 1 49 49 TYR HA H 1 3.9250 0.00425 . 1 . . . . 60 TYR HA . 15945 1 193 . 1 1 49 49 TYR CA C 13 62.8470 0.087 . 1 . . . . 60 TYR CA . 15945 1 194 . 1 1 49 49 TYR CB C 13 38.4840 0.087 . 1 . . . . 60 TYR CB . 15945 1 195 . 1 1 49 49 TYR N N 15 124.3580 0.07 . 1 . . . . 60 TYR N . 15945 1 196 . 1 1 50 50 ILE H H 1 8.4390 0.00425 . 1 . . . . 61 ILE HN . 15945 1 197 . 1 1 50 50 ILE CA C 13 66.1310 0.087 . 1 . . . . 61 ILE CA . 15945 1 198 . 1 1 50 50 ILE CB C 13 39.0330 0.087 . 1 . . . . 61 ILE CB . 15945 1 199 . 1 1 50 50 ILE N N 15 118.7020 0.07 . 1 . . . . 61 ILE N . 15945 1 200 . 1 1 51 51 MET H H 1 7.9020 0.00425 . 1 . . . . 62 MET HN . 15945 1 201 . 1 1 51 51 MET HA H 1 4.3000 0.00425 . 1 . . . . 62 MET HA . 15945 1 202 . 1 1 51 51 MET HB2 H 1 3.2190 0.00425 . 2 . . . . 62 MET HB1 . 15945 1 203 . 1 1 51 51 MET HB3 H 1 3.2190 0.00425 . 2 . . . . 62 MET HB2 . 15945 1 204 . 1 1 51 51 MET CA C 13 58.2790 0.087 . 1 . . . . 62 MET CA . 15945 1 205 . 1 1 51 51 MET CB C 13 31.9160 0.087 . 1 . . . . 62 MET CB . 15945 1 206 . 1 1 51 51 MET N N 15 115.6230 0.07 . 1 . . . . 62 MET N . 15945 1 207 . 1 1 52 52 THR H H 1 8.6020 0.00425 . 1 . . . . 63 THR HN . 15945 1 208 . 1 1 52 52 THR HA H 1 4.0240 0.00425 . 1 . . . . 63 THR HA . 15945 1 209 . 1 1 52 52 THR CA C 13 66.3750 0.087 . 1 . . . . 63 THR CA . 15945 1 210 . 1 1 52 52 THR CB C 13 69.0830 0.087 . 1 . . . . 63 THR CB . 15945 1 211 . 1 1 52 52 THR N N 15 116.4020 0.07 . 1 . . . . 63 THR N . 15945 1 212 . 1 1 53 53 LYS H H 1 4.1080 0.00425 . 1 . . . . 64 LYS HN . 15945 1 213 . 1 1 53 53 LYS CA C 13 55.6860 0.087 . 1 . . . . 64 LYS CA . 15945 1 214 . 1 1 53 53 LYS CB C 13 30.9720 0.087 . 1 . . . . 64 LYS CB . 15945 1 215 . 1 1 53 53 LYS N N 15 118.4860 0.07 . 1 . . . . 64 LYS N . 15945 1 216 . 1 1 54 54 ARG H H 1 7.6270 0.00425 . 1 . . . . 65 ARG HN . 15945 1 217 . 1 1 54 54 ARG HA H 1 3.8130 0.00425 . 1 . . . . 65 ARG HA . 15945 1 218 . 1 1 54 54 ARG CA C 13 56.8240 0.087 . 1 . . . . 65 ARG CA . 15945 1 219 . 1 1 54 54 ARG CB C 13 26.6320 0.087 . 1 . . . . 65 ARG CB . 15945 1 220 . 1 1 54 54 ARG N N 15 116.0430 0.07 . 1 . . . . 65 ARG N . 15945 1 221 . 1 1 55 55 LEU H H 1 7.6460 0.00425 . 1 . . . . 66 LEU HN . 15945 1 222 . 1 1 55 55 LEU HA H 1 4.4410 0.00425 . 1 . . . . 66 LEU HA . 15945 1 223 . 1 1 55 55 LEU CA C 13 54.8120 0.087 . 1 . . . . 66 LEU CA . 15945 1 224 . 1 1 55 55 LEU CB C 13 42.2060 0.087 . 1 . . . . 66 LEU CB . 15945 1 225 . 1 1 55 55 LEU N N 15 115.1580 0.07 . 1 . . . . 66 LEU N . 15945 1 226 . 1 1 56 56 TYR H H 1 6.8910 0.00425 . 1 . . . . 67 TYR HN . 15945 1 227 . 1 1 56 56 TYR HA H 1 5.0880 0.00425 . 1 . . . . 67 TYR HA . 15945 1 228 . 1 1 56 56 TYR CA C 13 55.2980 0.087 . 1 . . . . 67 TYR CA . 15945 1 229 . 1 1 56 56 TYR CB C 13 39.4060 0.087 . 1 . . . . 67 TYR CB . 15945 1 230 . 1 1 56 56 TYR N N 15 114.2860 0.07 . 1 . . . . 67 TYR N . 