data_7003 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 7003 _Entry.Title ; NMR backbone assignment of the human HSP90 N-terminal domain ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2006-02-23 _Entry.Accession_date 2006-02-23 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _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 Harald Schwalbe . . . 7003 2 Doris Jacobs . M. . 7003 3 Bettina Elshorst . . . 7003 4 Krishna Saxena . . . 7003 5 Klaus Fiebig . M. . 7003 6 Martin Vogtherr . . . 7003 7 Thomas Langer . . . 7003 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID . . 'BMRZ, Frankfurt, Germany' . 7003 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 7003 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 558 7003 '15N chemical shifts' 168 7003 '1H chemical shifts' 168 7003 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 . . 2007-02-08 2006-02-23 update BMRB 'complete entry citation' 7003 1 . . 2006-08-07 2006-02-23 original author 'original release' 7003 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 7003 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 16821127 _Citation.Full_citation . _Citation.Title 'NMR Backbone Assignment of the N-terminal Domain of Human HSP90' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 36 _Citation.Journal_issue 'Suppl. 5' _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 52 _Citation.Page_last 52 _Citation.Year 2006 _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 Doris Jacobs . M. . 7003 1 2 Thomas Langer . . . 7003 1 3 Bettina Elshorst . . . 7003 1 4 Krishna Saxena . . . 7003 1 5 Klaus Fiebig . M. . 7003 1 6 Martin Vogtherr . . . 7003 1 7 Harald Schwalbe . . . 7003 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 7003 _Assembly.ID 1 _Assembly.Name hsp90 _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 0 _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states no _Assembly.Ambiguous_chem_comp_sites no _Assembly.Molecules_in_chemical_exchange no _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details 'human heat shock protein 90 N-terminal domain' _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 'human heat shock protein 90 N-terminal domain' 1 $hsp90 . . yes native no no . . . 7003 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_hsp90 _Entity.Sf_category entity _Entity.Sf_framecode hsp90 _Entity.Entry_ID 7003 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name hsp90 _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 ; GHVETFAFQAEIAQLMSLII NTFYSNKEIFLRELISNSSD ALDKIRYETLTDPSKLDSGK ELHINLIPNKQDRTLTIVDT GIGMTKADLINNLGTIAKSG TKAFMEALQAGADISMIGQF GVGFYSAYLVAEKVTVITKH NDDEQYAWESSAGGSFTVRT DTGEPMGRGTKVILHLKEDQ TEYLEERRIKEIVKKHSQFI GYPITLFVE ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 209 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 19560 . Hsp90_N_domain . . . . . 100.00 221 100.00 100.00 2.49e-150 . . . . 7003 1 2 no PDB 1BYQ . "Hsp90 N-Terminal Domain Bound To Adp-Mg" . . . . . 99.52 228 99.52 99.52 2.04e-148 . . . . 7003 1 3 no PDB 1OSF . "Human Hsp90 In Complex With 17-desmethoxy-17-n,n- Dimethylaminoethylamino-geldanamycin" . . . . . 99.04 215 99.52 100.00 9.30e-148 . . . . 7003 1 4 no PDB 1UY6 . "Human Hsp90-Alpha With 9-Butyl-8-(3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 5 no PDB 1UY7 . "Human Hsp90-alpha With 9-butyl-8-(4-methoxy-benzyl)-9h-purin-6-ylamine" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 6 no PDB 1UY8 . "Human Hsp90-Alpha With 9-Butyl-8-(3-Trimethoxy-Benzyl)-9h-Purin-6ylamine" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 7 no PDB 1UY9 . "Human Hsp90-Alpha With 8-Benzo[1,3]dioxol-,5-Ylmethyl-9-Butyl-9h-Purin-6-Ylamine" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 8 no PDB 1UYC . "Human Hsp90-Alpha With 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-9h-Purin-6-Ylamine" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 9 no PDB 1UYD . "Human Hsp90-Alpha With 9-Butyl-8- (2-Chloro-3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 10 no PDB 1UYE . "Human Hsp90-Alpha With 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl) -9-Pent-4-Ylnyl-9h-Purin-6-Ylamine" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 11 no PDB 1UYF . "Human Hsp90-Alpha With 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl) -2-Fluoro-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 12 no PDB 1UYG . "Human Hsp90-Alpha With 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 13 no PDB 1UYH . "Human Hsp90-Alpha With 9-Butyl-8- (2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 14 no PDB 1UYI . "Human Hsp90-Alpha With 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9- Pent-9h-Purin-6-Ylamine" . . . . . 99.52 236 99.52 100.00 3.87e-149 . . . . 7003 1 15 no PDB 1UYK . "Human Hsp90-Alpha With 8-Benzo[1,3]dioxol-,5-Ylmethyl-9-But Yl-2-Fluoro-9h-Purin-6-Ylamine" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 16 no PDB 1UYL . "Structure-Activity Relationships In Purine-Based Inhibitor Binding To Hsp90 Isoforms" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 17 no PDB 1YC1 . "Crystal Structures Of Human Hsp90alpha Complexed With Dihydroxyphenylpyrazoles" . . . . . 99.04 264 100.00 100.00 3.68e-147 . . . . 7003 1 18 no PDB 1YC3 . "Crystal Structure Of Human Hsp90alpha Complexed With Dihydroxyphenylpyrazoles" . . . . . 99.04 264 100.00 100.00 3.68e-147 . . . . 7003 1 19 no PDB 1YC4 . "Crystal Structure Of Human Hsp90alpha Complexed With Dihydroxyphenylpyrazoles" . . . . . 99.04 264 100.00 100.00 3.68e-147 . . . . 7003 1 20 no PDB 1YER . 'Human Hsp90 Geldanamycin-Binding Domain, "closed" Conformation' . . . . . 99.52 228 99.52 99.52 2.04e-148 . . . . 7003 1 21 no PDB 1YES . 'Human Hsp90 Geldanamycin-Binding Domain, "open" Conformation' . . . . . 99.52 228 99.52 99.52 2.04e-148 . . . . 7003 1 22 no PDB 1YET . "Geldanamycin Bound To The Hsp90 Geldanamycin-Binding Domain" . . . . . 99.52 228 99.52 99.52 2.04e-148 . . . . 7003 1 23 no PDB 2BSM . "Novel, Potent Small Molecule Inhibitors Of The Molecular Chaperone Hsp90 Discovered Through Structure-Based Design" . . . . . 99.52 235 99.04 99.52 7.63e-148 . . . . 7003 1 24 no PDB 2BT0 . "Novel, Potent Small Molecule Inhibitors Of The Molecular Chaperone Hsp90 Discovered Through Structure-Based Design" . . . . . 99.52 235 99.04 99.52 7.63e-148 . . . . 7003 1 25 no PDB 2BYH . "3-(5-Chloro-2,4-Dihydroxyphenyl)-Pyrazole-4-Carboxamides As Inhibitors Of The Hsp90 Molecular Chaperone" . . . . . 99.52 235 99.04 99.52 7.63e-148 . . . . 7003 1 26 no PDB 2BYI . "3-(5-Chloro-2,4-Dihydroxyphenyl)-Pyrazole-4-Carboxamides As Inhibitors Of The Hsp90 Molecular Chaperone" . . . . . 99.52 235 99.04 99.52 7.63e-148 . . . . 7003 1 27 no PDB 2BZ5 . "Structure-Based Discovery Of A New Class Of Hsp90 Inhibitors" . . . . . 99.52 235 99.04 99.52 7.63e-148 . . . . 7003 1 28 no PDB 2CCS . "Human Hsp90 With 4-Chloro-6-(4-Piperazin-1-Yl-1h-Pyrazol-3- Yl)-Benzene-1,2-Diol" . . . . . 99.52 236 99.52 99.52 1.55e-148 . . . . 7003 1 29 no PDB 2CCT . "Human Hsp90 With 5-(5-Chloro-2,4-Dihydroxy-Phenyl)-4- Piperazin-1-Yl-2h-Pyrazole-3-Carboxylic Acid Ethylamide" . . . . . 99.52 236 99.52 99.52 1.55e-148 . . . . 7003 1 30 no PDB 2CCU . "Human Hsp90 With 4-Chloro-6-(4-(4-(4-Methanesulphonyl- Benzyl)-Pierazin-1-Yl)-1h-Pyrazol-3-Yl)-Benzene-1,3-Diol" . . . . . 99.52 236 99.52 99.52 1.55e-148 . . . . 7003 1 31 no PDB 2FWY . "Structure Of Human Hsp90-Alpha Bound To The Potent Water Soluble Inhibitor Pu-H64" . . . . . 99.04 256 99.52 100.00 2.04e-147 . . . . 7003 1 32 no PDB 2FWZ . "Structure Of Human Hsp90-alpha Bound To The Potent Water Soluble Inhibitor Pu-h71" . . . . . 99.04 256 99.52 100.00 2.04e-147 . . . . 7003 1 33 no PDB 2H55 . "Structure Of Human Hsp90-Alpha Bound To The Potent Water Soluble Inhibitor Pu-Dz8" . . . . . 99.04 256 99.52 100.00 2.04e-147 . . . . 7003 1 34 no PDB 2JJC . "Hsp90 Alpha Atpase Domain With Bound Small Molecule Fragment" . . . . . 99.04 218 99.52 100.00 1.23e-147 . . . . 7003 1 35 no PDB 2K5B . "Human Cdc37-Hsp90 Docking Model Based On Nmr" . . . . . 99.04 210 100.00 100.00 2.10e-148 . . . . 7003 1 36 no PDB 2QF6 . "Hsp90 Complexed With A56322" . . . . . 99.04 207 100.00 100.00 2.79e-148 . . . . 7003 1 37 no PDB 2QFO . "Hsp90 Complexed With A143571 And A516383" . . . . . 99.04 207 99.52 100.00 7.81e-148 . . . . 7003 1 38 no PDB 2QG0 . "Hsp90 Complexed With A943037" . . . . . 99.04 207 99.52 100.00 7.81e-148 . . . . 7003 1 39 no PDB 2QG2 . "Hsp90 Complexed With A917985" . . . . . 99.04 207 100.00 100.00 2.79e-148 . . . . 7003 1 40 no PDB 2UWD . "Inhibition Of The Hsp90 Molecular Chaperone In Vitro And In Vivo By Novel, Synthetic, Potent Resorcinylic Pyrazole, Isoxazole A" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 41 no PDB 2VCI . "4,5 Diaryl Isoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents For The Treatment Of Cancer" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 42 no PDB 2VCJ . "4,5 Diaryl Isoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents For The Treatment Of Cancer" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 43 no PDB 2WI1 . "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 44 no PDB 2WI2 . "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 45 no PDB 2WI3 . "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 46 no PDB 2WI4 . "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 47 no PDB 2WI5 . "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 48 no PDB 2WI6 . "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 49 no PDB 2WI7 . "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 50 no PDB 2XAB . "Structure Of Hsp90 With An Inhibitor Bound" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 51 no PDB 2XDK . "Structure Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 52 no PDB 2XDL . "Structure Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 53 no PDB 2XDS . "Structure Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 54 no PDB 2XDU . "Structure Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 236 99.52 100.00 1.70e-147 . . . . 7003 1 55 no PDB 2XDX . "Structre Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 56 no PDB 2XHR . "Structure Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 57 no PDB 2XHT . "Structure Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 58 no PDB 2XHX . "Structure Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 249 100.00 100.00 8.46e-148 . . . . 7003 1 59 no PDB 2XJG . "Structure Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 249 100.00 100.00 8.46e-148 . . . . 7003 1 60 no PDB 2XJJ . "Structure Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 249 99.03 99.52 3.72e-146 . . . . 7003 1 61 no PDB 2XJX . "Structure Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 62 no PDB 2XK2 . "Structure Of Hsp90 With Small Molecule Inhibitor Bound" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 63 no PDB 2YE2 . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 64 no PDB 2YE3 . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 65 no PDB 2YE4 . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 66 no PDB 2YE5 . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 67 no PDB 2YE6 . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 68 no PDB 2YE7 . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.52 252 99.52 100.00 1.01e-148 . . . . 7003 1 69 no PDB 2YE8 . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.52 252 99.52 100.00 1.01e-148 . . . . 7003 1 70 no PDB 2YE9 . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 71 no PDB 2YEA . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 72 no PDB 2YEB . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 73 no PDB 2YEC . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 74 no PDB 2YED . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 75 no PDB 2YEE . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.52 252 99.04 99.52 1.54e-147 . . . . 7003 1 76 no PDB 2YEF . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 77 no PDB 2YEG . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 78 no PDB 2YEH . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.04 252 99.52 100.00 1.31e-147 . . . . 7003 1 79 no PDB 2YEI . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.52 252 99.52 100.00 1.01e-148 . . . . 7003 1 80 no PDB 2YEJ . "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" . . . . . 99.52 252 99.52 100.00 1.01e-148 . . . . 7003 1 81 no PDB 2YI0 . "Structural Characterization Of 5-Aryl-4-(5-Substituted-2-4- Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors." . . . . . 99.04 229 99.52 100.00 8.29e-148 . . . . 7003 1 82 no PDB 2YI5 . "Structural Characterization Of 5-Aryl-4-(5-Substituted-2-4- Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors." . . . . . 99.04 229 99.52 100.00 8.29e-148 . . . . 7003 1 83 no PDB 2YI6 . "Structural Characterization Of 5-Aryl-4-(5-Substituted-2- 4-Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors." . . . . . 99.04 229 99.52 100.00 8.29e-148 . . . . 7003 1 84 no PDB 2YI7 . "Structural Characterization Of 5-Aryl-4-(5-Substituted-2-4- Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors" . . . . . 99.04 229 99.52 100.00 8.29e-148 . . . . 7003 1 85 no PDB 2YJW . "Tricyclic Series Of Hsp90 Inhibitors" . . . . . 100.00 209 99.04 100.00 3.97e-149 . . . . 7003 1 86 no PDB 2YJX . "Tricyclic Series Of Hsp90 Inhibitors" . . . . . 100.00 209 99.04 100.00 3.97e-149 . . . . 7003 1 87 no PDB 2YK2 . "Tricyclic Series Of Hsp90 Inhibitors" . . . . . 100.00 209 99.04 100.00 3.97e-149 . . . . 7003 1 88 no PDB 2YK9 . "Tricyclic Series Of Hsp90 Inhibitors" . . . . . 100.00 209 99.04 100.00 3.97e-149 . . . . 7003 1 89 no PDB 2YKB . "Tricyclic Series Of Hsp90 Inhibitors" . . . . . 100.00 209 99.04 100.00 3.97e-149 . . . . 7003 1 90 no PDB 2YKC . "Tricyclic Series Of Hsp90 Inhibitors" . . . . . 100.00 209 99.04 100.00 3.97e-149 . . . . 7003 1 91 no PDB 2YKE . "Tricyclic Series Of Hsp90 Inhibitors" . . . . . 100.00 209 99.04 100.00 3.97e-149 . . . . 7003 1 92 no PDB 2YKI . "Tricyclic Series Of Hsp90 Inhibitors" . . . . . 100.00 209 99.04 100.00 3.97e-149 . . . . 7003 1 93 no PDB 2YKJ . "Tricyclic Series Of Hsp90 Inhibitors" . . . . . 100.00 209 99.04 100.00 3.97e-149 . . . . 7003 1 94 no PDB 3B24 . "Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazine Fragment Molecule" . . . . . 99.52 229 99.04 99.52 6.45e-148 . . . . 7003 1 95 no PDB 3B25 . "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ch4675194" . . . . . 99.52 229 99.04 99.52 6.45e-148 . . . . 7003 1 96 no PDB 3B26 . "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ro1127850" . . . . . 99.52 229 99.04 99.52 6.45e-148 . . . . 7003 1 97 no PDB 3B27 . "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ro4919127" . . . . . 99.52 229 99.04 99.52 6.45e-148 . . . . 7003 1 98 no PDB 3B28 . "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ch5015765" . . . . . 99.52 229 99.04 99.52 6.45e-148 . . . . 7003 1 99 no PDB 3BM9 . "Discovery Of Benzisoxazoles As Potent Inhibitors Of Chaperone Hsp90" . . . . . 99.04 226 99.52 100.00 8.05e-148 . . . . 7003 1 100 no PDB 3BMY . "Discovery Of Benzisoxazoles As Potent Inhibitors Of Chaperone Hsp90" . . . . . 99.04 226 99.52 100.00 8.05e-148 . . . . 7003 1 101 no PDB 3D0B . "Crystal Structure Of Benzamide Tetrahydro-4h-Carbazol-4-One Bound To Hsp90" . . . . . 99.52 232 99.04 99.52 8.36e-148 . . . . 7003 1 102 no PDB 3EKO . "Dihydroxylphenyl Amides As Inhibitors Of The Hsp90 Molecular Chaperone" . . . . . 99.04 226 99.52 100.00 1.53e-147 . . . . 7003 1 103 no PDB 3EKR . "Dihydroxylphenyl Amides As Inhibitors Of The Hsp90 Molecular Chaperone" . . . . . 99.04 226 99.52 100.00 1.53e-147 . . . . 7003 1 104 no PDB 3FT5 . "Structure Of Hsp90 Bound With A Novel Fragment" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 105 no PDB 3FT8 . "Structure Of Hsp90 Bound With A Noval Fragment." . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 106 no PDB 3HEK . "Hsp90 N-Terminal Domain In Complex With 1-{4-[(2r)-1-(5- Chloro-2,4-Dihydroxybenzoyl)pyrrolidin-2-Yl]benzyl}-3,3- Difluoropyrro" . . . . . 99.04 226 99.52 100.00 1.53e-147 . . . . 7003 1 107 no PDB 3HHU . "Human Heat-Shock Protein 90 (Hsp90) In Complex With {4-[3- (2,4-Dihydroxy-5-Isopropyl-Phenyl)-5-Thioxo- 1,5-Dihydro- [1,2,4]tri" . . . . . 99.04 224 99.52 100.00 9.64e-148 . . . . 7003 1 108 no PDB 3HYY . "Crystal Structure Of Hsp90 With Fragment 37-D04" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 109 no PDB 3HYZ . "Crystal Structure Of Hsp90 With Fragment 42-C03" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 110 no PDB 3HZ1 . "Crystal Structure Of Hsp90 With Fragments 37-D04 And 42-C03" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 111 no PDB 3HZ5 . "Crystal Structure Of Hsp90 With Fragment Z064" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 112 no PDB 3INW . "Hsp90 N-Terminal Domain With Pochoxime A" . . . . . 99.52 228 99.04 99.52 6.29e-148 . . . . 7003 1 113 no PDB 3INX . "Hsp90 N-Terminal Domain With Pochoxime B" . . . . . 99.52 228 99.04 99.52 6.29e-148 . . . . 7003 1 114 no PDB 3K97 . "Hsp90 N-Terminal Domain In Complex With 4-Chloro-6-{[(2r)-2- (2-Methylphenyl)pyrrolidin-1-Yl]carbonyl}benzene-1,3-Diol" . . . . . 99.04 251 99.52 100.00 5.95e-147 . . . . 7003 1 115 no PDB 3K98 . "Hsp90 N-Terminal Domain In Complex With (1r)-2-(5-Chloro-2, 4-Dihydroxybenzoyl)-N-Ethylisoindoline-1-Carboxamide" . . . . . 99.04 232 99.52 100.00 1.10e-147 . . . . 7003 1 116 no PDB 3K99 . "Hsp90 N-Terminal Domain In Complex With 4-(1,3-Dihydro-2h- Isoindol-2-Ylcarbonyl)benzene-1,3-Diol" . . . . . 99.04 232 99.52 100.00 1.10e-147 . . . . 7003 1 117 no PDB 3MNR . "Crystal Structure Of Benzamide Snx-1321 Bound To Hsp90" . . . . . 99.52 232 99.04 99.52 8.36e-148 . . . . 7003 1 118 no PDB 3O0I . "Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Pu-h54" . . . . . 99.04 256 99.52 100.00 2.04e-147 . . . . 7003 1 119 no PDB 3OW6 . "Crystal Structure Of Hsp90 With N-Aryl-Benzimidazolone I" . . . . . 99.04 207 100.00 100.00 2.79e-148 . . . . 7003 1 120 no PDB 3OWB . "Crystal Structure Of Hsp90 With Ver-49009" . . . . . 99.04 207 100.00 100.00 2.79e-148 . . . . 7003 1 121 no PDB 3OWD . "Crystal Structure Of Hsp90 With N-Aryl-Benzimidazolone Ii" . . . . . 99.04 207 100.00 100.00 2.79e-148 . . . . 7003 1 122 no PDB 3QDD . "Hsp90a N-Terminal Domain In Complex With Biib021" . . . . . 99.04 237 99.52 100.00 7.76e-148 . . . . 7003 1 123 no PDB 3QTF . "Design And Sar Of Macrocyclic Hsp90 Inhibitors With Increased Metabolic Stability And Potent Cell-Proliferation Activity" . . . . . 99.04 226 99.52 100.00 8.05e-148 . . . . 7003 1 124 no PDB 3R4M . "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 125 no PDB 3R4N . "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" . . . . . 99.04 226 99.52 100.00 1.53e-147 . . . . 7003 1 126 no PDB 3R4O . "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" . . . . . 99.04 226 99.52 100.00 1.53e-147 . . . . 7003 1 127 no PDB 3R4P . "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" . . . . . 99.04 226 99.52 100.00 1.53e-147 . . . . 7003 1 128 no PDB 3R91 . "Macrocyclic Lactams As Potent Hsp90 Inhibitors With Excellent Tumor Exposure And Extended Biomarker Activity." . . . . . 99.04 226 99.52 100.00 8.05e-148 . . . . 7003 1 129 no PDB 3R92 . "Discovery Of A Macrocyclic O-Aminobenzamide Hsp90 Inhibitor With Heterocyclic Tether That Shows Extended Biomarker Activity And" . . . . . 99.04 226 99.52 100.00 8.05e-148 . . . . 7003 1 130 no PDB 3RKZ . "Discovery Of A Stable Macrocyclic O-Aminobenzamide Hsp90 Inhibitor Capable Of Significantly Decreasing Tumor Volume In A Mouse " . . . . . 99.04 226 99.52 100.00 8.05e-148 . . . . 7003 1 131 no PDB 3RLP . "Co-Crystal Structure Of The Hsp90 Atp Binding Domain In Complex With 4-(2,4-Dichloro-5-Methoxyphenyl)-6-Methylpyrimidin-2-Amine" . . . . . 99.04 226 99.52 100.00 1.53e-147 . . . . 7003 1 132 no PDB 3RLQ . "Co-Crystal Structure Of The Hsp90 Atp Binding Domain In Complex With 4-(2,4-Dichloro-5-Methoxyphenyl)-2-Methyl-7h-Pyrrolo[2,3- " . . . . . 99.04 226 99.52 100.00 1.53e-147 . . . . 7003 1 133 no PDB 3RLR . "Co-crystal Structure Of The Hsp90 Atp Binding Domain In Complex With 4-(2,4-dichloro-5-methoxyphenyl)-2,6-dimethyl-7h-pyrrolo[2" . . . . . 99.04 226 99.52 100.00 1.53e-147 . . . . 7003 1 134 no PDB 3T0H . "Structure Insights Into Mechanisms Of Atp Hydrolysis And The Activation Of Human Hsp90" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 135 no PDB 3T0Z . "Hsp90 N-Terminal Domain Bound To Atp" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 136 no PDB 3T10 . "Hsp90 N-Terminal Domain Bound To Acp" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 137 no PDB 3T1K . "Hsp90 N-Terminal Domain Bound To Anp" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 138 no PDB 3T2S . "Hsp90 N-Terminal Domain Bound To Ags" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 139 no PDB 3TUH . "Crystal Structure Of The N-Terminal Domain Of An Hsp90 In The Presence Of An The Inhibitor Ganetespib" . . . . . 99.04 209 99.52 100.00 6.52e-148 . . . . 7003 1 140 no PDB 3VHA . "Hsp90 Alpha N-Terminal Domain In Complex With A Macrocyclic Inhibitor" . . . . . 99.52 229 99.04 99.52 6.45e-148 . . . . 7003 1 141 no PDB 3VHC . "Hsp90 Alpha N-Terminal Domain In Complex With A Macrocyclic Inhibitor" . . . . . 99.52 229 99.04 99.52 6.45e-148 . . . . 7003 1 142 no PDB 3VHD . "Hsp90 Alpha N-Terminal Domain In Complex With A Macrocyclic Inhibitor, Ch5164840" . . . . . 99.52 229 99.04 99.52 6.45e-148 . . . . 7003 1 143 no PDB 3WHA . "Hsp90 Alpha N-terminal Domain In Complex With A Tricyclic Inhibitor" . . . . . 99.52 229 99.04 99.52 6.45e-148 . . . . 7003 1 144 no PDB 4AWO . "Complex Of Hsp90 Atpase Domain With Tropane Derived Inhibitors" . . . . . 99.52 230 99.04 99.52 7.70e-148 . . . . 7003 1 145 no PDB 4AWP . "Complex Of Hsp90 Atpase Domain With Tropane Derived Inhibitors" . . . . . 99.52 230 99.04 99.52 7.70e-148 . . . . 7003 1 146 no PDB 4AWQ . "Complex Of Hsp90 Atpase Domain With Tropane Derived Inhibitors" . . . . . 99.52 230 99.04 99.52 7.70e-148 . . . . 7003 1 147 no PDB 4B7P . "Structure Of Hsp90 With Nms-e973 Inhibitor Bound" . . . . . 99.52 230 99.04 99.52 1.13e-147 . . . . 7003 1 148 no PDB 4BQG . "Structure Of Hsp90 With An Inhibitor Bound" . . . . . 99.52 230 99.04 99.52 1.13e-147 . . . . 7003 1 149 no PDB 4BQJ . "Structure Of Hsp90 With An Inhibitor Bound" . . . . . 99.52 230 99.04 99.52 1.13e-147 . . . . 7003 1 150 no PDB 4CWF . "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" . . . . . 99.52 230 99.04 99.52 1.13e-147 . . . . 7003 1 151 no PDB 4CWN . "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" . . . . . 99.52 230 99.04 99.52 1.13e-147 . . . . 7003 1 152 no PDB 4CWO . "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" . . . . . 99.52 230 99.04 99.52 1.13e-147 . . . . 7003 1 153 no PDB 4CWP . "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" . . . . . 99.52 230 99.04 99.52 1.13e-147 . . . . 7003 1 154 no PDB 4CWQ . "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" . . . . . 99.52 230 99.04 99.52 1.13e-147 . . . . 7003 1 155 no PDB 4CWR . "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" . . . . . 99.52 230 99.04 99.52 1.13e-147 . . . . 7003 1 156 no PDB 4CWS . "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" . . . . . 99.52 230 99.04 99.52 1.13e-147 . . . . 7003 1 157 no PDB 4CWT . "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" . . . . . 99.52 230 99.04 99.52 1.13e-147 . . . . 7003 1 158 no PDB 4EEH . "Hsp90 Alpha N-Terminal Domain In Complex With An Inhibitor 3-(4- Hydroxy-Phenyl)-1h-Indazol-6-Ol" . . . . . 99.52 229 99.04 99.52 8.76e-148 . . . . 7003 1 159 no PDB 4EFT . "Hsp90 Alpha N-Terminal Domain In Complex With An Inhibitor 3- Cyclohexyl-2-(6-Hydroxy-1h-Indazol-3-Yl)-Propionitrile" . . . . . 99.52 229 99.04 99.52 8.76e-148 . . . . 7003 1 160 no PDB 4EFU . "Hsp90 Alpha N-Terminal Domain In Complex With An Inhibitor 6-Hydroxy- 3-(3-Methyl-Benzyl)-1h-Indazole-5-Carboxylic Acid Benzyl-" . . . . . 99.52 229 99.04 99.52 8.76e-148 . . . . 7003 1 161 no PDB 4EGH . "Hsp90-Alpha Atpase Domain In Complex With (4-Hydroxyphenyl)morpholin- 4-Yl Methanone" . . . . . 99.04 232 99.52 100.00 1.11e-147 . . . . 