15945 1 231 . 1 1 57 57 ASP H H 1 8.6170 0.00425 . 1 . . . . 68 ASP HN . 15945 1 232 . 1 1 57 57 ASP CA C 13 54.1670 0.087 . 1 . . . . 68 ASP CA . 15945 1 233 . 1 1 57 57 ASP CB C 13 42.8470 0.087 . 1 . . . . 68 ASP CB . 15945 1 234 . 1 1 57 57 ASP N N 15 123.6520 0.07 . 1 . . . . 68 ASP N . 15945 1 235 . 1 1 58 58 GLU H H 1 8.6360 0.00425 . 1 . . . . 69 GLU HN . 15945 1 236 . 1 1 58 58 GLU HA H 1 3.9940 0.00425 . 1 . . . . 69 GLU HA . 15945 1 237 . 1 1 58 58 GLU CA C 13 59.1270 0.087 . 1 . . . . 69 GLU CA . 15945 1 238 . 1 1 58 58 GLU CB C 13 30.1480 0.087 . 1 . . . . 69 GLU CB . 15945 1 239 . 1 1 58 58 GLU N N 15 124.1810 0.07 . 1 . . . . 69 GLU N . 15945 1 240 . 1 1 59 59 LYS H H 1 8.2850 0.00425 . 1 . . . . 70 LYS HN . 15945 1 241 . 1 1 59 59 LYS HA H 1 4.3920 0.00425 . 1 . . . . 70 LYS HA . 15945 1 242 . 1 1 59 59 LYS HB2 H 1 1.9060 0.00425 . 2 . . . . 70 LYS HB1 . 15945 1 243 . 1 1 59 59 LYS HB3 H 1 1.9060 0.00425 . 2 . . . . 70 LYS HB2 . 15945 1 244 . 1 1 59 59 LYS CA C 13 57.1700 0.087 . 1 . . . . 70 LYS CA . 15945 1 245 . 1 1 59 59 LYS CB C 13 33.0740 0.087 . 1 . . . . 70 LYS CB . 15945 1 246 . 1 1 59 59 LYS N N 15 116.6370 0.07 . 1 . . . . 70 LYS N . 15945 1 247 . 1 1 60 60 GLN H H 1 8.3660 0.00425 . 1 . . . . 71 GLN HN . 15945 1 248 . 1 1 60 60 GLN HA H 1 4.6320 0.00425 . 1 . . . . 71 GLN HA . 15945 1 249 . 1 1 60 60 GLN HB2 H 1 1.8500 0.00425 . 2 . . . . 71 GLN HB1 . 15945 1 250 . 1 1 60 60 GLN HB3 H 1 1.8500 0.00425 . 2 . . . . 71 GLN HB2 . 15945 1 251 . 1 1 60 60 GLN CA C 13 54.3050 0.087 . 1 . . . . 71 GLN CA . 15945 1 252 . 1 1 60 60 GLN CB C 13 29.3710 0.087 . 1 . . . . 71 GLN CB . 15945 1 253 . 1 1 60 60 GLN N N 15 120.8770 0.07 . 1 . . . . 71 GLN N . 15945 1 254 . 1 1 61 61 GLN H H 1 8.2990 0.00425 . 1 . . . . 72 GLN HN . 15945 1 255 . 1 1 61 61 GLN HA H 1 4.2580 0.00425 . 1 . . . . 72 GLN HA . 15945 1 256 . 1 1 61 61 GLN CA C 13 58.8560 0.087 . 1 . . . . 72 GLN CA . 15945 1 257 . 1 1 61 61 GLN CB C 13 27.7050 0.087 . 1 . . . . 72 GLN CB . 15945 1 258 . 1 1 61 61 GLN N N 15 118.8360 0.07 . 1 . . . . 72 GLN N . 15945 1 259 . 1 1 62 62 HIS H H 1 7.8380 0.00425 . 1 . . . . 73 HIS HN . 15945 1 260 . 1 1 62 62 HIS CA C 13 56.0170 0.087 . 1 . . . . 73 HIS CA . 15945 1 261 . 1 1 62 62 HIS CB C 13 30.6850 0.087 . 1 . . . . 73 HIS CB . 15945 1 262 . 1 1 62 62 HIS N N 15 112.8170 0.07 . 1 . . . . 73 HIS N . 15945 1 263 . 1 1 63 63 ILE H H 1 7.6430 0.00425 . 1 . . . . 74 ILE HN . 15945 1 264 . 1 1 63 63 ILE HA H 1 4.1250 0.00425 . 1 . . . . 74 ILE HA . 15945 1 265 . 1 1 63 63 ILE CA C 13 59.8430 0.087 . 1 . . . . 74 ILE CA . 15945 1 266 . 1 1 63 63 ILE CB C 13 36.7430 0.087 . 1 . . . . 74 ILE CB . 15945 1 267 . 1 1 63 63 ILE N N 15 122.4810 0.07 . 1 . . . . 74 ILE N . 15945 1 268 . 1 1 64 64 VAL H H 1 8.3710 0.00425 . 1 . . . . 75 VAL HN . 15945 1 269 . 1 1 64 64 VAL HA H 1 3.8280 0.00425 . 1 . . . . 