7003 1 162 no PDB 4EGI . "Hsp90-Alpha Atpase Domain In Complex With 2-Amino-4-Ethylthio-6- Methyl-1,3,5-Triazine" . . . . . 99.04 232 99.52 100.00 1.11e-147 . . . . 7003 1 163 no PDB 4EGK . "Human Hsp90-Alpha Atpase Domain Bound To Radicicol" . . . . . 99.04 232 99.52 100.00 1.11e-147 . . . . 7003 1 164 no PDB 4FCP . "Targetting Conserved Water Molecules: Design Of 4-Aryl-5-Cyanopyrrolo [2,3-D] Pyrimidine Hsp90 Inhibitors Using Fragment-Based " . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 165 no PDB 4FCQ . "Targeting Conserved Water Molecules: Design Of 4-Aryl-5- Cyanopyrrolo[2,3-D]pyrimidine Hsp90 Inhibitors Using Fragment-Based Sc" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 166 no PDB 4FCR . "Targeting Conserved Water Molecules: Design Of 4-Aryl-5- Cyanopyrrolo[2,3-D]pyrimidine Hsp90 Inhibitors Using Fragment-Based Sc" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 167 no PDB 4HY6 . "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj1" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 168 no PDB 4JQL . "Synthesis Of Benzoquinone-ansamycin-inspired Macrocyclic Lactams From Shikimic Acid" . . . . . 99.04 249 99.52 100.00 2.47e-147 . . . . 7003 1 169 no PDB 4L8Z . "Crystal Structure Of Human Hsp90 With Rl1" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 170 no PDB 4L90 . "Crystal Structure Of Human Hsp90 With Rl3" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 171 no PDB 4L91 . "Crystal Structure Of Human Hsp90 With X29" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 172 no PDB 4L93 . "Crystal Structure Of Human Hsp90 With S36" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 173 no PDB 4L94 . "Crystal Structure Of Human Hsp90 With S46" . . . . . 99.52 228 99.04 99.52 6.15e-148 . . . . 7003 1 174 no PDB 4LWE . "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj2" . . . . . 99.04 208 99.52 100.00 7.75e-148 . . . . 7003 1 175 no PDB 4LWF . "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj3" . . . . . 99.04 208 99.52 100.00 7.75e-148 . . . . 7003 1 176 no PDB 4LWG . "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj4" . . . . . 99.04 208 99.52 100.00 7.75e-148 . . . . 7003 1 177 no PDB 4LWH . "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj5" . . . . . 99.04 209 99.52 100.00 6.52e-148 . . . . 7003 1 178 no PDB 4LWI . "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj6" . . . . . 99.04 208 99.52 100.00 7.75e-148 . . . . 7003 1 179 no PDB 4NH7 . "Correlation Between Chemotype-dependent Binding Conformations Of Hsp90 Alpha/beta And Isoform Selectivity" . . . . . 99.04 233 99.52 100.00 1.36e-147 . . . . 7003 1 180 no PDB 4NH8 . "Correlation Between Chemotype-dependent Binding Conformations Of Hsp90 Alpha/beta And Isoform Selectivity" . . . . . 99.04 233 99.52 100.00 1.36e-147 . . . . 7003 1 181 no PDB 4O05 . "Identification Of Novel Hsp90/isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Utilit" . . . . . 99.04 233 99.52 100.00 1.36e-147 . . . . 7003 1 182 no PDB 4O07 . "Identification Of Novel Hsp90/isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Utilit" . . . . . 99.04 233 99.52 100.00 1.36e-147 . . . . 7003 1 183 no PDB 4O09 . "Identification Of Novel Hsp90 / Isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Util" . . . . . 99.04 233 99.52 100.00 1.36e-147 . . . . 7003 1 184 no PDB 4O0B . "Identification Of Novel Hsp90/isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Utilit" . . . . . 99.04 233 99.52 100.00 1.36e-147 . . . . 7003 1 185 no PDB 4R3M . "Crystal Structure Of Human Hsp90 With Jr9" . . . . . 99.04 209 99.52 100.00 6.52e-148 . . . . 7003 1 186 no PDB 4U93 . "Crystal Structure Of Hsp90-alpha N-domain Bound To The Inhibitor Nvp- Hsp990" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 187 no PDB 4W7T . "Crystal Structure Of Hsp90-alpha N-domain Bound To The Inhibitor Nvp- Hsp990" . . . . . 99.52 236 99.04 99.52 5.64e-148 . . . . 7003 1 188 no DBJ BAB20777 . "heat shock protein 90 alpha [Equus caballus]" . . . . . 99.52 719 99.04 99.52 2.08e-142 . . . . 7003 1 189 no DBJ BAB23449 . "unnamed protein product [Mus musculus]" . . . . . 99.52 733 98.56 99.52 2.16e-141 . . . . 7003 1 190 no DBJ BAC36610 . "unnamed protein product [Mus musculus]" . . . . . 99.52 557 98.56 99.52 3.79e-143 . . . . 7003 1 191 no DBJ BAC40681 . "unnamed protein product [Mus musculus]" . . . . . 99.52 274 98.56 99.52 1.76e-147 . . . . 7003 1 192 no DBJ BAC82487 . "90-kDa heat shock protein alpha [Bos taurus]" . . . . . 99.52 733 99.04 99.52 2.53e-142 . . . . 7003 1 193 no EMBL CAA30255 . "unnamed protein product [Homo sapiens]" . . . . . 99.52 312 99.04 99.52 8.53e-148 . . . . 7003 1 194 no EMBL CAA33259 . "unnamed protein product [Homo sapiens]" . . . . . 99.52 732 99.52 99.52 8.92e-143 . . . . 7003 1 195 no EMBL CAC39453 . "heat shock protein 86 [Rattus norvegicus]" . . . . . 99.52 733 99.04 99.52 2.91e-142 . . . . 7003 1 196 no EMBL CAD21648 . "heat shock protein 86 [Rattus norvegicus]" . . . . . 99.52 733 99.04 99.52 2.91e-142 . . . . 7003 1 197 no EMBL CAD66568 . "unnamed protein product [Homo sapiens]" . . . . . 59.33 262 99.19 100.00 4.91e-80 . . . . 7003 1 198 no GB AAA36023 . "heat shock protein 86, partial [Homo sapiens]" . . . . . 99.52 312 99.04 99.52 8.53e-148 . . . . 7003 1 199 no GB AAA36992 . "heat shock protein 90A [Cricetulus griseus]" . . . . . 99.52 733 97.60 99.52 7.88e-141 . . . . 7003 1 200 no GB AAA37868 . "heat-shock protein hsp86, partial [Mus musculus]" . . . . . 99.52 347 98.56 99.52 1.40e-145 . . . . 7003 1 201 no GB AAA53068 . "heat shock protein 86 [Mus musculus]" . . . . . 99.52 733 98.56 99.52 2.16e-141 . . . . 7003 1 202 no GB AAA63194 . "heat shock protein [Homo sapiens]" . . . . . 99.52 732 99.04 99.52 3.02e-142 . . . . 7003 1 203 no REF NP_001012688 . "heat shock protein HSP 90-alpha [Bos taurus]" . . . . . 99.52 733 99.04 99.52 2.53e-142 . . . . 7003 1 204 no REF NP_001017963 . "heat shock protein HSP 90-alpha isoform 1 [Homo sapiens]" . . . . . 99.52 854 99.04 99.52 2.22e-140 . . . . 7003 1 205 no REF NP_001092042 . "heat shock protein HSP 90-alpha [Pan troglodytes]" . . . . . 99.52 733 98.56 99.04 2.99e-141 . . . . 7003 1 206 no REF NP_001157427 . "heat shock protein HSP 90-alpha [Equus caballus]" . . . . . 99.52 733 99.04 99.52 3.31e-142 . . . . 7003 1 207 no REF NP_001182596 . "heat shock protein 90kDa alpha (cytosolic), class A member 1 [Macaca mulatta]" . . . . . 99.52 733 99.04 99.52 2.88e-142 . . . . 7003 1 208 no SP A5A6K9 . "RecName: Full=Heat shock protein HSP 90-alpha [Pan troglodytes]" . . . . . 99.52 733 98.56 99.04 2.99e-141 . . . . 7003 1 209 no SP O02705 . "RecName: Full=Heat shock protein HSP 90-alpha [Sus scrofa]" . . . . . 99.52 733 99.04 99.52 2.88e-142 . . . . 7003 1 210 no SP P07900 . "RecName: Full=Heat shock protein HSP 90-alpha; AltName: Full=Heat shock 86 kDa; Short=HSP 86; Short=HSP86; AltName: Full=Lipopo" . . . . . 99.52 732 99.04 99.52 3.02e-142 . . . . 7003 1 211 no SP P07901 . "RecName: Full=Heat shock protein HSP 90-alpha; AltName: Full=Heat shock 86 kDa; Short=HSP 86; Short=HSP86; AltName: Full=Tumor-" . . . . . 99.52 733 98.56 99.52 2.16e-141 . . . . 7003 1 212 no SP P30946 . "RecName: Full=Heat shock protein HSP 90-alpha [Oryctolagus cuniculus]" . . . . . 99.52 694 98.08 99.04 3.93e-141 . . . . 7003 1 213 no TPG DAA17282 . "TPA: heat shock protein HSP 90-alpha [Bos taurus]" . . . . . 99.52 733 99.04 99.52 2.53e-142 . . . . 7003 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'hsp90 n-terminal domain' . 7003 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 15 GLY . 7003 1 2 16 HIS . 7003 1 3 17 VAL . 7003 1 4 18 GLU . 7003 1 5 19 THR . 7003 1 6 20 PHE . 7003 1 7 21 ALA . 7003 1 8 22 PHE . 7003 1 9 23 GLN . 7003 1 10 24 ALA . 7003 1 11 25 GLU . 7003 1 12 26 ILE . 7003 1 13 27 ALA . 7003 1 14 28 GLN . 7003 1 15 29 LEU . 7003 1 16 30 MET . 7003 1 17 31 SER . 7003 1 18 32 LEU . 7003 1 19 33 ILE . 7003 1 20 34 ILE . 7003 1 21 35 ASN . 7003 1 22 36 THR . 7003 1 23 37 PHE . 7003 1 24 38 TYR . 7003 1 25 39 SER . 7003 1 26 40 ASN . 7003 1 27 41 LYS . 7003 1 28 42 GLU . 7003 1 29 43 ILE . 7003 1 30 44 PHE . 7003 1 31 45 LEU . 7003 1 32 46 ARG . 7003 1 33 47 GLU . 7003 1 34 48 LEU . 7003 1 35 49 ILE . 7003 1 36 50 SER . 7003 1 37 51 ASN . 7003 1 38 52 SER . 7003 1 39 53 SER . 7003 1 40 54 ASP . 7003 1 41 55 ALA . 7003 1 42 56 LEU . 7003 1 43 57 ASP . 7003 1 44 58 LYS . 7003 1 45 59 ILE . 7003 1 46 60 ARG . 7003 1 47 61 TYR . 7003 1 48 62 GLU . 7003 1 49 63 THR . 7003 1 50 64 LEU . 7003 1 51 65 THR . 7003 1 52 66 ASP . 7003 1 53 67 PRO . 7003 1 54 68 SER . 7003 1 55 69 LYS . 7003 1 56 70 LEU . 7003 1 57 71 ASP . 7003 1 58 72 SER . 7003 1 59 73 GLY . 7003 1 60 74 LYS . 7003 1 61 75 GLU . 7003 1 62 76 LEU . 7003 1 63 77 HIS . 7003 1 64 78 ILE . 7003 1 65 79 ASN . 7003 1 66 80 LEU . 7003 1 67 81 ILE . 7003 1 68 82 PRO . 7003 1 69 83 ASN . 7003 1 70 84 LYS . 7003 1 71 85 GLN . 7003 1 72 86 ASP . 7003 1 73 87 ARG . 7003 1 74 88 THR . 7003 1 75 89 LEU . 7003 1 76 90 THR . 7003 1 77 91 ILE . 7003 1 78 92 VAL . 7003 1 79 93 ASP . 7003 1 80 94 THR . 7003 1 81 95 GLY . 7003 1 82 96 ILE . 7003 1 83 97 GLY . 7003 1 84 98 MET . 7003 1 85 99 THR . 7003 1 86 100 LYS . 7003 1 87 101 ALA . 7003 1 88 102 ASP . 7003 1 89 103 LEU . 7003 1 90 104 ILE . 7003 1 91 105 ASN . 7003 1 92 106 ASN . 7003 1 93 107 LEU . 7003 1 94 108 GLY . 7003 1 95 109 THR . 7003 1 96 110 ILE . 7003 1 97 111 ALA . 7003 1 98 112 LYS . 7003 1 99 113 SER . 7003 1 100 114 GLY . 7003 1 101 115 THR . 7003 1 102 116 LYS . 7003 1 103 117 ALA . 7003 1 104 118 PHE . 7003 1 105 119 MET . 7003 1 106 120 GLU . 7003 1 107 121 ALA . 7003 1 108 122 LEU . 7003 1 109 123 GLN . 7003 1 110 124 ALA . 7003 1 111 125 GLY . 7003 1 112 126 ALA . 7003 1 113 127 ASP . 7003 1 114 128 ILE . 7003 1 115 129 SER . 7003 1 116 130 MET . 7003 1 117 131 ILE . 7003 1 118 132 GLY . 7003 1 119 133 GLN . 7003 1 120 134 PHE . 7003 1 121 135 GLY . 7003 1 122 136 VAL . 7003 1 123 137 GLY . 7003 1 124 138 PHE . 7003 1 125 139 TYR . 7003 1 126 140 SER . 7003 1 127 141 ALA . 7003 1 128 142 TYR . 7003 1 129 143 LEU . 7003 1 130 144 VAL . 7003 1 131 145 ALA . 7003 1 132 146 GLU . 7003 1 133 147 LYS . 7003 1 134 148 VAL . 7003 1 135 149 THR . 7003 1 136 150 VAL . 7003 1 137 151 ILE . 7003 1 138 152 THR . 7003 1 139 153 LYS . 7003 1 140 154 HIS . 7003 1 141 155 ASN . 7003 1 142 156 ASP . 7003 1 143 157 ASP . 7003 1 144 158 GLU . 7003 1 145 159 GLN . 7003 1 146 160 TYR . 7003 1 147 161 ALA . 7003 1 148 162 TRP . 7003 1 149 163 GLU . 7003 1 150 164 SER . 7003 1 151 165 SER . 7003 1 152 166 ALA . 7003 1 153 167 GLY . 7003 1 154 168 GLY . 7003 1 155 169 SER . 7003 1 156 170 PHE . 7003 1 157 171 THR . 7003 1 158 172 VAL . 7003 1 159 173 ARG . 7003 1 160 174 THR . 7003 1 161 175 ASP . 7003 1 162 176 THR . 7003 1 163 177 GLY . 7003 1 164 178 GLU . 7003 1 165 179 PRO . 7003 1 166 180 MET . 7003 1 167 181 GLY . 7003 1 168 182 ARG . 7003 1 169 183 GLY . 7003 1 170 184 THR . 7003 1 171 185 LYS . 7003 1 172 186 VAL . 7003 1 173 187 ILE . 7003 1 174 188 LEU . 7003 1 175 189 HIS . 7003 1 176 190 LEU . 7003 1 177 191 LYS . 7003 1 178 192 GLU . 7003 1 179 193 ASP . 7003 1 180 194 GLN . 7003 1 181 195 THR . 7003 1 182 196 GLU . 7003 1 183 197 TYR . 7003 1 184 198 LEU . 7003 1 185 199 GLU . 7003 1 186 200 GLU . 7003 1 187 201 ARG . 7003 1 188 202 ARG . 7003 1 189 203 ILE . 7003 1 190 204 LYS . 7003 1 191 205 GLU . 7003 1 192 206 ILE . 7003 1 193 207 VAL . 7003 1 194 208 LYS . 7003 1 195 209 LYS . 7003 1 196 210 HIS . 7003 1 197 211 SER . 7003 1 198 212 GLN . 7003 1 199 213 PHE . 7003 1 200 214 ILE . 7003 1 201 215 GLY . 7003 1 202 216 TYR . 7003 1 203 217 PRO . 7003 1 204 218 ILE . 7003 1 205 219 THR . 7003 1 206 220 LEU . 7003 1 207 221 PHE . 7003 1 208 222 VAL . 7003 1 209 223 GLU . 7003 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 7003 1 . HIS 2 2 7003 1 . VAL 3 3 7003 1 . GLU 4 4 7003 1 . THR 5 5 7003 1 . PHE 6 6 7003 1 . ALA 7 7 7003 1 . PHE 8 8 7003 1 . GLN 9 9 7003 1 . ALA 10 10 7003 1 . GLU 11 11 7003 1 . ILE 12 12 7003 1 . ALA 13 13 7003 1 . GLN 14 14 7003 1 . LEU 15 15 7003 1 . MET 16 16 7003 1 . SER 17 17 7003 1 . LEU 18 18 7003 1 . ILE 19 19 7003 1 . ILE 20 20 7003 1 . ASN 21 21 7003 1 . THR 22 22 7003 1 . PHE 23 23 7003 1 . TYR 24 24 7003 1 . SER 25 25 7003 1 . ASN 26 26 7003 1 . LYS 27 27 7003 1 . GLU 28 28 7003 1 . ILE 29 29 7003 1 . PHE 30 30 7003 1 . LEU 31 31 7003 1 . ARG 32 32 7003 1 . GLU 33 33 7003 1 . LEU 34 34 7003 1 . ILE 35 35 7003 1 . SER 36 36 7003 1 . ASN 37 37 7003 1 . SER 38 38 7003 1 . SER 39 39 7003 1 . ASP 40 40 7003 1 . ALA 41 41 7003 1 . LEU 42 42 7003 1 . ASP 43 43 7003 1 . LYS 44 44 7003 1 . ILE 45 45 7003 1 . ARG 46 46 7003 1 . TYR 47 47 7003 1 . GLU 48 48 7003 1 . THR 49 49 7003 1 . LEU 50 50 7003 1 . THR 51 51 7003 1 . ASP 52 52 7003 1 . PRO 53 53 7003 1 . SER 54 54 7003 1 . LYS 55 55 7003 1 . LEU 56 56 7003 1 . ASP 57 57 7003 1 . SER 58 58 7003 1 . GLY 59 59 7003 1 . LYS 60 60 7003 1 . GLU 61 61 7003 1 . LEU 62 62 7003 1 . HIS 63 63 7003 1 . ILE 64 64 7003 1 . ASN 65 65 7003 1 . LEU 66 66 7003 1 . ILE 67 67 7003 1 . PRO 68 68 7003 1 . ASN 69 69 7003 1 . LYS 70 70 7003 1 . GLN 71 71 7003 1 . ASP 72 72 7003 1 . ARG 73 73 7003 1 . THR 74 74 7003 1 . LEU 75 75 7003 1 . THR 76 76 7003 1 . ILE 77 77 7003 1 . VAL 78 78 7003 1 . ASP 79 79 7003 1 . THR 80 80 7003 1 . GLY 81 81 7003 1 . ILE 82 82 7003 1 . GLY 83 83 7003 1 . MET 84 84 7003 1 . THR 85 85 7003 1 . LYS 86 86 7003 1 . ALA 87 87 7003 1 . ASP 88 88 7003 1 . LEU 89 89 7003 1 . ILE 90 90 7003 1 . ASN 91 91 7003 1 . ASN 92 92 7003 1 . LEU 93 93 7003 1 . GLY 94 94 7003 1 . THR 95 95 7003 1 . ILE 96 96 7003 1 . ALA 97 97 7003 1 . LYS 98 98 7003 1 . SER 99 99 7003 1 . GLY 100 100 7003 1 . THR 101 101 7003 1 . LYS 102 102 7003 1 . ALA 103 103 7003 1 . PHE 104 104 7003 1 . MET 105 105 7003 1 . GLU 106 106 7003 1 . ALA 107 107 7003 1 . LEU 108 108 7003 1 . GLN 109 109 7003 1 . ALA 110 110 7003 1 . GLY 111 111 7003 1 . ALA 112 112 7003 1 . ASP 113 113 7003 1 . ILE 114 114 7003 1 . SER 115 115 7003 1 . MET 116 116 7003 1 . ILE 117 117 7003 1 . GLY 118 118 7003 1 . GLN 119 119 7003 1 . PHE 120 120 7003 1 . GLY 121 121 7003 1 . VAL 122 122 7003 1 . GLY 123 123 7003 1 . PHE 124 124 7003 1 . TYR 125 125 7003 1 . SER 126 126 7003 1 . ALA 127 127 7003 1 . TYR 128 128 7003 1 . LEU 129 129 7003 1 . VAL 130 130 7003 1 . ALA 131 131 7003 1 . GLU 132 132 7003 1 . LYS 133 133 7003 1 . VAL 134 134 7003 1 . THR 135 135 7003 1 . VAL 136 136 7003 1 . ILE 137 137 7003 1 . THR 138 138 7003 1 . LYS 139 139 7003 1 . HIS 140 140 7003 1 . ASN 141 141 7003 1 . ASP 142 142 7003 1 . ASP 143 143 7003 1 . GLU 144 144 7003 1 . GLN 145 145 7003 1 . TYR 146 146 7003 1 . ALA 147 147 7003 1 . TRP 148 148 7003 1 . GLU 149 149 7003 1 . SER 150 150 7003 1 . SER 151 151 7003 1 . ALA 152 152 7003 1 . GLY 153 153 7003 1 . GLY 154 154 7003 1 . SER 155 155 7003 1 . PHE 156 156 7003 1 . THR 157 157 7003 1 . VAL 158 158 7003 1 . ARG 159 159 7003 1 . THR 160 160 7003 1 . ASP 161 161 7003 1 . THR 162 162 7003 1 . GLY 163 163 7003 1 . GLU 164 164 7003 1 . PRO 165 165 7003 1 . MET 166 166 7003 1 . GLY 167 167 7003 1 . ARG 168 168 7003 1 . GLY 169 169 7003 1 . THR 170 170 7003 1 . LYS 171 171 7003 1 . VAL 172 172 7003 1 . ILE 173 173 7003 1 . LEU 174 174 7003 1 . HIS 175 175 7003 1 . LEU 176 176 7003 1 . LYS 177 177 7003 1 . GLU 178 178 7003 1 . ASP 179 179 7003 1 . GLN 180 180 7003 1 . THR 181 181 7003 1 . GLU 182 182 7003 1 . TYR 183 183 7003 1 . LEU 184 184 7003 1 . GLU 185 185 7003 1 . GLU 186 186 7003 1 . ARG 187 187 7003 1 . ARG 188 188 7003 1 . ILE 189 189 7003 1 . LYS 190 190 7003 1 . GLU 191 191 7003 1 . ILE 192 192 7003 1 . VAL 193 193 7003 1 . LYS 194 194 7003 1 . LYS 195 195 7003 1 . HIS 196 196 7003 1 . SER 197 197 7003 1 . GLN 198 198 7003 1 . PHE 199 199 7003 1 . ILE 200 200 7003 1 . GLY 201 201 7003 1 . TYR 202 202 7003 1 . PRO 203 203 7003 1 . ILE 204 204 7003 1 . THR 205 205 7003 1 . LEU 206 206 7003 1 . PHE 207 207 7003 1 . VAL 208 208 7003 1 . GLU 209 209 7003 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 7003 _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 $hsp90 . 9606 organism no . Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 7003 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 7003 _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 $hsp90 . 'recombinant technology' . 'E. coli' . . . . . . . . . . . . . . . . . . . . . . . . . . . 7003 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 7003 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _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 hsp90 '[U-2H; U-13C; U-15N]' . . 1 $hsp90 . . 1.5 . . mM 0.2 . . . 7003 1 2 'sodium phosphate' . . . . . . . 20 . . mM 1 . . . 7003 1 stop_ save_ ####################### # Sample conditions # ####################### save_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode conditions_1 _Sample_condition_list.Entry_ID 7003 _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 pH 7.5 0.1 pH 7003 1 temperature 298 0.1 K 7003 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_800MHz_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode 800MHz_spectrometer _NMR_spectrometer.Entry_ID 7003 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX800 _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_NMR_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode NMR_experiment_list _Experiment_list.Entry_ID 7003 _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 1H15N_TROSY no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . 1 $800MHz_spectrometer . . . . . . . . . . . . . . . . 7003 1 2 TROSY_HNCO no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . 1 $800MHz_spectrometer . . . . . . . . . . . . . . . . 7003 1 3 TROSY_HNCACO no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . 1 $800MHz_spectrometer . . . . . . . . . . . . . . . . 7003 1 4 TROSY_HNCACB no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . 1 $800MHz_spectrometer . . . . . . . . . . . . . . . . 7003 1 5 TROSY_HNCOCACB no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . 1 $800MHz_spectrometer . . . . . . . . . . . . . . . . 7003 1 6 TROSY_HNCA no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . 1 $800MHz_spectrometer . . . . . . . . . . . . . . . . 7003 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_referencing _Chem_shift_reference.Entry_ID 7003 _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 0.0 . indirect 0.251449530 . . . 1 $entry_citation . . 1 $entry_citation 7003 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . 1 $entry_citation . . 1 $entry_citation 7003 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . 1 $entry_citation . . 1 $entry_citation 7003 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_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 7003 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_referencing _Assigned_chem_shift_list.Chem_shift_1H_err 0.1 _Assigned_chem_shift_list.Chem_shift_13C_err 0.5 _Assigned_chem_shift_list.Chem_shift_15N_err 0.5 _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 1H15N_TROSY 1 $sample_1 isotropic 7003 1 2 TROSY_HNCO 1 $sample_1 isotropic 7003 1 3 TROSY_HNCACO 1 $sample_1 isotropic 7003 1 4 TROSY_HNCACB 1 $sample_1 isotropic 7003 1 5 TROSY_HNCOCACB 1 $sample_1 isotropic 7003 1 stop_ loop_ _Systematic_chem_shift_offset.Type _Systematic_chem_shift_offset.Atom_type _Systematic_chem_shift_offset.Atom_isotope_number _Systematic_chem_shift_offset.Val _Systematic_chem_shift_offset.Val_err _Systematic_chem_shift_offset.Entry_ID _Systematic_chem_shift_offset.Assigned_chem_shift_list_ID 'spectrometer error' 13C . 2.27 . 7003 1 'TROSY effect' 1H . 0.056 . 7003 1 'TROSY effect' 15N . -0.236 . 7003 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 VAL C C 13 177.757 0.500 . 1 . . . . 17 VAL C . 7003 1 2 . 1 1 3 3 VAL CA C 13 52.822 0.500 . 1 . . . . 17 VAL CA . 7003 1 3 . 1 1 3 3 VAL CB C 13 31.788 0.500 . 1 . . . . 17 VAL CB . 7003 1 4 . 1 1 4 4 GLU H H 1 8.501 0.002 . 1 . . . . 18 GLU H . 7003 1 5 . 1 1 4 4 GLU C C 13 178.081 0.209 . 1 . . . . 18 GLU C . 7003 1 6 . 1 1 4 4 GLU CA C 13 52.931 0.087 . 1 . . . . 18 GLU CA . 7003 1 7 . 1 1 4 4 GLU CB C 13 31.073 0.153 . 1 . . . . 18 GLU CB . 7003 1 8 . 1 1 4 4 GLU N N 15 124.977 0.500 . 1 . . . . 18 GLU N . 7003 1 9 . 1 1 5 5 THR H H 1 7.855 0.004 . 1 . . . . 19 THR H . 7003 1 10 . 1 1 5 5 THR C C 13 179.533 0.122 . 1 . . . . 19 THR C . 7003 1 11 . 1 1 5 5 THR CA C 13 59.294 0.500 . 1 . . . . 19 THR CA . 7003 1 12 . 1 1 5 5 THR CB C 13 67.108 0.500 . 1 . . . . 19 THR CB . 7003 1 13 . 1 1 5 5 THR N N 15 118.211 0.500 . 1 . . . . 19 THR N . 7003 1 14 . 1 1 6 6 PHE H H 1 8.617 0.001 . 1 . . . . 20 PHE H . 7003 1 15 . 1 1 6 6 PHE C C 13 178.785 0.121 . 1 . . . . 20 PHE C . 7003 1 16 . 1 1 6 6 PHE CA C 13 53.360 0.500 . 1 . . . . 20 PHE CA . 7003 1 17 . 1 1 6 6 PHE CB C 13 39.612 0.087 . 1 . . . . 20 PHE CB . 7003 1 18 . 1 1 6 6 PHE N N 15 125.406 0.500 . 1 . . . . 20 PHE N . 7003 1 19 . 1 1 7 7 ALA H H 1 8.151 0.001 . 1 . . . . 21 ALA H . 7003 1 20 . 1 1 7 7 ALA C C 13 173.266 0.135 . 1 . . . . 21 ALA C . 7003 1 21 . 1 1 7 7 ALA CA C 13 48.052 0.500 . 1 . . . . 21 ALA CA . 7003 1 22 . 1 1 7 7 ALA CB C 13 16.600 0.500 . 1 . . . . 21 ALA CB . 7003 1 23 . 1 1 7 7 ALA N N 15 122.437 0.500 . 1 . . . . 21 ALA N . 7003 1 24 . 1 1 8 8 PHE H H 1 7.583 0.001 . 1 . . . . 22 PHE H . 7003 1 25 . 1 1 8 8 PHE C C 13 174.908 0.500 . 1 . . . . 22 PHE C . 7003 1 26 . 1 1 8 8 PHE CA C 13 56.338 0.500 . 1 . . . . 22 PHE CA . 7003 1 27 . 1 1 8 8 PHE CB C 13 38.007 0.500 . 1 . . . . 22 PHE CB . 7003 1 28 . 1 1 8 8 PHE N N 15 118.638 0.500 . 1 . . . . 22 PHE N . 7003 1 29 . 1 1 11 11 GLU C C 13 173.797 0.500 . 1 . . . . 25 GLU C . 7003 1 30 . 1 1 11 11 GLU CA C 13 57.504 0.500 . 1 . . . . 25 GLU CA . 7003 1 31 . 1 1 11 11 GLU CB C 13 25.986 0.500 . 1 . . . . 25 GLU CB . 7003 1 32 . 1 1 12 12 ILE H H 1 7.159 0.006 . 1 . . . . 26 ILE H . 7003 1 33 . 1 1 12 12 ILE C C 13 174.550 0.065 . 1 . . . . 26 ILE C . 7003 1 34 . 1 1 12 12 ILE CA C 13 61.272 0.153 . 1 . . . . 26 ILE CA . 7003 1 35 . 1 1 12 12 ILE CB C 13 34.238 0.500 . 1 . . . . 26 ILE CB . 7003 1 36 . 1 1 12 12 ILE N N 15 120.211 0.500 . 1 . . . . 26 ILE N . 7003 1 37 . 1 1 13 13 ALA H H 1 8.082 0.002 . 1 . . . . 27 ALA H . 7003 1 38 . 1 1 13 13 ALA C C 13 171.456 0.058 . 1 . . . . 27 ALA C . 7003 1 39 . 1 1 13 13 ALA CA C 13 52.667 0.500 . 1 . . . . 27 ALA CA . 7003 1 40 . 1 1 13 13 ALA CB C 13 14.621 0.087 . 1 . . . . 27 ALA CB . 7003 1 41 . 1 1 13 13 ALA N N 15 121.571 0.500 . 1 . . . . 27 ALA N . 7003 1 42 . 1 1 14 14 GLN H H 1 7.807 0.005 . 1 . . . . 28 GLN H . 7003 1 43 . 1 1 14 14 GLN C C 13 173.931 0.091 . 1 . . . . 28 GLN C . 7003 1 44 . 1 1 14 14 GLN CA C 13 55.964 0.500 . 1 . . . . 28 GLN CA . 7003 1 45 . 1 1 14 14 GLN CB C 13 25.270 0.021 . 1 . . . . 28 GLN CB . 7003 1 46 . 1 1 14 14 GLN N N 15 118.860 0.500 . 1 . . . . 28 GLN N . 7003 1 47 . 1 1 15 15 LEU H H 1 7.994 0.100 . 1 . . . . 29 LEU H . 7003 1 48 . 1 1 15 15 LEU C C 13 174.154 0.171 . 1 . . . . 29 LEU C . 7003 1 49 . 1 1 15 15 LEU CA C 13 55.700 0.087 . 1 . . . . 29 LEU CA . 7003 1 50 . 1 1 15 15 LEU CB C 13 37.700 0.500 . 1 . . . . 29 LEU CB . 7003 1 51 . 1 1 15 15 LEU N N 15 123.376 0.500 . 1 . . . . 29 LEU N . 7003 1 52 . 1 1 16 16 MET H H 1 8.230 0.003 . 1 . . . . 30 MET H . 7003 1 53 . 1 1 16 16 MET C C 13 175.334 0.027 . 1 . . . . 30 MET C . 7003 1 54 . 1 1 16 16 MET CA C 13 57.843 0.021 . 1 . . . . 30 MET CA . 7003 1 55 . 1 1 16 16 MET CB C 13 30.479 0.153 . 1 . . . . 30 MET CB . 7003 1 56 . 1 1 16 16 MET N N 15 116.907 0.500 . 1 . . . . 30 MET N . 7003 1 57 . 1 1 17 17 SER H H 1 7.517 0.005 . 1 . . . . 31 SER H . 7003 1 58 . 1 1 17 17 SER C C 13 175.819 0.022 . 1 . . . . 31 SER C . 7003 1 59 . 1 1 17 17 SER CA C 13 58.832 0.500 . 1 . . . . 31 SER CA . 7003 1 60 . 1 1 17 17 SER CB C 13 60.283 0.500 . 1 . . . . 31 SER CB . 7003 1 61 . 1 1 17 17 SER N N 15 111.961 0.500 . 1 . . . . 31 SER N . 7003 1 62 . 1 1 18 18 LEU H H 1 7.704 0.004 . 1 . . . . 32 LEU H . 7003 1 63 . 1 1 18 18 LEU C C 13 172.391 0.066 . 1 . . . . 32 LEU C . 7003 1 64 . 1 1 18 18 LEU CA C 13 55.634 0.500 . 1 . . . . 32 LEU CA . 7003 1 65 . 1 1 18 18 LEU CB C 13 38.985 0.021 . 1 . . . . 32 LEU CB . 7003 1 66 . 1 1 18 18 LEU N N 15 122.111 0.500 . 1 . . . . 32 LEU N . 7003 1 67 . 