75 VAL HA . 15945 1 270 . 1 1 64 64 VAL CA C 13 60.7980 0.087 . 1 . . . . 75 VAL CA . 15945 1 271 . 1 1 64 64 VAL CB C 13 32.5070 0.087 . 1 . . . . 75 VAL CB . 15945 1 272 . 1 1 64 64 VAL N N 15 126.2080 0.07 . 1 . . . . 75 VAL N . 15945 1 273 . 1 1 65 65 TYR H H 1 8.3780 0.00425 . 1 . . . . 76 TYR HN . 15945 1 274 . 1 1 65 65 TYR CA C 13 58.4630 0.087 . 1 . . . . 76 TYR CA . 15945 1 275 . 1 1 65 65 TYR CB C 13 41.7690 0.087 . 1 . . . . 76 TYR CB . 15945 1 276 . 1 1 65 65 TYR N N 15 125.8160 0.07 . 1 . . . . 76 TYR N . 15945 1 277 . 1 1 66 66 CYS H H 1 8.4710 0.00425 . 1 . . . . 77 CYS HN . 15945 1 278 . 1 1 66 66 CYS CA C 13 55.9760 0.087 . 1 . . . . 77 CYS CA . 15945 1 279 . 1 1 66 66 CYS CB C 13 29.4820 0.087 . 1 . . . . 77 CYS CB . 15945 1 280 . 1 1 67 67 SER H H 1 7.7560 0.00425 . 1 . . . . 78 SER HN . 15945 1 281 . 1 1 67 67 SER CA C 13 60.3890 0.087 . 1 . . . . 78 SER CA . 15945 1 282 . 1 1 67 67 SER CB C 13 47.3620 0.087 . 1 . . . . 78 SER CB . 15945 1 283 . 1 1 67 67 SER N N 15 116.5510 0.07 . 1 . . . . 78 SER N . 15945 1 284 . 1 1 68 68 ASN H H 1 8.7580 0.00425 . 1 . . . . 79 ASN HN . 15945 1 285 . 1 1 68 68 ASN CA C 13 55.0580 0.087 . 1 . . . . 79 ASN CA . 15945 1 286 . 1 1 68 68 ASN CB C 13 37.9430 0.087 . 1 . . . . 79 ASN CB . 15945 1 287 . 1 1 68 68 ASN N N 15 118.1150 0.07 . 1 . . . . 79 ASN N . 15945 1 288 . 1 1 69 69 ASP H H 1 7.6920 0.00425 . 1 . . . . 80 ASP HN . 15945 1 289 . 1 1 69 69 ASP CA C 13 53.3520 0.087 . 1 . . . . 80 ASP CA . 15945 1 290 . 1 1 69 69 ASP N N 15 118.3520 0.07 . 1 . . . . 80 ASP N . 15945 1 291 . 1 1 70 70 LEU H H 1 9.8590 0.00425 . 1 . . . . 81 LEU HN . 15945 1 292 . 1 1 70 70 LEU CA C 13 58.2290 0.087 . 1 . . . . 81 LEU CA . 15945 1 293 . 1 1 70 70 LEU CB C 13 42.1530 0.087 . 1 . . . . 81 LEU CB . 15945 1 294 . 1 1 71 71 LEU H H 1 9.8680 0.00425 . 1 . . . . 82 LEU HN . 15945 1 295 . 1 1 71 71 LEU CA C 13 58.1690 0.087 . 1 . . . . 82 LEU CA . 15945 1 296 . 1 1 71 71 LEU CB C 13 42.6100 0.087 . 1 . . . . 82 LEU CB . 15945 1 297 . 1 1 71 71 LEU N N 15 118.5690 0.07 . 1 . . . . 82 LEU N . 15945 1 298 . 1 1 72 72 GLY H H 1 7.7760 0.00425 . 1 . . . . 83 GLY HN . 15945 1 299 . 1 1 72 72 GLY HA2 H 1 4.1160 0.00425 . 2 . . . . 83 GLY HA1 . 15945 1 300 . 1 1 72 72 GLY HA3 H 1 4.1160 0.00425 . 2 . . . . 83 GLY HA2 . 15945 1 301 . 1 1 72 72 GLY CA C 13 47.9710 0.087 . 1 . . . . 83 GLY CA . 15945 1 302 . 1 1 72 72 GLY N N 15 106.6110 0.07 . 1 . . . . 83 GLY N . 15945 1 303 . 1 1 73 73 ASP H H 1 7.5520 0.00425 . 1 . . . . 84 ASP HN . 15945 1 304 . 1 1 73 73 ASP HA H 1 4.4330 0.00425 . 1 . . . . 84 ASP HA . 15945 1 305 . 1 1 73 73 ASP HB2 H 1 2.9050 0.00425 . 2 . . . . 84 ASP HB1 . 15945 1 306 . 1 1 73 73 ASP HB3 H 1 2.9050 0.00425 . 2 . . . . 84 ASP HB2 . 15945 1 307 . 1 1 73 73 ASP CA C 13 56.9970 0.087 . 1 . . . . 84 ASP CA . 15945 1 308 . 1 1 73 73 ASP CB C 13 40.1860 0.087 . 