1 1 19 19 ILE H H 1 8.045 0.003 . 1 . . . . 33 ILE H . 7003 1 68 . 1 1 19 19 ILE C C 13 175.663 0.076 . 1 . . . . 33 ILE C . 7003 1 69 . 1 1 19 19 ILE CA C 13 62.162 0.219 . 1 . . . . 33 ILE CA . 7003 1 70 . 1 1 19 19 ILE CB C 13 35.029 0.500 . 1 . . . . 33 ILE CB . 7003 1 71 . 1 1 19 19 ILE N N 15 120.088 0.500 . 1 . . . . 33 ILE N . 7003 1 72 . 1 1 20 20 ILE H H 1 8.009 0.005 . 1 . . . . 34 ILE H . 7003 1 73 . 1 1 20 20 ILE C C 13 174.629 0.053 . 1 . . . . 34 ILE C . 7003 1 74 . 1 1 20 20 ILE CA C 13 61.668 0.153 . 1 . . . . 34 ILE CA . 7003 1 75 . 1 1 20 20 ILE CB C 13 35.985 0.087 . 1 . . . . 34 ILE CB . 7003 1 76 . 1 1 20 20 ILE N N 15 116.795 0.500 . 1 . . . . 34 ILE N . 7003 1 77 . 1 1 21 21 ASN H H 1 7.598 0.001 . 1 . . . . 35 ASN H . 7003 1 78 . 1 1 21 21 ASN C C 13 177.203 0.072 . 1 . . . . 35 ASN C . 7003 1 79 . 1 1 21 21 ASN CA C 13 51.678 0.500 . 1 . . . . 35 ASN CA . 7003 1 80 . 1 1 21 21 ASN CB C 13 37.469 0.500 . 1 . . . . 35 ASN CB . 7003 1 81 . 1 1 21 21 ASN N N 15 114.603 0.500 . 1 . . . . 35 ASN N . 7003 1 82 . 1 1 22 22 THR H H 1 7.199 0.007 . 1 . . . . 36 THR H . 7003 1 83 . 1 1 22 22 THR C C 13 179.487 0.500 . 1 . . . . 36 THR C . 7003 1 84 . 1 1 22 22 THR CA C 13 59.898 0.500 . 1 . . . . 36 THR CA . 7003 1 85 . 1 1 22 22 THR CB C 13 66.888 0.500 . 1 . . . . 36 THR CB . 7003 1 86 . 1 1 22 22 THR N N 15 117.019 0.500 . 1 . . . . 36 THR N . 7003 1 87 . 1 1 23 23 PHE C C 13 177.424 0.500 . 1 . . . . 37 PHE C . 7003 1 88 . 1 1 23 23 PHE CA C 13 58.427 0.500 . 1 . . . . 37 PHE CA . 7003 1 89 . 1 1 23 23 PHE CB C 13 37.129 0.500 . 1 . . . . 37 PHE CB . 7003 1 90 . 1 1 24 24 TYR H H 1 7.026 0.002 . 1 . . . . 38 TYR H . 7003 1 91 . 1 1 24 24 TYR C C 13 175.349 0.150 . 1 . . . . 38 TYR C . 7003 1 92 . 1 1 24 24 TYR CA C 13 58.800 0.500 . 1 . . . . 38 TYR CA . 7003 1 93 . 1 1 24 24 TYR CB C 13 34.436 0.500 . 1 . . . . 38 TYR CB . 7003 1 94 . 1 1 24 24 TYR N N 15 110.256 0.500 . 1 . . . . 38 TYR N . 7003 1 95 . 1 1 25 25 SER H H 1 7.879 0.100 . 1 . . . . 39 SER H . 7003 1 96 . 1 1 25 25 SER C C 13 175.289 0.500 . 1 . . . . 39 SER C . 7003 1 97 . 1 1 25 25 SER CA C 13 59.173 0.500 . 1 . . . . 39 SER CA . 7003 1 98 . 1 1 25 25 SER CB C 13 60.492 0.500 . 1 . . . . 39 SER CB . 7003 1 99 . 1 1 25 25 SER N N 15 114.412 0.500 . 1 . . . . 39 SER N . 7003 1 100 . 1 1 26 26 ASN C C 13 177.732 0.500 . 1 . . . . 40 ASN C . 7003 1 101 . 1 1 26 26 ASN CA C 13 49.459 0.500 . 1 . . . . 40 ASN CA . 7003 1 102 . 1 1 26 26 ASN CB C 13 34.623 0.500 . 1 . . . . 40 ASN CB . 7003 1 103 . 1 1 27 27 LYS H H 1 7.777 0.008 . 1 . . . . 41 LYS H . 7003 1 104 . 1 1 27 27 LYS C C 13 175.357 0.073 . 1 . . . . 41 LYS C . 7003 1 105 . 1 1 27 27 LYS CA C 13 56.525 0.500 . 1 . . . . 41 LYS CA . 7003 1 106 . 1 1 27 27 LYS CB C 13 29.787 0.500 . 1 . . . . 41 LYS CB . 7003 1 107 . 1 1 27 27 LYS N N 15 117.300 0.500 . 1 . . . . 41 LYS N . 7003 1 108 . 1 1 28 28 GLU H H 1 8.275 0.003 . 1 . . . . 42 GLU H . 7003 1 109 . 1 1 28 28 GLU C C 13 176.866 0.070 . 1 . . . . 42 GLU C . 7003 1 110 . 1 1 28 28 GLU CA C 13 55.536 0.152 . 1 . . . . 42 GLU CA . 7003 1 111 . 1 1 28 28 GLU CB C 13 26.194 0.500 . 1 . . . . 42 GLU CB . 7003 1 112 . 1 1 28 28 GLU N N 15 114.535 0.500 . 1 . . . . 42 GLU N . 7003 1 113 . 1 1 29 29 ILE H H 1 6.742 0.003 . 1 . . . . 43 ILE H . 7003 1 114 . 1 1 29 29 ILE C C 13 175.844 0.131 . 1 . . . . 43 ILE C . 7003 1 115 . 1 1 29 29 ILE CA C 13 59.492 0.021 . 1 . . . . 43 ILE CA . 7003 1 116 . 1 1 29 29 ILE CB C 13 35.128 0.500 . 1 . . . . 43 ILE CB . 7003 1 117 . 1 1 29 29 ILE N N 15 112.419 0.500 . 1 . . . . 43 ILE N . 7003 1 118 . 1 1 30 30 PHE H H 1 7.843 0.003 . 1 . . . . 44 PHE H . 7003 1 119 . 1 1 30 30 PHE C C 13 176.342 0.500 . 1 . . . . 44 PHE C . 7003 1 120 . 1 1 30 30 PHE CA C 13 56.799 0.500 . 1 . . . . 44 PHE CA . 7003 1 121 . 1 1 30 30 PHE CB C 13 35.040 0.500 . 1 . . . . 44 PHE CB . 7003 1 122 . 1 1 30 30 PHE N N 15 120.582 0.500 . 1 . . . . 44 PHE N . 7003 1 123 . 1 1 31 31 LEU C C 13 174.316 0.500 . 1 . . . . 45 LEU C . 7003 1 124 . 1 1 31 31 LEU CA C 13 53.679 0.500 . 1 . . . . 45 LEU CA . 7003 1 125 . 1 1 31 31 LEU CB C 13 37.591 0.500 . 1 . . . . 45 LEU CB . 7003 1 126 . 1 1 32 32 ARG H H 1 6.331 0.100 . 1 . . . . 46 ARG H . 7003 1 127 . 1 1 32 32 ARG C C 13 173.326 0.073 . 1 . . . . 46 ARG C . 7003 1 128 . 1 1 32 32 ARG CA C 13 55.733 0.153 . 1 . . . . 46 ARG CA . 7003 1 129 . 1 1 32 32 ARG CB C 13 26.292 0.500 . 1 . . . . 46 ARG CB . 7003 1 130 . 1 1 32 32 ARG N N 15 117.514 0.500 . 1 . . . . 46 ARG N . 7003 1 131 . 1 1 33 33 GLU H H 1 7.587 0.005 . 1 . . . . 47 GLU H . 7003 1 132 . 1 1 33 33 GLU C C 13 173.095 0.500 . 1 . . . . 47 GLU C . 7003 1 133 . 1 1 33 33 GLU CA C 13 55.634 0.087 . 1 . . . . 47 GLU CA . 7003 1 134 . 1 1 33 33 GLU CB C 13 25.534 0.021 . 1 . . . . 47 GLU CB . 7003 1 135 . 1 1 33 33 GLU N N 15 116.974 0.500 . 1 . . . . 47 GLU N . 7003 1 136 . 1 1 34 34 LEU H H 1 7.749 0.004 . 1 . . . . 48 LEU H . 7003 1 137 . 1 1 34 34 LEU C C 13 172.423 0.038 . 1 . . . . 48 LEU C . 7003 1 138 . 1 1 34 34 LEU CA C 13 55.437 0.500 . 1 . . . . 48 LEU CA . 7003 1 139 . 1 1 34 34 LEU CB C 13 37.634 0.087 . 1 . . . . 48 LEU CB . 7003 1 140 . 1 1 34 34 LEU N N 15 119.604 0.500 . 1 . . . . 48 LEU N . 7003 1 141 . 1 1 35 35 ILE H H 1 8.112 0.100 . 1 . . . . 49 ILE H . 7003 1 142 . 1 1 35 35 ILE C C 13 174.414 0.174 . 1 . . . . 49 ILE C . 7003 1 143 . 1 1 35 35 ILE CA C 13 63.382 0.153 . 1 . . . . 49 ILE CA . 7003 1 144 . 1 1 35 35 ILE CB C 13 34.205 0.087 . 1 . . . . 49 ILE CB . 7003 1 145 . 1 1 35 35 ILE N N 15 120.166 0.500 . 1 . . . . 49 ILE N . 7003 1 146 . 1 1 36 36 SER H H 1 8.127 0.003 . 1 . . . . 50 SER H . 7003 1 147 . 1 1 36 36 SER C C 13 175.569 0.131 . 1 . . . . 50 SER C . 7003 1 148 . 1 1 36 36 SER CA C 13 59.393 0.500 . 1 . . . . 50 SER CA . 7003 1 149 . 1 1 36 36 SER CB C 13 60.448 0.087 . 1 . . . . 50 SER CB . 7003 1 150 . 1 1 36 36 SER N N 15 117.008 0.500 . 1 . . . . 50 SER N . 7003 1 151 . 1 1 37 37 ASN H H 1 7.772 0.001 . 1 . . . . 51 ASN H . 7003 1 152 . 1 1 37 37 ASN C C 13 173.198 0.500 . 1 . . . . 51 ASN C . 7003 1 153 . 1 1 37 37 ASN CA C 13 53.360 0.021 . 1 . . . . 51 ASN CA . 7003 1 154 . 1 1 37 37 ASN CB C 13 34.930 0.500 . 1 . . . . 51 ASN CB . 7003 1 155 . 1 1 37 37 ASN N N 15 120.719 0.500 . 1 . . . . 51 ASN N . 7003 1 156 . 1 1 38 38 SER H H 1 8.266 0.100 . 1 . . . . 52 SER H . 7003 1 157 . 1 1 38 38 SER C C 13 176.995 0.120 . 1 . . . . 52 SER C . 7003 1 158 . 1 1 38 38 SER CA C 13 60.909 0.500 . 1 . . . . 52 SER CA . 7003 1 159 . 1 1 38 38 SER CB C 13 60.184 0.500 . 1 . . . . 52 SER CB . 7003 1 160 . 1 1 38 38 SER N N 15 121.009 0.500 . 1 . . . . 52 SER N . 7003 1 161 . 1 1 39 39 SER H H 1 8.451 0.002 . 1 . . . . 53 SER H . 7003 1 162 . 1 1 39 39 SER C C 13 175.814 0.104 . 1 . . . . 53 SER C . 7003 1 163 . 1 1 39 39 SER CA C 13 59.030 0.500 . 1 . . . . 53 SER CA . 7003 1 164 . 1 1 39 39 SER CB C 13 60.514 0.500 . 1 . . . . 53 SER CB . 7003 1 165 . 1 1 39 39 SER N N 15 116.143 0.500 . 1 . . . . 53 SER N . 7003 1 166 . 1 1 40 40 ASP H H 1 8.068 0.001 . 1 . . . . 54 ASP H . 7003 1 167 . 1 1 40 40 ASP C C 13 173.816 0.106 . 1 . . . . 54 ASP C . 7003 1 168 . 1 1 40 40 ASP CA C 13 54.810 0.500 . 1 . . . . 54 ASP CA . 7003 1 169 . 1 1 40 40 ASP CB C 13 37.601 0.021 . 1 . . . . 54 ASP CB . 7003 1 170 . 1 1 40 40 ASP N N 15 119.661 0.500 . 1 . . . . 54 ASP N . 7003 1 171 . 1 1 41 41 ALA H H 1 7.732 0.001 . 1 . . . . 55 ALA H . 7003 1 172 . 1 1 41 41 ALA C C 13 170.427 0.106 . 1 . . . . 55 ALA C . 7003 1 173 . 1 1 41 41 ALA CA C 13 52.568 0.021 . 1 . . . . 55 ALA CA . 7003 1 174 . 1 1 41 41 ALA CB C 13 16.072 0.087 . 1 . . . . 55 ALA CB . 7003 1 175 . 1 1 41 41 ALA N N 15 123.376 0.500 . 1 . . . . 55 ALA N . 7003 1 176 . 1 1 42 42 LEU H H 1 8.351 0.001 . 1 . . . . 56 LEU H . 7003 1 177 . 1 1 42 42 LEU C C 13 174.473 0.077 . 1 . . . . 56 LEU C . 7003 1 178 . 1 1 42 42 LEU CA C 13 55.107 0.500 . 1 . . . . 56 LEU CA . 7003 1 179 . 1 1 42 42 LEU CB C 13 37.700 0.086 . 1 . . . . 56 LEU CB . 7003 1 180 . 1 1 42 42 LEU N N 15 124.670 0.500 . 1 . . . . 56 LEU N . 7003 1 181 . 1 1 43 43 ASP H H 1 8.701 0.002 . 1 . . . . 57 ASP H . 7003 1 182 . 1 1 43 43 ASP C C 13 173.418 0.074 . 1 . . . . 57 ASP C . 7003 1 183 . 1 1 43 43 ASP CA C 13 54.514 0.500 . 1 . . . . 57 ASP CA . 7003 1 184 . 1 1 43 43 ASP CB C 13 37.073 0.153 . 1 . . . . 57 ASP CB . 7003 1 185 . 1 1 43 43 ASP N N 15 119.930 0.500 . 1 . . . . 57 ASP N . 7003 1 186 . 1 1 44 44 LYS H H 1 7.648 0.001 . 1 . . . . 58 LYS H . 7003 1 187 . 1 1 44 44 LYS C C 13 172.675 0.144 . 1 . . . . 58 LYS C . 7003 1 188 . 1 1 44 44 LYS CA C 13 57.481 0.219 . 1 . . . . 58 LYS CA . 7003 1 189 . 1 1 44 44 LYS CB C 13 29.820 0.500 . 1 . . . . 58 LYS CB . 7003 1 190 . 1 1 44 44 LYS N N 15 117.469 0.500 . 1 . . . . 58 LYS N . 7003 1 191 . 1 1 45 45 ILE H H 1 7.241 0.002 . 1 . . . . 59 ILE H . 7003 1 192 . 1 1 45 45 ILE C C 13 176.134 0.071 . 1 . . . . 59 ILE C . 7003 1 193 . 1 1 45 45 ILE CA C 13 57.448 0.021 . 1 . . . . 59 ILE CA . 7003 1 194 . 1 1 45 45 ILE CB C 13 35.326 0.500 . 1 . . . . 59 ILE CB . 7003 1 195 . 1 1 45 45 ILE N N 15 117.143 0.500 . 1 . . . . 59 ILE N . 7003 1 196 . 1 1 46 46 ARG H H 1 8.462 0.100 . 1 . . . . 60 ARG H . 7003 1 197 . 1 1 46 46 ARG C C 13 172.634 0.103 . 1 . . . . 60 ARG C . 7003 1 198 . 1 1 46 46 ARG CA C 13 57.382 0.021 . 1 . . . . 60 ARG CA . 7003 1 199 . 1 1 46 46 ARG CB C 13 27.084 0.500 . 1 . . . . 60 ARG CB . 7003 1 200 . 1 1 46 46 ARG N N 15 127.098 0.500 . 1 . . . . 60 ARG N . 7003 1 201 . 1 1 47 47 TYR H H 1 8.569 0.100 . 1 . . . . 61 TYR H . 7003 1 202 . 1 1 47 47 TYR C C 13 172.514 0.035 . 1 . . . . 61 TYR C . 7003 1 203 . 1 1 47 47 TYR CA C 13 58.404 0.500 . 1 . . . . 61 TYR CA . 7003 1 204 . 1 1 47 47 TYR CB C 13 34.864 0.087 . 1 . . . . 61 TYR CB . 7003 1 205 . 1 1 47 47 TYR N N 15 118.627 0.500 . 1 . . . . 61 TYR N . 7003 1 206 . 1 1 48 48 GLU H H 1 7.986 0.100 . 1 . . . . 62 GLU H . 7003 1 207 . 1 1 48 48 GLU C C 13 172.445 0.051 . 1 . . . . 62 GLU C . 7003 1 208 . 1 1 48 48 GLU CA C 13 57.382 0.500 . 1 . . . . 62 GLU CA . 7003 1 209 . 1 1 48 48 GLU CB C 13 26.919 0.500 . 1 . . . . 62 GLU CB . 7003 1 210 . 1 1 48 48 GLU N N 15 119.380 0.500 . 1 . . . . 62 GLU N . 7003 1 211 . 1 1 49 49 THR H H 1 8.193 0.005 . 1 . . . . 63 THR H . 7003 1 212 . 1 1 49 49 THR C C 13 177.336 0.093 . 1 . . . . 63 THR C . 7003 1 213 . 1 1 49 49 THR CA C 13 57.481 0.087 . 1 . . . . 63 THR CA . 7003 1 214 . 1 1 49 49 THR CB C 13 60.975 0.087 . 1 . . . . 63 THR CB . 7003 1 215 . 1 1 49 49 THR N N 15 114.367 0.500 . 1 . . . . 63 THR N . 7003 1 216 . 1 1 50 50 LEU H H 1 7.252 0.003 . 1 . . . . 64 LEU H . 7003 1 217 . 1 1 50 50 LEU C C 13 173.060 0.500 . 1 . . . . 64 LEU C . 7003 1 218 . 1 1 50 50 LEU CA C 13 54.557 0.500 . 1 . . . . 64 LEU CA . 7003 1 219 . 1 1 50 50 LEU CB C 13 38.337 0.500 . 1 . . . . 64 LEU CB . 7003 1 220 . 1 1 50 50 LEU N N 15 121.886 0.500 . 1 . . . . 64 LEU N . 7003 1 221 . 1 1 51 51 THR C C 13 177.685 0.500 . 1 . . . . 65 THR C . 7003 1 222 . 1 1 51 51 THR CA C 13 59.482 0.500 . 1 . . . . 65 THR CA . 7003 1 223 . 1 1 51 51 THR CB C 13 66.735 0.500 . 1 . . . . 65 THR CB . 7003 1 224 . 1 1 52 52 ASP H H 1 7.197 0.004 . 1 . . . . 66 ASP H . 7003 1 225 . 1 1 52 52 ASP C C 13 178.831 0.500 . 1 . . . . 66 ASP C . 7003 1 226 . 1 1 52 52 ASP CA C 13 48.557 0.500 . 1 . . . . 66 ASP CA . 7003 1 227 . 1 1 52 52 ASP CB C 13 38.403 0.500 . 1 . . . . 66 ASP CB . 7003 1 228 . 1 1 52 52 ASP N N 15 118.098 0.500 . 1 . . . . 66 ASP N . 7003 1 229 . 1 1 53 53 PRO C C 13 173.393 0.500 . 1 . . . . 67 PRO C . 7003 1 230 . 1 1 53 53 PRO CA C 13 61.790 0.500 . 1 . . . . 67 PRO CA . 7003 1 231 . 1 1 53 53 PRO CB C 13 28.887 0.500 . 1 . . . . 67 PRO CB . 7003 1 232 . 1 1 54 54 SER H H 1 7.939 0.100 . 1 . . . . 68 SER H . 7003 1 233 . 1 1 54 54 SER C C 13 175.364 0.077 . 1 . . . . 68 SER C . 7003 1 234 . 1 1 54 54 SER CA C 13 58.239 0.153 . 1 . . . . 68 SER CA . 7003 1 235 . 1 1 54 54 SER CB C 13 60.316 0.219 . 1 . . . . 68 SER CB . 7003 1 236 . 1 1 54 54 SER N N 15 115.378 0.500 . 1 . . . . 68 SER N . 7003 1 237 . 1 1 55 55 LYS H H 1 7.729 0.002 . 1 . . . . 69 LYS H . 7003 1 238 . 1 1 55 55 LYS C C 13 175.487 0.090 . 1 . . . . 