1 . . . . 84 ASP CB . 15945 1 309 . 1 1 73 73 ASP N N 15 122.9790 0.07 . 1 . . . . 84 ASP N . 15945 1 310 . 1 1 74 74 LEU H H 1 8.0690 0.00425 . 1 . . . . 85 LEU HN . 15945 1 311 . 1 1 74 74 LEU HA H 1 4.1380 0.00425 . 1 . . . . 85 LEU HA . 15945 1 312 . 1 1 74 74 LEU CA C 13 57.2570 0.087 . 1 . . . . 85 LEU CA . 15945 1 313 . 1 1 74 74 LEU CB C 13 38.5680 0.087 . 1 . . . . 85 LEU CB . 15945 1 314 . 1 1 74 74 LEU N N 15 118.9220 0.07 . 1 . . . . 85 LEU N . 15945 1 315 . 1 1 75 75 PHE H H 1 8.4360 0.00425 . 1 . . . . 86 PHE HN . 15945 1 316 . 1 1 75 75 PHE CA C 13 56.0650 0.087 . 1 . . . . 86 PHE CA . 15945 1 317 . 1 1 75 75 PHE CB C 13 38.2720 0.087 . 1 . . . . 86 PHE CB . 15945 1 318 . 1 1 75 75 PHE N N 15 117.2560 0.07 . 1 . . . . 86 PHE N . 15945 1 319 . 1 1 76 76 GLY H H 1 8.3380 0.00425 . 1 . . . . 87 GLY HN . 15945 1 320 . 1 1 76 76 GLY HA2 H 1 3.9870 0.00425 . 2 . . . . 87 GLY HA1 . 15945 1 321 . 1 1 76 76 GLY HA3 H 1 3.9870 0.00425 . 2 . . . . 87 GLY HA2 . 15945 1 322 . 1 1 76 76 GLY CA C 13 46.5250 0.087 . 1 . . . . 87 GLY CA . 15945 1 323 . 1 1 76 76 GLY N N 15 108.3950 0.07 . 1 . . . . 87 GLY N . 15945 1 324 . 1 1 77 77 VAL H H 1 7.1310 0.00425 . 1 . . . . 88 VAL HN . 15945 1 325 . 1 1 77 77 VAL HA H 1 5.0090 0.00425 . 1 . . . . 88 VAL HA . 15945 1 326 . 1 1 77 77 VAL CA C 13 56.9990 0.087 . 1 . . . . 88 VAL CA . 15945 1 327 . 1 1 77 77 VAL N N 15 108.5000 0.07 . 1 . . . . 88 VAL N . 15945 1 328 . 1 1 78 78 PRO CA C 13 63.3300 0.087 . 1 . . . . 89 PRO CA . 15945 1 329 . 1 1 78 78 PRO CB C 13 32.1140 0.087 . 1 . . . . 89 PRO CB . 15945 1 330 . 1 1 79 79 SER H H 1 7.2630 0.00425 . 1 . . . . 90 SER HN . 15945 1 331 . 1 1 79 79 SER HA H 1 5.4810 0.00425 . 1 . . . . 90 SER HA . 15945 1 332 . 1 1 79 79 SER CA C 13 56.7170 0.087 . 1 . . . . 90 SER CA . 15945 1 333 . 1 1 79 79 SER CB C 13 64.9870 0.087 . 1 . . . . 90 SER CB . 15945 1 334 . 1 1 79 79 SER N N 15 111.3020 0.07 . 1 . . . . 90 SER N . 15945 1 335 . 1 1 80 80 PHE H H 1 8.2650 0.00425 . 1 . . . . 91 PHE HN . 15945 1 336 . 1 1 80 80 PHE CA C 13 56.7880 0.087 . 1 . . . . 91 PHE CA . 15945 1 337 . 1 1 80 80 PHE CB C 13 39.6600 0.087 . 1 . . . . 91 PHE CB . 15945 1 338 . 1 1 80 80 PHE N N 15 114.4660 0.07 . 1 . . . . 91 PHE N . 15945 1 339 . 1 1 81 81 SER H H 1 8.7780 0.00425 . 1 . . . . 92 SER HN . 15945 1 340 . 1 1 81 81 SER CA C 13 54.4560 0.087 . 1 . . . . 92 SER CA . 15945 1 341 . 1 1 81 81 SER CB C 13 63.9620 0.087 . 1 . . . . 92 SER CB . 15945 1 342 . 1 1 81 81 SER N N 15 112.7840 0.07 . 1 . . . . 92 SER N . 15945 1 343 . 1 1 82 82 VAL H H 1 9.3910 0.00425 . 1 . . . . 93 VAL HN . 15945 1 344 . 1 1 82 82 VAL HA H 1 4.3400 0.00425 . 1 . . . . 93 VAL HA . 15945 1 345 . 1 1 82 82 VAL CA C 13 63.6320 0.087 . 1 . . . . 93 VAL CA . 15945 1 346 . 1 1 82 82 VAL CB C 13 30.7900 0.087 . 1 . . . . 93 VAL CB . 15945 1 347 . 