69 LYS C . 7003 1 239 . 1 1 55 55 LYS CA C 13 54.942 0.153 . 1 . . . . 69 LYS CA . 7003 1 240 . 1 1 55 55 LYS CB C 13 29.358 0.021 . 1 . . . . 69 LYS CB . 7003 1 241 . 1 1 55 55 LYS N N 15 123.309 0.500 . 1 . . . . 69 LYS N . 7003 1 242 . 1 1 56 56 LEU H H 1 7.106 0.004 . 1 . . . . 70 LEU H . 7003 1 243 . 1 1 56 56 LEU C C 13 173.784 0.134 . 1 . . . . 70 LEU C . 7003 1 244 . 1 1 56 56 LEU CA C 13 51.151 0.500 . 1 . . . . 70 LEU CA . 7003 1 245 . 1 1 56 56 LEU CB C 13 37.370 0.219 . 1 . . . . 70 LEU CB . 7003 1 246 . 1 1 56 56 LEU N N 15 111.739 0.500 . 1 . . . . 70 LEU N . 7003 1 247 . 1 1 57 57 ASP H H 1 7.895 0.001 . 1 . . . . 71 ASP H . 7003 1 248 . 1 1 57 57 ASP C C 13 175.150 0.087 . 1 . . . . 71 ASP C . 7003 1 249 . 1 1 57 57 ASP CA C 13 54.843 0.500 . 1 . . . . 71 ASP CA . 7003 1 250 . 1 1 57 57 ASP CB C 13 36.513 0.500 . 1 . . . . 71 ASP CB . 7003 1 251 . 1 1 57 57 ASP N N 15 123.641 0.500 . 1 . . . . 71 ASP N . 7003 1 252 . 1 1 58 58 SER H H 1 7.336 0.100 . 1 . . . . 72 SER H . 7003 1 253 . 1 1 58 58 SER C C 13 177.648 0.107 . 1 . . . . 72 SER C . 7003 1 254 . 1 1 58 58 SER CA C 13 54.250 0.219 . 1 . . . . 72 SER CA . 7003 1 255 . 1 1 58 58 SER CB C 13 59.854 0.087 . 1 . . . . 72 SER CB . 7003 1 256 . 1 1 58 58 SER N N 15 109.174 0.500 . 1 . . . . 72 SER N . 7003 1 257 . 1 1 59 59 GLY H H 1 7.538 0.001 . 1 . . . . 73 GLY H . 7003 1 258 . 1 1 59 59 GLY C C 13 177.743 0.500 . 1 . . . . 73 GLY C . 7003 1 259 . 1 1 59 59 GLY CA C 13 43.876 0.500 . 1 . . . . 73 GLY CA . 7003 1 260 . 1 1 59 59 GLY N N 15 111.545 0.500 . 1 . . . . 73 GLY N . 7003 1 261 . 1 1 60 60 LYS C C 13 176.516 0.500 . 1 . . . . 74 LYS C . 7003 1 262 . 1 1 60 60 LYS CA C 13 54.932 0.500 . 1 . . . . 74 LYS CA . 7003 1 263 . 1 1 60 60 LYS CB C 13 30.403 0.500 . 1 . . . . 74 LYS CB . 7003 1 264 . 1 1 61 61 GLU H H 1 7.505 0.100 . 1 . . . . 75 GLU H . 7003 1 265 . 1 1 61 61 GLU C C 13 175.274 0.500 . 1 . . . . 75 GLU C . 7003 1 266 . 1 1 61 61 GLU CA C 13 53.832 0.500 . 1 . . . . 75 GLU CA . 7003 1 267 . 1 1 61 61 GLU CB C 13 26.732 0.500 . 1 . . . . 75 GLU CB . 7003 1 268 . 1 1 61 61 GLU N N 15 116.828 0.500 . 1 . . . . 75 GLU N . 7003 1 269 . 1 1 62 62 LEU C C 13 178.862 0.500 . 1 . . . . 76 LEU C . 7003 1 270 . 1 1 62 62 LEU CA C 13 51.174 0.500 . 1 . . . . 76 LEU CA . 7003 1 271 . 1 1 62 62 LEU CB C 13 37.722 0.500 . 1 . . . . 76 LEU CB . 7003 1 272 . 1 1 63 63 HIS H H 1 7.537 0.004 . 1 . . . . 77 HIS H . 7003 1 273 . 1 1 63 63 HIS C C 13 179.847 0.170 . 1 . . . . 77 HIS C . 7003 1 274 . 1 1 63 63 HIS CA C 13 52.041 0.500 . 1 . . . . 77 HIS CA . 7003 1 275 . 1 1 63 63 HIS CB C 13 30.249 0.218 . 1 . . . . 77 HIS CB . 7003 1 276 . 1 1 63 63 HIS N N 15 119.245 0.500 . 1 . . . . 77 HIS N . 7003 1 277 . 1 1 64 64 ILE H H 1 8.027 0.001 . 1 . . . . 78 ILE H . 7003 1 278 . 1 1 64 64 ILE C C 13 177.351 0.063 . 1 . . . . 78 ILE C . 7003 1 279 . 1 1 64 64 ILE CA C 13 57.613 0.500 . 1 . . . . 78 ILE CA . 7003 1 280 . 1 1 64 64 ILE CB C 13 37.930 0.021 . 1 . . . . 78 ILE CB . 7003 1 281 . 1 1 64 64 ILE N N 15 117.548 0.500 . 1 . . . . 78 ILE N . 7003 1 282 . 1 1 65 65 ASN H H 1 9.622 0.003 . 1 . . . . 79 ASN H . 7003 1 283 . 1 1 65 65 ASN C C 13 178.987 0.072 . 1 . . . . 79 ASN C . 7003 1 284 . 1 1 65 65 ASN CA C 13 48.381 0.087 . 1 . . . . 79 ASN CA . 7003 1 285 . 1 1 65 65 ASN CB C 13 39.315 0.021 . 1 . . . . 79 ASN CB . 7003 1 286 . 1 1 65 65 ASN N N 15 125.259 0.500 . 1 . . . . 79 ASN N . 7003 1 287 . 1 1 66 66 LEU H H 1 8.908 0.004 . 1 . . . . 80 LEU H . 7003 1 288 . 1 1 66 66 LEU C C 13 176.264 0.025 . 1 . . . . 80 LEU C . 7003 1 289 . 1 1 66 66 LEU CA C 13 50.656 0.500 . 1 . . . . 80 LEU CA . 7003 1 290 . 1 1 66 66 LEU CB C 13 41.524 0.087 . 1 . . . . 80 LEU CB . 7003 1 291 . 1 1 66 66 LEU N N 15 122.313 0.500 . 1 . . . . 80 LEU N . 7003 1 292 . 1 1 67 67 ILE H H 1 9.206 0.004 . 1 . . . . 81 ILE H . 7003 1 293 . 1 1 67 67 ILE C C 13 177.090 0.500 . 1 . . . . 81 ILE C . 7003 1 294 . 1 1 67 67 ILE CA C 13 56.206 0.500 . 1 . . . . 81 ILE CA . 7003 1 295 . 1 1 67 67 ILE CB C 13 38.667 0.500 . 1 . . . . 81 ILE CB . 7003 1 296 . 1 1 67 67 ILE N N 15 120.166 0.500 . 1 . . . . 81 ILE N . 7003 1 297 . 1 1 68 68 PRO C C 13 176.847 0.500 . 1 . . . . 82 PRO C . 7003 1 298 . 1 1 68 68 PRO CA C 13 59.482 0.500 . 1 . . . . 82 PRO CA . 7003 1 299 . 1 1 68 68 PRO CB C 13 30.272 0.500 . 1 . . . . 82 PRO CB . 7003 1 300 . 1 1 69 69 ASN H H 1 9.032 0.006 . 1 . . . . 83 ASN H . 7003 1 301 . 1 1 69 69 ASN C C 13 176.816 0.500 . 1 . . . . 83 ASN C . 7003 1 302 . 1 1 69 69 ASN CA C 13 49.876 0.500 . 1 . . . . 83 ASN CA . 7003 1 303 . 1 1 69 69 ASN CB C 13 37.018 0.500 . 1 . . . . 83 ASN CB . 7003 1 304 . 1 1 69 69 ASN N N 15 121.717 0.500 . 1 . . . . 83 ASN N . 7003 1 305 . 1 1 70 70 LYS C C 13 173.993 0.500 . 1 . . . . 84 LYS C . 7003 1 306 . 1 1 70 70 LYS CA C 13 56.844 0.500 . 1 . . . . 84 LYS CA . 7003 1 307 . 1 1 70 70 LYS CB C 13 29.678 0.500 . 1 . . . . 84 LYS CB . 7003 1 308 . 1 1 71 71 GLN H H 1 8.351 0.002 . 1 . . . . 85 GLN H . 7003 1 309 . 1 1 71 71 GLN C C 13 174.721 0.083 . 1 . . . . 85 GLN C . 7003 1 310 . 1 1 71 71 GLN CA C 13 56.294 0.219 . 1 . . . . 85 GLN CA . 7003 1 311 . 1 1 71 71 GLN CB C 13 25.204 0.021 . 1 . . . . 85 GLN CB . 7003 1 312 . 1 1 71 71 GLN N N 15 119.885 0.500 . 1 . . . . 85 GLN N . 7003 1 313 . 1 1 72 72 ASP H H 1 7.638 0.001 . 1 . . . . 86 ASP H . 7003 1 314 . 1 1 72 72 ASP C C 13 177.007 0.046 . 1 . . . . 86 ASP C . 7003 1 315 . 1 1 72 72 ASP CA C 13 51.085 0.500 . 1 . . . . 86 ASP CA . 7003 1 316 . 1 1 72 72 ASP CB C 13 37.996 0.153 . 1 . . . . 86 ASP CB . 7003 1 317 . 1 1 72 72 ASP N N 15 116.795 0.500 . 1 . . . . 86 ASP N . 7003 1 318 . 1 1 73 73 ARG H H 1 7.800 0.001 . 1 . . . . 87 ARG H . 7003 1 319 . 1 1 73 73 ARG C C 13 177.855 0.185 . 1 . . . . 87 ARG C . 7003 1 320 . 1 1 73 73 ARG CA C 13 54.415 0.500 . 1 . . . . 87 ARG CA . 7003 1 321 . 1 1 73 73 ARG CB C 13 26.655 0.021 . 1 . . . . 87 ARG CB . 7003 1 322 . 1 1 73 73 ARG N N 15 120.605 0.500 . 1 . . . . 87 ARG N . 7003 1 323 . 1 1 74 74 THR H H 1 7.898 0.001 . 1 . . . . 88 THR H . 7003 1 324 . 1 1 74 74 THR C C 13 179.315 0.022 . 1 . . . . 88 THR C . 7003 1 325 . 1 1 74 74 THR CA C 13 55.140 0.500 . 1 . . . . 88 THR CA . 7003 1 326 . 1 1 74 74 THR CB C 13 69.877 0.500 . 1 . . . . 88 THR CB . 7003 1 327 . 1 1 74 74 THR N N 15 106.258 0.500 . 1 . . . . 88 THR N . 7003 1 328 . 1 1 75 75 LEU H H 1 8.317 0.002 . 1 . . . . 89 LEU H . 7003 1 329 . 1 1 75 75 LEU C C 13 178.035 0.087 . 1 . . . . 89 LEU C . 7003 1 330 . 1 1 75 75 LEU CA C 13 51.052 0.500 . 1 . . . . 89 LEU CA . 7003 1 331 . 1 1 75 75 LEU CB C 13 42.282 0.021 . 1 . . . . 89 LEU CB . 7003 1 332 . 1 1 75 75 LEU N N 15 122.336 0.500 . 1 . . . . 89 LEU N . 7003 1 333 . 1 1 76 76 THR H H 1 7.917 0.001 . 1 . . . . 90 THR H . 7003 1 334 . 1 1 76 76 THR C C 13 179.108 0.187 . 1 . . . . 90 THR C . 7003 1 335 . 1 1 76 76 THR CA C 13 58.997 0.500 . 1 . . . . 90 THR CA . 7003 1 336 . 1 1 76 76 THR CB C 13 67.108 0.086 . 1 . . . . 90 THR CB . 7003 1 337 . 1 1 76 76 THR N N 15 124.217 0.500 . 1 . . . . 90 THR N . 7003 1 338 . 1 1 77 77 ILE H H 1 9.336 0.002 . 1 . . . . 91 ILE H . 7003 1 339 . 1 1 77 77 ILE C C 13 177.095 0.074 . 1 . . . . 91 ILE C . 7003 1 340 . 1 1 77 77 ILE CA C 13 57.711 0.021 . 1 . . . . 91 ILE CA . 7003 1 341 . 1 1 77 77 ILE CB C 13 37.106 0.500 . 1 . . . . 91 ILE CB . 7003 1 342 . 1 1 77 77 ILE N N 15 127.895 0.500 . 1 . . . . 91 ILE N . 7003 1 343 . 1 1 78 78 VAL H H 1 9.532 0.005 . 1 . . . . 92 VAL H . 7003 1 344 . 1 1 78 78 VAL C C 13 178.332 0.026 . 1 . . . . 92 VAL C . 7003 1 345 . 1 1 78 78 VAL CA C 13 57.810 0.500 . 1 . . . . 92 VAL CA . 7003 1 346 . 1 1 78 78 VAL CB C 13 32.095 0.500 . 1 . . . . 92 VAL CB . 7003 1 347 . 1 1 78 78 VAL N N 15 129.906 0.500 . 1 . . . . 92 VAL N . 7003 1 348 . 1 1 79 79 ASP H H 1 9.353 0.001 . 1 . . . . 93 ASP H . 7003 1 349 . 1 1 79 79 ASP C C 13 176.319 0.149 . 1 . . . . 93 ASP C . 7003 1 350 . 1 1 79 79 ASP CA C 13 50.059 0.161 . 1 . . . . 93 ASP CA . 7003 1 351 . 1 1 79 79 ASP CB C 13 43.667 0.021 . 1 . . . . 93 ASP CB . 7003 1 352 . 1 1 79 79 ASP N N 15 123.371 0.500 . 1 . . . . 93 ASP N . 7003 1 353 . 1 1 80 80 THR H H 1 7.134 0.008 . 1 . . . . 94 THR H . 7003 1 354 . 1 1 80 80 THR C C 13 177.594 0.091 . 1 . . . . 94 THR C . 7003 1 355 . 1 1 80 80 THR CA C 13 56.162 0.500 . 1 . . . . 94 THR CA . 7003 1 356 . 1 1 80 80 THR CB C 13 63.415 0.500 . 1 . . . . 94 THR CB . 7003 1 357 . 1 1 80 80 THR N N 15 109.299 0.500 . 1 . . . . 94 THR N . 7003 1 358 . 1 1 81 81 GLY H H 1 9.432 0.002 . 1 . . . . 95 GLY H . 7003 1 359 . 1 1 81 81 GLY C C 13 180.181 0.117 . 1 . . . . 95 GLY C . 7003 1 360 . 1 1 81 81 GLY CA C 13 41.821 0.021 . 1 . . . . 95 GLY CA . 7003 1 361 . 1 1 81 81 GLY N N 15 108.907 0.500 . 1 . . . . 95 GLY N . 7003 1 362 . 1 1 82 82 ILE H H 1 6.732 0.001 . 1 . . . . 96 ILE H . 7003 1 363 . 1 1 82 82 ILE C C 13 179.203 0.134 . 1 . . . . 96 ILE C . 7003 1 364 . 1 1 82 82 ILE CA C 13 59.887 0.021 . 1 . . . . 96 ILE CA . 7003 1 365 . 1 1 82 82 ILE CB C 13 37.667 0.021 . 1 . . . . 96 ILE CB . 7003 1 366 . 1 1 82 82 ILE N N 15 115.862 0.500 . 1 . . . . 96 ILE N . 7003 1 367 . 1 1 83 83 GLY H H 1 7.559 0.002 . 1 . . . . 97 GLY H . 7003 1 368 . 1 1 83 83 GLY C C 13 179.237 0.312 . 1 . . . . 97 GLY C . 7003 1 369 . 1 1 83 83 GLY CA C 13 41.095 0.021 . 1 . . . . 97 GLY CA . 7003 1 370 . 1 1 83 83 GLY N N 15 103.655 0.500 . 1 . . . . 97 GLY N . 7003 1 371 . 1 1 84 84 MET H H 1 7.576 0.001 . 1 . . . . 98 MET H . 7003 1 372 . 1 1 84 84 MET C C 13 177.310 0.104 . 1 . . . . 98 MET C . 7003 1 373 . 1 1 84 84 MET CA C 13 52.634 0.021 . 1 . . . . 98 MET CA . 7003 1 374 . 1 1 84 84 MET CB C 13 34.699 0.021 . 1 . . . . 98 MET CB . 7003 1 375 . 1 1 84 84 MET N N 15 117.000 0.500 . 1 . . . . 98 MET N . 7003 1 376 . 1 1 85 85 THR H H 1 7.951 0.005 . 1 . . . . 99 THR H . 7003 1 377 . 1 1 85 85 THR C C 13 178.340 0.118 . 1 . . . . 99 THR C . 7003 1 378 . 1 1 85 85 THR CA C 13 58.272 0.087 . 1 . . . . 99 THR CA . 7003 1 379 . 1 1 85 85 THR CB C 13 67.866 0.500 . 1 . . . . 99 THR CB . 7003 1 380 . 1 1 85 85 THR N N 15 112.315 0.500 . 1 . . . . 99 THR N . 7003 1 381 . 1 1 86 86 LYS H H 1 8.515 0.007 . 1 . . . . 100 LYS H . 7003 1 382 . 1 1 86 86 LYS C C 13 174.345 0.035 . 1 . . . . 100 LYS C . 7003 1 383 . 1 1 86 86 LYS CA C 13 58.206 0.087 . 1 . . . . 100 LYS CA . 7003 1 384 . 1 1 86 86 LYS CB C 13 28.468 0.500 . 1 . . . . 100 LYS CB . 7003 1 385 . 1 1 86 86 LYS N N 15 121.133 0.500 . 1 . . . . 100 LYS N . 7003 1 386 . 1 1 87 87 ALA H H 1 7.753 0.001 . 1 . . . . 101 ALA H . 7003 1 387 . 1 1 87 87 ALA C C 13 172.521 0.082 . 1 . . . . 101 ALA C . 7003 1 388 . 1 1 87 87 ALA CA C 13 51.975 0.500 . 1 . . . . 101 ALA CA . 7003 1 389 . 1 1 87 87 ALA CB C 13 15.050 0.021 . 1 . . . . 101 ALA CB . 7003 1 390 . 1 1 87 87 ALA N N 15 116.705 0.500 . 1 . . . . 101 ALA N . 7003 1 391 . 1 1 88 88 ASP H H 1 7.292 0.001 . 1 . . . . 102 ASP H . 7003 1 392 . 1 1 88 88 ASP C C 13 174.360 0.125 . 1 . . . . 102 ASP C . 7003 1 393 . 1 1 88 88 ASP CA C 13 54.448 0.218 . 1 . . . . 102 ASP CA . 7003 1 394 . 1 1 88 88 ASP CB C 13 37.667 0.152 . 1 . . . . 102 ASP CB . 7003 1 395 . 1 1 88 88 ASP N N 15 117.593 0.500 . 1 . . . . 102 ASP N . 7003 1 396 . 1 1 89 89 LEU H H 1 8.045 0.005 . 1 . . . . 103 LEU H . 7003 1 397 . 1 1 89 89 LEU C C 13 174.721 0.268 . 1 . . . . 103 LEU C . 7003 1 398 . 1 1 89 89 LEU CA C 13 55.173 0.500 . 1 . . . . 103 LEU CA . 7003 1 399 . 1 1 89 89 LEU CB C 13 40.106 0.153 . 1 . . . . 103 LEU CB . 7003 1 400 . 1 1 89 89 LEU N N 15 121.459 0.500 . 1 . . . . 103 LEU N . 7003 1 401 . 1 1 90 90 ILE H H 1 7.472 0.004 . 1 . . . . 104 ILE H . 7003 1 402 . 1 1 90 90 ILE C C 13 173.380 0.242 . 1 . . . . 104 ILE C . 7003 1 403 . 1 1 90 90 ILE CA C 13 62.030 0.500 . 1 . . . . 104 ILE CA . 7003 1 404 . 1 1 90 90 ILE CB C 13 35.853 0.500 . 1 . . . . 104 ILE CB . 7003 1 405 . 1 1 90 90 ILE N N 15 116.042 0.500 . 1 . . . . 104 ILE N . 7003 1 406 . 1 1 91 91 ASN H H 1 8.208 0.009 . 1 . . . . 105 ASN H . 7003 1 407 . 1 1 91 91 ASN C C 13 174.920 0.184 . 1 . . . . 105 ASN C . 7003 1 408 . 1 1 91 91 ASN CA C 13 52.634 0.021 . 1 . . . . 105 ASN CA . 7003 1 409 . 1 1 91 91 ASN CB C 13 35.886 0.500 . 1 . . . . 