1 1 82 82 VAL N N 15 122.7960 0.07 . 1 . . . . 93 VAL N . 15945 1 348 . 1 1 83 83 LYS H H 1 8.0760 0.00425 . 1 . . . . 94 LYS HN . 15945 1 349 . 1 1 83 83 LYS HA H 1 4.2000 0.00425 . 1 . . . . 94 LYS HA . 15945 1 350 . 1 1 83 83 LYS CA C 13 56.8610 0.087 . 1 . . . . 94 LYS CA . 15945 1 351 . 1 1 83 83 LYS CB C 13 32.5850 0.087 . 1 . . . . 94 LYS CB . 15945 1 352 . 1 1 83 83 LYS N N 15 116.6400 0.07 . 1 . . . . 94 LYS N . 15945 1 353 . 1 1 84 84 GLU H H 1 7.4250 0.00425 . 1 . . . . 95 GLU HN . 15945 1 354 . 1 1 84 84 GLU HA H 1 4.6000 0.00425 . 1 . . . . 95 GLU HA . 15945 1 355 . 1 1 84 84 GLU CA C 13 54.6950 0.087 . 1 . . . . 95 GLU CA . 15945 1 356 . 1 1 84 84 GLU CB C 13 27.9050 0.087 . 1 . . . . 95 GLU CB . 15945 1 357 . 1 1 84 84 GLU N N 15 120.0340 0.07 . 1 . . . . 95 GLU N . 15945 1 358 . 1 1 85 85 HIS H H 1 7.6800 0.00425 . 1 . . . . 96 HIS HN . 15945 1 359 . 1 1 85 85 HIS CA C 13 59.9200 0.087 . 1 . . . . 96 HIS CA . 15945 1 360 . 1 1 85 85 HIS N N 15 120.7610 0.07 . 1 . . . . 96 HIS N . 15945 1 361 . 1 1 86 86 ARG CA C 13 58.5830 0.087 . 1 . . . . 97 ARG CA . 15945 1 362 . 1 1 86 86 ARG CB C 13 27.5590 0.087 . 1 . . . . 97 ARG CB . 15945 1 363 . 1 1 87 87 LYS H H 1 7.7230 0.00425 . 1 . . . . 98 LYS HN . 15945 1 364 . 1 1 87 87 LYS HA H 1 4.0320 0.00425 . 1 . . . . 98 LYS HA . 15945 1 365 . 1 1 87 87 LYS HE2 H 1 2.7860 0.00425 . 2 . . . . 98 LYS HE1 . 15945 1 366 . 1 1 87 87 LYS HE3 H 1 2.7860 0.00425 . 2 . . . . 98 LYS HE2 . 15945 1 367 . 1 1 87 87 LYS HG2 H 1 -0.2330 0.00425 . 2 . . . . 98 LYS HG1 . 15945 1 368 . 1 1 87 87 LYS HG3 H 1 -0.2330 0.00425 . 2 . . . . 98 LYS HG2 . 15945 1 369 . 1 1 87 87 LYS CA C 13 59.8750 0.087 . 1 . . . . 98 LYS CA . 15945 1 370 . 1 1 87 87 LYS CB C 13 32.3960 0.087 . 1 . . . . 98 LYS CB . 15945 1 371 . 1 1 87 87 LYS N N 15 120.6310 0.07 . 1 . . . . 98 LYS N . 15945 1 372 . 1 1 88 88 ILE H H 1 7.9260 0.00425 . 1 . . . . 99 ILE HN . 15945 1 373 . 1 1 88 88 ILE CA C 13 65.3590 0.087 . 1 . . . . 99 ILE CA . 15945 1 374 . 1 1 88 88 ILE CB C 13 37.5260 0.087 . 1 . . . . 99 ILE CB . 15945 1 375 . 1 1 88 88 ILE N N 15 118.9380 0.07 . 1 . . . . 99 ILE N . 15945 1 376 . 1 1 89 89 TYR H H 1 8.5540 0.00425 . 1 . . . . 100 TYR HN . 15945 1 377 . 1 1 89 89 TYR CA C 13 62.9100 0.087 . 1 . . . . 100 TYR CA . 15945 1 378 . 1 1 89 89 TYR CB C 13 37.2000 0.087 . 1 . . . . 100 TYR CB . 15945 1 379 . 1 1 89 89 TYR N N 15 121.1110 0.07 . 1 . . . . 100 TYR N . 15945 1 380 . 1 1 90 90 THR H H 1 8.1970 0.00425 . 1 . . . . 101 THR HN . 15945 1 381 . 1 1 90 90 THR CA C 13 67.3790 0.087 . 1 . . . . 101 THR CA . 15945 1 382 . 1 1 90 90 THR CB C 13 68.8080 0.087 . 1 . . . . 101 THR CB . 15945 1 383 . 1 1 90 90 THR N N 15 114.0790 0.07 . 1 . . . . 101 THR N . 15945 1 384 . 1 1 91 91 MET H H 1 7.6580 0.00425 . 1 . . . . 102 MET HN . 15945 1 385 . 1 1 91 91 MET CA C 13 59.7450 0.087 . 1 . . . . 102 MET CA . 15945 1 386 . 1 1 91 91 MET N N 15 119.9490 0.07 . 1 . . . . 102 MET N . 15945 1 387 . 1 1 92 92 ILE H H 1 8.2030 0.00425 . 1 . . . . 103 ILE HN . 15945 1 388 . 1 1 92 92 ILE CA C 13 66.0120 0.087 . 1 . . . . 103 ILE CA . 15945 1 389 . 1 1 92 92 ILE CB C 13 37.4200 0.087 . 1 . . . . 103 ILE CB . 15945 1 390 . 1 1 92 92 ILE N N 15 119.9770 0.07 . 1 . . . . 103 ILE N . 15945 1 391 . 1 1 93 93 TYR H H 1 8.8790 0.00425 . 1 . . . . 104 TYR HN . 15945 1 392 . 1 1 93 93 TYR CA C 13 61.3870 0.087 . 1 . . . . 104 TYR CA . 15945 1 393 . 1 1 93 93 TYR CB C 13 37.7290 0.087 . 1 . . . . 104 TYR CB . 15945 1 394 . 1 1 93 93 TYR N N 15 119.7260 0.07 . 1 . . . . 104 TYR N . 15945 1 395 . 1 1 94 94 ARG H H 1 7.1070 0.00425 . 1 . . . . 105 ARG HN . 15945 1 396 . 1 1 94 94 ARG N N 15 114.7490 0.07 . 1 . . . . 105 ARG N . 15945 1 397 . 1 1 96 96 LEU CA C 13 53.3270 0.087 . 1 . . . . 107 LEU CA . 15945 1 398 . 1 1 96 96 LEU CB C 13 47.0890 0.087 . 1 . . . . 107 LEU CB . 15945 1 399 . 1 1 97 97 VAL H H 1 8.6070 0.00425 . 1 . . . . 108 VAL HN . 15945 1 400 . 1 1 97 97 VAL CA C 13 58.1990 0.087 . 1 . . . . 108 VAL CA . 15945 1 401 . 1 1 97 97 VAL N N 15 128.3180 0.07 . 1 . . . . 108 VAL N . 15945 1 402 . 1 1 98 98 VAL H H 1 8.7600 0.00425 . 1 . . . . 109 VAL HN . 15945 1 403 . 1 1 98 98 VAL HA H 1 4.1110 0.00425 . 1 . . . . 109 VAL HA . 15945 1 404 . 1 1 98 98 VAL CA C 13 63.1770 0.087 . 1 . . . . 109 VAL CA . 15945 1 405 . 1 1 98 98 VAL CB C 13 32.4540 0.087 . 1 . . . . 109 VAL CB . 15945 1 406 . 1 1 98 98 VAL N N 15 127.7890 0.07 . 1 . . . . 109 VAL N . 15945 1 407 . 1 1 99 99 VAL H H 1 8.4310 0.00425 . 1 . . . . 110 VAL HN . 15945 1 408 . 1 1 99 99 VAL HA H 1 3.9820 0.00425 . 1 . . . . 110 VAL HA . 15945 1 409 . 1 1 99 99 VAL CA C 13 63.1060 0.087 . 1 . . . . 110 VAL CA . 15945 1 410 . 1 1 99 99 VAL CB C 13 32.3450 0.087 . 1 . . . . 110 VAL CB . 15945 1 411 . 1 1 99 99 VAL N N 15 127.0140 0.07 . 1 . . . . 110 VAL N . 15945 1 412 . 1 1 100 100 ASN H H 1 8.3050 0.00425 . 1 . . . . 111 ASN HN . 15945 1 413 . 1 1 100 100 ASN HB2 H 1 2.8210 0.00425 . 2 . . . . 111 ASN HB1 . 15945 1 414 . 1 1 100 100 ASN HB3 H 1 2.8210 0.00425 . 2 . . . . 111 ASN HB2 . 15945 1 415 . 1 1 100 100 ASN CA C 13 53.3300 0.087 . 1 . . . . 111 ASN CA . 15945 1 416 . 1 1 100 100 ASN CB C 13 40.0530 0.087 . 1 . . . . 111 ASN CB . 15945 1 417 . 1 1 100 100 ASN N N 15 122.4470 0.07 . 1 . . . . 111 ASN N . 15945 1 418 . 1 1 101 101 GLN H H 1 8.4870 0.00425 . 1 . . . . 112 GLN HN . 15945 1 419 . 1 1 101 101 GLN CA C 13 56.2040 0.087 . 1 . . . . 112 GLN CA . 15945 1 420 . 1 1 101 101 GLN CB C 13 29.6120 0.087 . 1 . . . . 112 GLN CB . 15945 1 421 . 1 1 101 101 GLN N N 15 121.6150 0.07 . 1 . . . . 112 GLN N . 15945 1 422 . 1 1 102 102 GLN H H 1 8.4600 0.00425 . 1 . . . . 113 GLN HN . 15945 1 423 . 1 1 102 102 GLN HA H 1 4.3230 0.00425 . 1 . . . . 113 GLN HA . 15945 1 424 . 