105 ASN CB . 7003 1 410 . 1 1 91 91 ASN N N 15 117.683 0.500 . 1 . . . . 105 ASN N . 7003 1 411 . 1 1 92 92 ASN H H 1 8.641 0.006 . 1 . . . . 106 ASN H . 7003 1 412 . 1 1 92 92 ASN C C 13 176.259 0.500 . 1 . . . . 106 ASN C . 7003 1 413 . 1 1 92 92 ASN CA C 13 52.184 0.500 . 1 . . . . 106 ASN CA . 7003 1 414 . 1 1 92 92 ASN CB C 13 35.436 0.500 . 1 . . . . 106 ASN CB . 7003 1 415 . 1 1 92 92 ASN N N 15 116.278 0.500 . 1 . . . . 106 ASN N . 7003 1 416 . 1 1 102 102 LYS C C 13 173.947 0.500 . 1 . . . . 116 LYS C . 7003 1 417 . 1 1 102 102 LYS CA C 13 56.976 0.500 . 1 . . . . 116 LYS CA . 7003 1 418 . 1 1 102 102 LYS CB C 13 28.953 0.500 . 1 . . . . 116 LYS CB . 7003 1 419 . 1 1 103 103 ALA H H 1 7.773 0.001 . 1 . . . . 117 ALA H . 7003 1 420 . 1 1 103 103 ALA C C 13 171.740 0.085 . 1 . . . . 117 ALA C . 7003 1 421 . 1 1 103 103 ALA CA C 13 52.074 0.500 . 1 . . . . 117 ALA CA . 7003 1 422 . 1 1 103 103 ALA CB C 13 15.248 0.021 . 1 . . . . 117 ALA CB . 7003 1 423 . 1 1 103 103 ALA N N 15 120.719 0.500 . 1 . . . . 117 ALA N . 7003 1 424 . 1 1 104 104 PHE H H 1 8.215 0.100 . 1 . . . . 118 PHE H . 7003 1 425 . 1 1 104 104 PHE C C 13 175.893 0.139 . 1 . . . . 118 PHE C . 7003 1 426 . 1 1 104 104 PHE CA C 13 56.590 0.021 . 1 . . . . 118 PHE CA . 7003 1 427 . 1 1 104 104 PHE CB C 13 35.161 0.153 . 1 . . . . 118 PHE CB . 7003 1 428 . 1 1 104 104 PHE N N 15 120.121 0.500 . 1 . . . . 118 PHE N . 7003 1 429 . 1 1 105 105 MET H H 1 7.738 0.007 . 1 . . . . 119 MET H . 7003 1 430 . 1 1 105 105 MET C C 13 173.364 0.088 . 1 . . . . 119 MET C . 7003 1 431 . 1 1 105 105 MET CA C 13 57.019 0.500 . 1 . . . . 119 MET CA . 7003 1 432 . 1 1 105 105 MET CB C 13 29.556 0.021 . 1 . . . . 119 MET CB . 7003 1 433 . 1 1 105 105 MET N N 15 117.447 0.500 . 1 . . . . 119 MET N . 7003 1 434 . 1 1 106 106 GLU H H 1 7.970 0.006 . 1 . . . . 120 GLU H . 7003 1 435 . 1 1 106 106 GLU C C 13 172.997 0.500 . 1 . . . . 120 GLU C . 7003 1 436 . 1 1 106 106 GLU CA C 13 56.656 0.021 . 1 . . . . 120 GLU CA . 7003 1 437 . 1 1 106 106 GLU CB C 13 26.128 0.152 . 1 . . . . 120 GLU CB . 7003 1 438 . 1 1 106 106 GLU N N 15 118.672 0.500 . 1 . . . . 120 GLU N . 7003 1 439 . 1 1 107 107 ALA H H 1 7.674 0.002 . 1 . . . . 121 ALA H . 7003 1 440 . 1 1 107 107 ALA C C 13 171.247 0.036 . 1 . . . . 121 ALA C . 7003 1 441 . 1 1 107 107 ALA CA C 13 52.338 0.500 . 1 . . . . 121 ALA CA . 7003 1 442 . 1 1 107 107 ALA CB C 13 13.830 0.500 . 1 . . . . 121 ALA CB . 7003 1 443 . 1 1 107 107 ALA N N 15 124.180 0.500 . 1 . . . . 121 ALA N . 7003 1 444 . 1 1 108 108 LEU H H 1 8.197 0.001 . 1 . . . . 122 LEU H . 7003 1 445 . 1 1 108 108 LEU C C 13 170.750 0.067 . 1 . . . . 122 LEU C . 7003 1 446 . 1 1 108 108 LEU CA C 13 54.909 0.087 . 1 . . . . 122 LEU CA . 7003 1 447 . 1 1 108 108 LEU CB C 13 38.293 0.087 . 1 . . . . 122 LEU CB . 7003 1 448 . 1 1 108 108 LEU N N 15 120.188 0.500 . 1 . . . . 122 LEU N . 7003 1 449 . 1 1 109 109 GLN H H 1 7.701 0.002 . 1 . . . . 123 GLN H . 7003 1 450 . 1 1 109 109 GLN C C 13 175.632 0.076 . 1 . . . . 123 GLN C . 7003 1 451 . 1 1 109 109 GLN CA C 13 55.569 0.500 . 1 . . . . 123 GLN CA . 7003 1 452 . 1 1 109 109 GLN CB C 13 25.303 0.500 . 1 . . . . 123 GLN CB . 7003 1 453 . 1 1 109 109 GLN N N 15 119.515 0.500 . 1 . . . . 123 GLN N . 7003 1 454 . 1 1 110 110 ALA H H 1 7.281 0.001 . 1 . . . . 124 ALA H . 7003 1 455 . 1 1 110 110 ALA C C 13 174.805 0.069 . 1 . . . . 124 ALA C . 7003 1 456 . 1 1 110 110 ALA CA C 13 49.107 0.500 . 1 . . . . 124 ALA CA . 7003 1 457 . 1 1 110 110 ALA CB C 13 15.940 0.087 . 1 . . . . 124 ALA CB . 7003 1 458 . 1 1 110 110 ALA N N 15 120.391 0.500 . 1 . . . . 124 ALA N . 7003 1 459 . 1 1 111 111 GLY H H 1 7.539 0.100 . 1 . . . . 125 GLY H . 7003 1 460 . 1 1 111 111 GLY C C 13 177.474 0.245 . 1 . . . . 125 GLY C . 7003 1 461 . 1 1 111 111 GLY CA C 13 42.612 0.500 . 1 . . . . 125 GLY CA . 7003 1 462 . 1 1 111 111 GLY N N 15 106.137 0.500 . 1 . . . . 125 GLY N . 7003 1 463 . 1 1 112 112 ALA H H 1 7.988 0.001 . 1 . . . . 126 ALA H . 7003 1 464 . 1 1 112 112 ALA C C 13 176.882 0.131 . 1 . . . . 126 ALA C . 7003 1 465 . 1 1 112 112 ALA CA C 13 49.667 0.021 . 1 . . . . 126 ALA CA . 7003 1 466 . 1 1 112 112 ALA CB C 13 16.468 0.500 . 1 . . . . 126 ALA CB . 7003 1 467 . 1 1 112 112 ALA N N 15 123.395 0.500 . 1 . . . . 126 ALA N . 7003 1 468 . 1 1 113 113 ASP H H 1 8.040 0.003 . 1 . . . . 127 ASP H . 7003 1 469 . 1 1 113 113 ASP C C 13 175.247 0.097 . 1 . . . . 127 ASP C . 7003 1 470 . 1 1 113 113 ASP CA C 13 51.217 0.087 . 1 . . . . 127 ASP CA . 7003 1 471 . 1 1 113 113 ASP CB C 13 41.392 0.219 . 1 . . . . 127 ASP CB . 7003 1 472 . 1 1 113 113 ASP N N 15 118.649 0.500 . 1 . . . . 127 ASP N . 7003 1 473 . 1 1 114 114 ILE H H 1 7.585 0.006 . 1 . . . . 128 ILE H . 7003 1 474 . 1 1 114 114 ILE C C 13 177.076 0.500 . 1 . . . . 128 ILE C . 7003 1 475 . 1 1 114 114 ILE CA C 13 58.997 0.500 . 1 . . . . 128 ILE CA . 7003 1 476 . 1 1 114 114 ILE CB C 13 35.095 0.021 . 1 . . . . 128 ILE CB . 7003 1 477 . 1 1 114 114 ILE N N 15 123.236 0.500 . 1 . . . . 128 ILE N . 7003 1 478 . 1 1 115 115 SER H H 1 8.430 0.003 . 1 . . . . 129 SER H . 7003 1 479 . 1 1 115 115 SER C C 13 176.514 0.202 . 1 . . . . 129 SER C . 7003 1 480 . 1 1 115 115 SER CA C 13 58.008 0.500 . 1 . . . . 129 SER CA . 7003 1 481 . 1 1 115 115 SER CB C 13 60.481 0.500 . 1 . . . . 129 SER CB . 7003 1 482 . 1 1 115 115 SER N N 15 114.535 0.500 . 1 . . . . 129 SER N . 7003 1 483 . 1 1 116 116 MET H H 1 7.859 0.002 . 1 . . . . 130 MET H . 7003 1 484 . 1 1 116 116 MET C C 13 175.943 0.169 . 1 . . . . 130 MET C . 7003 1 485 . 1 1 116 116 MET CA C 13 53.887 0.153 . 1 . . . . 130 MET CA . 7003 1 486 . 1 1 116 116 MET CB C 13 30.183 0.500 . 1 . . . . 130 MET CB . 7003 1 487 . 1 1 116 116 MET N N 15 120.188 0.500 . 1 . . . . 130 MET N . 7003 1 488 . 1 1 117 117 ILE H H 1 7.721 0.006 . 1 . . . . 131 ILE H . 7003 1 489 . 1 1 117 117 ILE C C 13 176.968 0.500 . 1 . . . . 131 ILE C . 7003 1 490 . 1 1 117 117 ILE CA C 13 62.338 0.500 . 1 . . . . 131 ILE CA . 7003 1 491 . 1 1 117 117 ILE CB C 13 34.381 0.500 . 1 . . . . 131 ILE CB . 7003 1 492 . 1 1 117 117 ILE N N 15 119.391 0.500 . 1 . . . . 131 ILE N . 7003 1 493 . 1 1 118 118 GLY C C 13 174.760 0.500 . 1 . . . . 132 GLY C . 7003 1 494 . 1 1 118 118 GLY CA C 13 44.052 0.500 . 1 . . . . 132 GLY CA . 7003 1 495 . 1 1 119 119 GLN H H 1 7.873 0.100 . 1 . . . . 133 GLN H . 7003 1 496 . 1 1 119 119 GLN C C 13 175.731 0.090 . 1 . . . . 133 GLN C . 7003 1 497 . 1 1 119 119 GLN CA C 13 54.349 0.500 . 1 . . . . 133 GLN CA . 7003 1 498 . 1 1 119 119 GLN CB C 13 24.875 0.021 . 1 . . . . 133 GLN CB . 7003 1 499 . 1 1 119 119 GLN N N 15 120.133 0.500 . 1 . . . . 133 GLN N . 7003 1 500 . 1 1 120 120 PHE H H 1 7.220 0.100 . 1 . . . . 134 PHE H . 7003 1 501 . 1 1 120 120 PHE C C 13 176.228 0.500 . 1 . . . . 134 PHE C . 7003 1 502 . 1 1 120 120 PHE CA C 13 55.305 0.500 . 1 . . . . 134 PHE CA . 7003 1 503 . 1 1 120 120 PHE CB C 13 37.348 0.500 . 1 . . . . 134 PHE CB . 7003 1 504 . 1 1 120 120 PHE N N 15 115.671 0.500 . 1 . . . . 134 PHE N . 7003 1 505 . 1 1 121 121 GLY H H 1 7.601 0.003 . 1 . . . . 135 GLY H . 7003 1 506 . 1 1 121 121 GLY C C 13 177.747 0.500 . 1 . . . . 135 GLY C . 7003 1 507 . 1 1 121 121 GLY CA C 13 44.128 0.021 . 1 . . . . 135 GLY CA . 7003 1 508 . 1 1 121 121 GLY N N 15 109.271 0.500 . 1 . . . . 135 GLY N . 7003 1 509 . 1 1 122 122 VAL H H 1 6.471 0.004 . 1 . . . . 136 VAL H . 7003 1 510 . 1 1 122 122 VAL C C 13 176.833 0.104 . 1 . . . . 136 VAL C . 7003 1 511 . 1 1 122 122 VAL CA C 13 57.118 0.021 . 1 . . . . 136 VAL CA . 7003 1 512 . 1 1 122 122 VAL CB C 13 28.172 0.500 . 1 . . . . 136 VAL CB . 7003 1 513 . 1 1 122 122 VAL N N 15 108.203 0.500 . 1 . . . . 136 VAL N . 7003 1 514 . 1 1 123 123 GLY H H 1 8.618 0.002 . 1 . . . . 137 GLY H . 7003 1 515 . 1 1 123 123 GLY C C 13 176.696 0.500 . 1 . . . . 137 GLY C . 7003 1 516 . 1 1 123 123 GLY CA C 13 44.997 0.500 . 1 . . . . 137 GLY CA . 7003 1 517 . 1 1 123 123 GLY N N 15 107.730 0.500 . 1 . . . . 137 GLY N . 7003 1 518 . 1 1 124 124 PHE C C 13 176.847 0.500 . 1 . . . . 138 PHE C . 7003 1 519 . 1 1 124 124 PHE CA C 13 54.075 0.500 . 1 . . . . 138 PHE CA . 7003 1 520 . 1 1 124 124 PHE CB C 13 35.283 0.500 . 1 . . . . 138 PHE CB . 7003 1 521 . 1 1 125 125 TYR H H 1 7.002 0.003 . 1 . . . . 139 TYR H . 7003 1 522 . 1 1 125 125 TYR C C 13 175.152 0.500 . 1 . . . . 139 TYR C . 7003 1 523 . 1 1 125 125 TYR CA C 13 56.667 0.500 . 1 . . . . 139 TYR CA . 7003 1 524 . 1 1 125 125 TYR CB C 13 33.458 0.500 . 1 . . . . 139 TYR CB . 7003 1 525 . 1 1 125 125 TYR N N 15 121.661 0.500 . 1 . . . . 139 TYR N . 7003 1 526 . 1 1 126 126 SER C C 13 177.079 0.500 . 1 . . . . 140 SER C . 7003 1 527 . 1 1 126 126 SER CA C 13 59.416 0.500 . 1 . . . . 140 SER CA . 7003 1 528 . 1 1 126 126 SER CB C 13 60.405 0.500 . 1 . . . . 140 SER CB . 7003 1 529 . 1 1 127 127 ALA H H 1 7.884 0.002 . 1 . . . . 141 ALA H . 7003 1 530 . 1 1 127 127 ALA C C 13 173.632 0.106 . 1 . . . . 141 ALA C . 7003 1 531 . 1 1 127 127 ALA CA C 13 52.436 0.021 . 1 . . . . 141 ALA CA . 7003 1 532 . 1 1 127 127 ALA CB C 13 15.611 0.086 . 1 . . . . 141 ALA CB . 7003 1 533 . 1 1 127 127 ALA N N 15 125.382 0.500 . 1 . . . . 141 ALA N . 7003 1 534 . 1 1 128 128 TYR H H 1 7.280 0.005 . 1 . . . . 142 TYR H . 7003 1 535 . 1 1 128 128 TYR C C 13 176.912 0.101 . 1 . . . . 142 TYR C . 7003 1 536 . 1 1 128 128 TYR CA C 13 58.305 0.153 . 1 . . . . 142 TYR CA . 7003 1 537 . 1 1 128 128 TYR CB C 13 33.644 0.500 . 1 . . . . 142 TYR CB . 7003 1 538 . 1 1 128 128 TYR N N 15 112.003 0.500 . 1 . . . . 142 TYR N . 7003 1 539 . 1 1 129 129 LEU H H 1 7.940 0.001 . 1 . . . . 143 LEU H . 7003 1 540 . 1 1 129 129 LEU C C 13 173.686 0.030 . 1 . . . . 143 LEU C . 7003 1 541 . 1 1 129 129 LEU CA C 13 54.942 0.153 . 1 . . . . 143 LEU CA . 7003 1 542 . 1 1 129 129 LEU CB C 13 40.469 0.087 . 1 . . . . 143 LEU CB . 7003 1 543 . 1 1 129 129 LEU N N 15 118.593 0.500 . 1 . . . . 143 LEU N . 7003 1 544 . 1 1 130 130 VAL H H 1 6.482 0.003 . 1 . . . . 144 VAL H . 7003 1 545 . 1 1 130 130 VAL C C 13 178.958 0.131 . 1 . . . . 144 VAL C . 7003 1 546 . 1 1 130 130 VAL CA C 13 57.415 0.500 . 1 . . . . 144 VAL CA . 7003 1 547 . 1 1 130 130 VAL CB C 13 30.512 0.087 . 1 . . . . 144 VAL CB . 7003 1 548 . 1 1 130 130 VAL N N 15 102.671 0.500 . 1 . . . . 144 VAL N . 7003 1 549 . 1 1 131 131 ALA H H 1 7.558 0.001 . 1 . . . . 145 ALA H . 7003 1 550 . 1 1 131 131 ALA C C 13 176.736 0.176 . 1 . . . . 145 ALA C . 7003 1 551 . 1 1 131 131 ALA CA C 13 48.019 0.021 . 1 . . . . 145 ALA CA . 7003 1 552 . 1 1 131 131 ALA CB C 13 18.808 0.021 . 1 . . . . 145 ALA CB . 7003 1 553 . 1 1 131 131 ALA N N 15 124.388 0.500 . 1 . . . . 145 ALA N . 7003 1 554 . 1 1 132 132 GLU H H 1 8.425 0.001 . 1 . . . . 146 GLU H . 7003 1 555 . 1 1 132 132 GLU C C 13 176.974 0.316 . 1 . . . . 146 GLU C . 7003 1 556 . 1 1 132 132 GLU CA C 13 53.129 0.087 . 1 . . . . 146 GLU CA . 7003 1 557 . 1 1 132 132 GLU CB C 13 27.908 0.021 . 1 . . . . 146 GLU CB . 7003 1 558 . 1 1 132 132 GLU N N 15 118.053 0.500 . 1 . . . . 146 GLU N . 7003 1 559 . 1 1 133 133 LYS H H 1 7.319 0.004 . 1 . . . . 147 LYS H . 7003 1 560 . 1 1 133 133 LYS C C 13 179.333 0.058 . 1 . . . . 147 LYS C . 7003 1 561 . 1 1 133 133 LYS CA C 13 53.030 0.153 . 1 . . . . 147 LYS CA . 7003 1 562 . 1 1 133 133 LYS CB C 13 32.392 0.500 . 1 . . . . 147 LYS CB . 7003 1 563 . 1 1 133 133 LYS N N 15 117.042 0.500 . 1 . . . . 147 LYS N . 7003 1 564 . 1 1 134 134 VAL H H 1 7.922 0.002 . 1 . . . . 148 VAL H . 7003 1 565 . 1 1 134 134 VAL C C 13 178.176 0.125 . 1 . . . . 148 VAL C . 7003 1 566 . 1 1 134 134 VAL CA C 13 58.766 0.021 . 1 . . . . 148 VAL CA . 7003 1 567 . 1 1 134 134 VAL CB C 13 32.425 0.500 . 1 . . . . 148 VAL CB . 7003 1 568 . 1 1 134 134 VAL N N 15 125.664 0.500 . 1 . . . . 148 VAL N . 7003 1 569 . 1 1 135 135 THR H H 1 8.976 0.002 . 1 . . . . 149 THR H . 7003 1 570 . 1 1 135 135 THR C C 13 179.029 0.061 . 1 . . . . 149 THR C . 7003 1 571 . 1 1 135 135 THR CA C 13 58.865 0.500 . 1 . . . . 149 THR CA . 7003 1 572 . 1 1 135 135 THR CB C 13 67.965 0.087 . 1 . . . . 149 THR CB . 7003 1 573 . 1 1 135 135 THR N N 15 124.916 0.500 . 1 . . . . 149 THR N . 7003 1 574 . 