1 1 102 102 GLN HB2 H 1 2.0480 0.00425 . 2 . . . . 113 GLN HB1 . 15945 1 425 . 1 1 102 102 GLN HB3 H 1 2.0480 0.00425 . 2 . . . . 113 GLN HB2 . 15945 1 426 . 1 1 102 102 GLN CA C 13 56.0210 0.087 . 1 . . . . 113 GLN CA . 15945 1 427 . 1 1 102 102 GLN CB C 13 29.5940 0.087 . 1 . . . . 113 GLN CB . 15945 1 428 . 1 1 102 102 GLN N N 15 121.2230 0.07 . 1 . . . . 113 GLN N . 15945 1 429 . 1 1 103 103 GLU H H 1 8.4510 0.00425 . 1 . . . . 114 GLU HN . 15945 1 430 . 1 1 103 103 GLU HA H 1 4.3330 0.00425 . 1 . . . . 114 GLU HA . 15945 1 431 . 1 1 103 103 GLU HB2 H 1 2.3510 0.00425 . 2 . . . . 114 GLU HB1 . 15945 1 432 . 1 1 103 103 GLU HB3 H 1 2.0270 0.00425 . 2 . . . . 114 GLU HB2 . 15945 1 433 . 1 1 103 103 GLU CA C 13 56.5400 0.087 . 1 . . . . 114 GLU CA . 15945 1 434 . 1 1 103 103 GLU CB C 13 30.1020 0.087 . 1 . . . . 114 GLU CB . 15945 1 435 . 1 1 103 103 GLU N N 15 122.1270 0.07 . 1 . . . . 114 GLU N . 15945 1 436 . 1 1 104 104 SER H H 1 8.0980 0.00425 . 1 . . . . 115 SER HN . 15945 1 437 . 1 1 104 104 SER HA H 1 4.5140 0.00425 . 1 . . . . 115 SER HA . 15945 1 438 . 1 1 104 104 SER HB2 H 1 3.8960 0.00425 . 2 . . . . 115 SER HB1 . 15945 1 439 . 1 1 104 104 SER HB3 H 1 3.8960 0.00425 . 2 . . . . 115 SER HB2 . 15945 1 440 . 1 1 104 104 SER CA C 13 58.2800 0.087 . 1 . . . . 115 SER CA . 15945 1 441 . 1 1 104 104 SER CB C 13 63.8670 0.087 . 1 . . . . 115 SER CB . 15945 1 442 . 1 1 104 104 SER N N 15 116.8540 0.07 . 1 . . . . 115 SER N . 15945 1 443 . 1 1 105 105 SER H H 1 8.4890 0.00425 . 1 . . . . 116 SER HN . 15945 1 444 . 1 1 105 105 SER CA C 13 58.4630 0.087 . 1 . . . . 116 SER CA . 15945 1 445 . 1 1 105 105 SER CB C 13 63.8270 0.087 . 1 . . . . 116 SER CB . 15945 1 446 . 1 1 105 105 SER N N 15 118.0520 0.07 . 1 . . . . 116 SER N . 15945 1 447 . 1 1 106 106 ASP H H 1 8.4110 0.00425 . 1 . . . . 117 ASP HN . 15945 1 448 . 1 1 106 106 ASP HA H 1 4.5620 0.00425 . 1 . . . . 117 ASP HA . 15945 1 449 . 1 1 106 106 ASP HB2 H 1 2.7000 0.00425 . 2 . . . . 117 ASP HB1 . 15945 1 450 . 1 1 106 106 ASP HB3 H 1 2.7000 0.00425 . 2 . . . . 117 ASP HB2 . 15945 1 451 . 1 1 106 106 ASP CA C 13 54.5810 0.087 . 1 . . . . 117 ASP CA . 15945 1 452 . 1 1 106 106 ASP CB C 13 40.4890 0.087 . 1 . . . . 117 ASP CB . 15945 1 453 . 1 1 106 106 ASP N N 15 122.4130 0.07 . 1 . . . . 117 ASP N . 15945 1 454 . 1 1 107 107 SER H H 1 7.5380 0.00425 . 1 . . . . 118 SER HN . 15945 1 455 . 1 1 107 107 SER HA H 1 6.8530 0.00425 . 1 . . . . 118 SER HA . 15945 1 456 . 1 1 107 107 SER CA C 13 58.8960 0.087 . 1 . . . . 118 SER CA . 15945 1 457 . 1 1 107 107 SER CB C 13 63.7360 0.087 . 1 . . . . 118 SER CB . 15945 1 458 . 1 1 108 108 GLY H H 1 8.5150 0.00425 . 1 . . . . 119 GLY HN . 15945 1 459 . 1 1 108 108 GLY HA2 H 1 4.0220 0.00425 . 2 . . . . 119 GLY HA1 . 15945 1 460 . 1 1 108 108 GLY HA3 H 1 4.0220 0.00425 . 2 . . . . 119 GLY HA2 . 15945 1 461 . 1 1 108 108 GLY CA C 13 45.5360 0.087 . 1 . . . . 119 GLY CA . 15945 1 462 . 1 1 108 108 GLY N N 15 110.8950 0.07 . 1 . . . . 119 GLY N . 15945 1 463 . 1 1 109 109 THR H H 1 8.0790 0.00425 . 1 . . . . 120 THR HN . 15945 1 464 . 1 1 109 109 THR HA H 1 4.4180 0.00425 . 1 . . . . 120 THR HA . 15945 1 465 . 1 1 109 109 THR CA C 13 61.7920 0.087 . 1 . . . . 120 THR CA . 15945 1 466 . 1 1 109 109 THR CB C 13 69.8600 0.087 . 1 . . . . 120 THR CB . 15945 1 467 . 1 1 109 109 THR N N 15 113.5210 0.07 . 1 . . . . 120 THR N . 15945 1 468 . 1 1 110 110 SER H H 1 8.3370 0.00425 . 1 . . . . 121 SER HN . 15945 1 469 . 1 1 110 110 SER HA H 1 4.3710 0.00425 . 1 . . . . 121 SER HA . 15945 1 470 . 1 1 110 110 SER HB2 H 1 3.9690 0.00425 . 2 . . . . 121 SER HB1 . 15945 1 471 . 1 1 110 110 SER HB3 H 1 3.9690 0.00425 . 2 . . . . 121 SER HB2 . 15945 1 472 . 1 1 110 110 SER CA C 13 58.3520 0.087 . 1 . . . . 121 SER CA . 15945 1 473 . 1 1 110 110 SER CB C 13 63.7710 0.087 . 1 . . . . 121 SER CB . 15945 1 474 . 1 1 110 110 SER N N 15 118.7020 0.07 . 1 . . . . 121 SER N . 15945 1 475 . 1 1 111 111 VAL H H 1 8.2610 0.00425 . 1 . . . . 122 VAL HN . 15945 1 476 . 1 1 111 111 VAL CA C 13 62.2050 0.087 . 1 . . . . 122 VAL CA . 15945 1 477 . 1 1 111 111 VAL CB C 13 32.7580 0.087 . 1 . . . . 122 VAL CB . 15945 1 478 . 1 1 111 111 VAL N N 15 121.7140 0.07 . 1 . . . . 122 VAL N . 15945 1 479 . 1 1 112 112 SER H H 1 8.3640 0.00425 . 1 . . . . 123 SER HN . 15945 1 480 . 1 1 112 112 SER HA H 1 4.4970 0.00425 . 1 . . . . 123 SER HA . 15945 1 481 . 1 1 112 112 SER HB2 H 1 3.8660 0.00425 . 2 . . . . 123 SER HB1 . 15945 1 482 . 1 1 112 112 SER HB3 H 1 3.8660 0.00425 . 2 . . . . 123 SER HB2 . 15945 1 483 . 1 1 112 112 SER CA C 13 58.1700 0.087 . 1 . . . . 123 SER CA . 15945 1 484 . 1 1 112 112 SER CB C 13 63.9060 0.087 . 1 . . . . 123 SER CB . 15945 1 485 . 1 1 112 112 SER N N 15 119.5170 0.07 . 1 . . . . 123 SER N . 15945 1 486 . 1 1 113 113 GLU H H 1 8.4890 0.00425 . 1 . . . . 124 GLU HN . 15945 1 487 . 1 1 113 113 GLU HA H 1 4.3260 0.00425 . 1 . . . . 124 GLU HA . 15945 1 488 . 1 1 113 113 GLU HB2 H 1 2.2210 0.00425 . 2 . . . . 124 GLU HB1 . 15945 1 489 . 1 1 113 113 GLU HB3 H 1 1.9400 0.00425 . 2 . . . . 124 GLU HB2 . 15945 1 490 . 1 1 113 113 GLU CA C 13 56.6410 0.087 . 1 . . . . 124 GLU CA . 15945 1 491 . 1 1 113 113 GLU CB C 13 30.5730 0.087 . 1 . . . . 124 GLU CB . 15945 1 492 . 1 1 113 113 GLU N N 15 123.4980 0.07 . 1 . . . . 124 GLU N . 15945 1 493 . 1 1 114 114 ASN H H 1 8.0600 0.00425 . 1 . . . . 125 ASN HN . 15945 1 494 . 1 1 114 114 ASN HB2 H 1 2.7280 0.00425 . 2 . . . . 125 ASN HB1 . 15945 1 495 . 1 1 114 114 ASN HB3 H 1 2.7280 0.00425 . 2 . . . . 125 ASN HB2 . 15945 1 496 . 1 1 114 114 ASN CA C 13 56.4310 0.087 . 1 . . . . 125 ASN CA . 15945 1 497 . 1 1 114 114 ASN N N 15 124.4550 0.07 . 1 . . . . 125 ASN N . 15945 1 stop_ save_