1 1 136 136 VAL H H 1 10.349 0.004 . 1 . . . . 150 VAL H . 7003 1 575 . 1 1 136 136 VAL C C 13 177.783 0.127 . 1 . . . . 150 VAL C . 7003 1 576 . 1 1 136 136 VAL CA C 13 58.371 0.021 . 1 . . . . 150 VAL CA . 7003 1 577 . 1 1 136 136 VAL CB C 13 31.435 0.500 . 1 . . . . 150 VAL CB . 7003 1 578 . 1 1 136 136 VAL N N 15 128.373 0.500 . 1 . . . . 150 VAL N . 7003 1 579 . 1 1 137 137 ILE H H 1 9.516 0.100 . 1 . . . . 151 ILE H . 7003 1 580 . 1 1 137 137 ILE C C 13 176.914 0.081 . 1 . . . . 151 ILE C . 7003 1 581 . 1 1 137 137 ILE CA C 13 56.294 0.500 . 1 . . . . 151 ILE CA . 7003 1 582 . 1 1 137 137 ILE CB C 13 36.183 0.500 . 1 . . . . 151 ILE CB . 7003 1 583 . 1 1 137 137 ILE N N 15 128.643 0.500 . 1 . . . . 151 ILE N . 7003 1 584 . 1 1 138 138 THR H H 1 9.072 0.002 . 1 . . . . 152 THR H . 7003 1 585 . 1 1 138 138 THR C C 13 175.901 0.500 . 1 . . . . 152 THR C . 7003 1 586 . 1 1 138 138 THR CA C 13 57.052 0.500 . 1 . . . . 152 THR CA . 7003 1 587 . 1 1 138 138 THR CB C 13 68.525 0.153 . 1 . . . . 152 THR CB . 7003 1 588 . 1 1 138 138 THR N N 15 122.133 0.500 . 1 . . . . 152 THR N . 7003 1 589 . 1 1 139 139 LYS H H 1 8.778 0.003 . 1 . . . . 153 LYS H . 7003 1 590 . 1 1 139 139 LYS C C 13 180.224 0.059 . 1 . . . . 153 LYS C . 7003 1 591 . 1 1 139 139 LYS CA C 13 52.107 0.021 . 1 . . . . 153 LYS CA . 7003 1 592 . 1 1 139 139 LYS CB C 13 33.809 0.500 . 1 . . . . 153 LYS CB . 7003 1 593 . 1 1 139 139 LYS N N 15 127.368 0.500 . 1 . . . . 153 LYS N . 7003 1 594 . 1 1 140 140 HIS H H 1 9.553 0.004 . 1 . . . . 154 HIS H . 7003 1 595 . 1 1 140 140 HIS C C 13 175.632 0.041 . 1 . . . . 154 HIS C . 7003 1 596 . 1 1 140 140 HIS CA C 13 51.711 0.285 . 1 . . . . 154 HIS CA . 7003 1 597 . 1 1 140 140 HIS CB C 13 31.996 0.153 . 1 . . . . 154 HIS CB . 7003 1 598 . 1 1 140 140 HIS N N 15 132.015 0.500 . 1 . . . . 154 HIS N . 7003 1 599 . 1 1 141 141 ASN H H 1 9.521 0.004 . 1 . . . . 155 ASN H . 7003 1 600 . 1 1 141 141 ASN C C 13 174.890 0.500 . 1 . . . . 155 ASN C . 7003 1 601 . 1 1 141 141 ASN CA C 13 53.371 0.500 . 1 . . . . 155 ASN CA . 7003 1 602 . 1 1 141 141 ASN CB C 13 35.633 0.500 . 1 . . . . 155 ASN CB . 7003 1 603 . 1 1 141 141 ASN N N 15 126.203 0.500 . 1 . . . . 155 ASN N . 7003 1 604 . 1 1 142 142 ASP C C 13 176.758 0.500 . 1 . . . . 156 ASP C . 7003 1 605 . 1 1 142 142 ASP CA C 13 52.031 0.500 . 1 . . . . 156 ASP CA . 7003 1 606 . 1 1 142 142 ASP CB C 13 37.920 0.500 . 1 . . . . 156 ASP CB . 7003 1 607 . 1 1 143 143 ASP H H 1 8.251 0.003 . 1 . . . . 157 ASP H . 7003 1 608 . 1 1 143 143 ASP C C 13 178.337 0.112 . 1 . . . . 157 ASP C . 7003 1 609 . 1 1 143 143 ASP CA C 13 49.960 0.079 . 1 . . . . 157 ASP CA . 7003 1 610 . 1 1 143 143 ASP CB C 13 43.238 0.087 . 1 . . . . 157 ASP CB . 7003 1 611 . 1 1 143 143 ASP N N 15 123.800 0.500 . 1 . . . . 157 ASP N . 7003 1 612 . 1 1 144 144 GLU H H 1 9.245 0.001 . 1 . . . . 158 GLU H . 7003 1 613 . 1 1 144 144 GLU C C 13 179.399 0.068 . 1 . . . . 158 GLU C . 7003 1 614 . 1 1 144 144 GLU CA C 13 51.645 0.153 . 1 . . . . 158 GLU CA . 7003 1 615 . 1 1 144 144 GLU CB C 13 27.842 0.021 . 1 . . . . 158 GLU CB . 7003 1 616 . 1 1 144 144 GLU N N 15 117.705 0.500 . 1 . . . . 158 GLU N . 7003 1 617 . 1 1 145 145 GLN H H 1 8.014 0.100 . 1 . . . . 159 GLN H . 7003 1 618 . 1 1 145 145 GLN C C 13 176.163 0.500 . 1 . . . . 159 GLN C . 7003 1 619 . 1 1 145 145 GLN CA C 13 53.459 0.500 . 1 . . . . 159 GLN CA . 7003 1 620 . 1 1 145 145 GLN CB C 13 27.743 0.087 . 1 . . . . 159 GLN CB . 7003 1 621 . 1 1 145 145 GLN N N 15 119.526 0.500 . 1 . . . . 159 GLN N . 7003 1 622 . 1 1 146 146 TYR H H 1 8.584 0.100 . 1 . . . . 160 TYR H . 7003 1 623 . 1 1 146 146 TYR C C 13 178.685 0.106 . 1 . . . . 160 TYR C . 7003 1 624 . 1 1 146 146 TYR CA C 13 55.799 0.500 . 1 . . . . 160 TYR CA . 7003 1 625 . 1 1 146 146 TYR CB C 13 42.051 0.500 . 1 . . . . 160 TYR CB . 7003 1 626 . 1 1 146 146 TYR N N 15 124.695 0.500 . 1 . . . . 160 TYR N . 7003 1 627 . 1 1 147 147 ALA H H 1 9.178 0.004 . 1 . . . . 161 ALA H . 7003 1 628 . 1 1 147 147 ALA C C 13 176.571 0.089 . 1 . . . . 161 ALA C . 7003 1 629 . 1 1 147 147 ALA CA C 13 47.788 0.219 . 1 . . . . 161 ALA CA . 7003 1 630 . 1 1 147 147 ALA CB C 13 18.940 0.500 . 1 . . . . 161 ALA CB . 7003 1 631 . 1 1 147 147 ALA N N 15 119.672 0.500 . 1 . . . . 161 ALA N . 7003 1 632 . 1 1 148 148 TRP H H 1 10.232 0.001 . 1 . . . . 162 TRP H . 7003 1 633 . 1 1 148 148 TRP C C 13 176.297 0.139 . 1 . . . . 162 TRP C . 7003 1 634 . 1 1 148 148 TRP CA C 13 52.667 0.087 . 1 . . . . 162 TRP CA . 7003 1 635 . 1 1 148 148 TRP CB C 13 33.216 0.087 . 1 . . . . 162 TRP CB . 7003 1 636 . 1 1 148 148 TRP N N 15 130.041 0.500 . 1 . . . . 162 TRP N . 7003 1 637 . 1 1 149 149 GLU H H 1 8.619 0.002 . 1 . . . . 163 GLU H . 7003 1 638 . 1 1 149 149 GLU C C 13 177.065 0.134 . 1 . . . . 163 GLU C . 7003 1 639 . 1 1 149 149 GLU CA C 13 53.590 0.087 . 1 . . . . 163 GLU CA . 7003 1 640 . 1 1 149 149 GLU CB C 13 31.600 0.021 . 1 . . . . 163 GLU CB . 7003 1 641 . 1 1 149 149 GLU N N 15 126.460 0.500 . 1 . . . . 163 GLU N . 7003 1 642 . 1 1 150 150 SER H H 1 8.164 0.002 . 1 . . . . 164 SER H . 7003 1 643 . 1 1 150 150 SER C C 13 175.320 0.500 . 1 . . . . 164 SER C . 7003 1 644 . 1 1 150 150 SER CA C 13 56.997 0.500 . 1 . . . . 164 SER CA . 7003 1 645 . 1 1 150 150 SER CB C 13 63.723 0.500 . 1 . . . . 164 SER CB . 7003 1 646 . 1 1 150 150 SER N N 15 113.704 0.500 . 1 . . . . 164 SER N . 7003 1 647 . 1 1 154 154 GLY C C 13 177.839 0.500 . 1 . . . . 168 GLY C . 7003 1 648 . 1 1 154 154 GLY CA C 13 43.195 0.500 . 1 . . . . 168 GLY CA . 7003 1 649 . 1 1 155 155 SER H H 1 7.659 0.001 . 1 . . . . 169 SER H . 7003 1 650 . 1 1 155 155 SER C C 13 180.711 0.157 . 1 . . . . 169 SER C . 7003 1 651 . 1 1 155 155 SER CA C 13 54.481 0.500 . 1 . . . . 169 SER CA . 7003 1 652 . 1 1 155 155 SER CB C 13 64.668 0.087 . 1 . . . . 169 SER CB . 7003 1 653 . 1 1 155 155 SER N N 15 115.738 0.500 . 1 . . . . 169 SER N . 7003 1 654 . 1 1 156 156 PHE H H 1 8.689 0.005 . 1 . . . . 170 PHE H . 7003 1 655 . 1 1 156 156 PHE C C 13 180.046 0.172 . 1 . . . . 170 PHE C . 7003 1 656 . 1 1 156 156 PHE CA C 13 52.404 0.500 . 1 . . . . 170 PHE CA . 7003 1 657 . 1 1 156 156 PHE CB C 13 39.117 0.021 . 1 . . . . 170 PHE CB . 7003 1 658 . 1 1 156 156 PHE N N 15 119.560 0.500 . 1 . . . . 170 PHE N . 7003 1 659 . 1 1 157 157 THR H H 1 8.685 0.001 . 1 . . . . 171 THR H . 7003 1 660 . 1 1 157 157 THR C C 13 177.701 0.092 . 1 . . . . 171 THR C . 7003 1 661 . 1 1 157 157 THR CA C 13 56.195 0.500 . 1 . . . . 171 THR CA . 7003 1 662 . 1 1 157 157 THR CB C 13 69.877 0.087 . 1 . . . . 171 THR CB . 7003 1 663 . 1 1 157 157 THR N N 15 110.366 0.500 . 1 . . . . 171 THR N . 7003 1 664 . 1 1 158 158 VAL H H 1 8.734 0.001 . 1 . . . . 172 VAL H . 7003 1 665 . 1 1 158 158 VAL C C 13 177.467 0.081 . 1 . . . . 172 VAL C . 7003 1 666 . 1 1 158 158 VAL CA C 13 58.700 0.021 . 1 . . . . 172 VAL CA . 7003 1 667 . 1 1 158 158 VAL CB C 13 33.249 0.021 . 1 . . . . 172 VAL CB . 7003 1 668 . 1 1 158 158 VAL N N 15 118.481 0.500 . 1 . . . . 172 VAL N . 7003 1 669 . 1 1 159 159 ARG H H 1 9.107 0.100 . 1 . . . . 173 ARG H . 7003 1 670 . 1 1 159 159 ARG C C 13 176.842 0.149 . 1 . . . . 173 ARG C . 7003 1 671 . 1 1 159 159 ARG CA C 13 51.217 0.219 . 1 . . . . 173 ARG CA . 7003 1 672 . 1 1 159 159 ARG CB C 13 31.106 0.500 . 1 . . . . 173 ARG CB . 7003 1 673 . 1 1 159 159 ARG N N 15 124.683 0.500 . 1 . . . . 173 ARG N . 7003 1 674 . 1 1 160 160 THR H H 1 8.730 0.001 . 1 . . . . 174 THR H . 7003 1 675 . 1 1 160 160 THR C C 13 177.745 0.058 . 1 . . . . 174 THR C . 7003 1 676 . 1 1 160 160 THR CA C 13 60.975 0.087 . 1 . . . . 174 THR CA . 7003 1 677 . 1 1 160 160 THR CB C 13 66.184 0.500 . 1 . . . . 174 THR CB . 7003 1 678 . 1 1 160 160 THR N N 15 117.705 0.500 . 1 . . . . 174 THR N . 7003 1 679 . 1 1 161 161 ASP H H 1 8.481 0.002 . 1 . . . . 175 ASP H . 7003 1 680 . 1 1 161 161 ASP C C 13 176.167 0.500 . 1 . . . . 175 ASP C . 7003 1 681 . 1 1 161 161 ASP CA C 13 51.854 0.500 . 1 . . . . 175 ASP CA . 7003 1 682 . 1 1 161 161 ASP CB C 13 41.040 0.500 . 1 . . . . 175 ASP CB . 7003 1 683 . 1 1 161 161 ASP N N 15 126.362 0.500 . 1 . . . . 175 ASP N . 7003 1 684 . 1 1 162 162 THR C C 13 177.362 0.500 . 1 . . . . 176 THR C . 7003 1 685 . 1 1 162 162 THR CA C 13 58.295 0.500 . 1 . . . . 176 THR CA . 7003 1 686 . 1 1 162 162 THR CB C 13 65.878 0.500 . 1 . . . . 176 THR CB . 7003 1 687 . 1 1 163 163 GLY H H 1 7.689 0.001 . 1 . . . . 177 GLY H . 7003 1 688 . 1 1 163 163 GLY C C 13 179.360 0.111 . 1 . . . . 177 GLY C . 7003 1 689 . 1 1 163 163 GLY CA C 13 41.491 0.153 . 1 . . . . 177 GLY CA . 7003 1 690 . 1 1 163 163 GLY N N 15 110.255 0.500 . 1 . . . . 177 GLY N . 7003 1 691 . 1 1 164 164 GLU H H 1 8.168 0.001 . 1 . . . . 178 GLU H . 7003 1 692 . 1 1 164 164 GLU C C 13 176.648 0.500 . 1 . . . . 178 GLU C . 7003 1 693 . 1 1 164 164 GLU CA C 13 52.052 0.500 . 1 . . . . 178 GLU CA . 7003 1 694 . 1 1 164 164 GLU CB C 13 26.402 0.500 . 1 . . . . 178 GLU CB . 7003 1 695 . 1 1 164 164 GLU N N 15 121.019 0.069 . 1 . . . . 178 GLU N . 7003 1 696 . 1 1 165 165 PRO C C 13 174.529 0.500 . 1 . . . . 179 PRO C . 7003 1 697 . 1 1 165 165 PRO CA C 13 60.537 0.500 . 1 . . . . 179 PRO CA . 7003 1 698 . 1 1 165 165 PRO CB C 13 29.217 0.500 . 1 . . . . 179 PRO CB . 7003 1 699 . 1 1 166 166 MET H H 1 9.295 0.001 . 1 . . . . 180 MET H . 7003 1 700 . 1 1 166 166 MET C C 13 175.778 0.113 . 1 . . . . 180 MET C . 7003 1 701 . 1 1 166 166 MET CA C 13 52.206 0.500 . 1 . . . . 180 MET CA . 7003 1 702 . 1 1 166 166 MET CB C 13 32.139 0.500 . 1 . . . . 180 MET CB . 7003 1 703 . 1 1 166 166 MET N N 15 124.094 0.500 . 1 . . . . 180 MET N . 7003 1 704 . 1 1 167 167 GLY H H 1 8.455 0.017 . 1 . . . . 181 GLY H . 7003 1 705 . 1 1 167 167 GLY C C 13 178.482 0.500 . 1 . . . . 181 GLY C . 7003 1 706 . 1 1 167 167 GLY CA C 13 44.392 0.500 . 1 . . . . 181 GLY CA . 7003 1 707 . 1 1 167 167 GLY N N 15 111.432 0.500 . 1 . . . . 181 GLY N . 7003 1 708 . 1 1 168 168 ARG H H 1 7.308 0.002 . 1 . . . . 182 ARG H . 7003 1 709 . 1 1 168 168 ARG C C 13 177.724 0.108 . 1 . . . . 182 ARG C . 7003 1 710 . 1 1 168 168 ARG CA C 13 54.316 0.087 . 1 . . . . 182 ARG CA . 7003 1 711 . 1 1 168 168 ARG CB C 13 27.347 0.500 . 1 . . . . 182 ARG CB . 7003 1 712 . 1 1 168 168 ARG N N 15 120.020 0.500 . 1 . . . . 182 ARG N . 7003 1 713 . 1 1 169 169 GLY H H 1 9.051 0.002 . 1 . . . . 183 GLY H . 7003 1 714 . 1 1 169 169 GLY C C 13 179.955 0.138 . 1 . . . . 183 GLY C . 7003 1 715 . 1 1 169 169 GLY CA C 13 41.326 0.500 . 1 . . . . 183 GLY CA . 7003 1 716 . 1 1 169 169 GLY N N 15 115.525 0.500 . 1 . . . . 183 GLY N . 7003 1 717 . 1 1 170 170 THR H H 1 7.635 0.001 . 1 . . . . 184 THR H . 7003 1 718 . 1 1 170 170 THR C C 13 181.341 0.500 . 1 . . . . 184 THR C . 7003 1 719 . 1 1 170 170 THR CA C 13 59.525 0.087 . 1 . . . . 184 THR CA . 7003 1 720 . 1 1 170 170 THR CB C 13 69.745 0.087 . 1 . . . . 184 THR CB . 7003 1 721 . 1 1 170 170 THR N N 15 116.120 0.500 . 1 . . . . 184 THR N . 7003 1 722 . 1 1 171 171 LYS H H 1 9.912 0.002 . 1 . . . . 185 LYS H . 7003 1 723 . 1 1 171 171 LYS C C 13 178.832 0.133 . 1 . . . . 185 LYS C . 7003 1 724 . 1 1 171 171 LYS CA C 13 51.678 0.500 . 1 . . . . 185 LYS CA . 7003 1 725 . 1 1 171 171 LYS CB C 13 32.556 0.087 . 1 . . . . 185 LYS CB . 7003 1 726 . 1 1 171 171 LYS N N 15 128.263 0.500 . 1 . . . . 185 LYS N . 7003 1 727 . 1 1 172 172 VAL H H 1 9.066 0.001 . 1 . . . . 186 VAL H . 7003 1 728 . 1 1 172 172 VAL C C 13 177.947 0.083 . 1 . . . . 186 VAL C . 7003 1 729 . 1 1 172 172 VAL CA C 13 59.195 0.500 . 1 . . . . 186 VAL CA . 7003 1 730 . 1 1 172 172 VAL CB C 13 30.117 0.500 . 1 . . . . 186 VAL CB . 7003 1 731 . 1 1 172 172 VAL N N 15 126.546 0.500 . 1 . . . . 186 VAL N . 7003 1 732 . 1 1 173 173 ILE H H 1 9.858 0.100 . 1 . . . . 187 ILE H . 7003 1 733 . 1 1 173 173 ILE C C 13 177.388 0.500 . 1 . . . . 187 ILE C . 7003 1 734 . 1 1 173 173 ILE CA C 13 58.832 0.153 . 1 . . . . 187 ILE CA . 7003 1 735 . 1 1 173 173 ILE CB C 13 36.447 0.500 . 1 . . . . 187 ILE CB . 7003 1 736 . 1 1 173 173 ILE N N 15 127.871 0.500 . 1 . . . . 187 ILE N . 7003 1 737 . 1 1 174 174 LEU H H 1 8.760 0.100 . 1 . . . . 188 LEU H . 7003 1 738 . 1 1 174 174 LEU C C 13 177.059 0.500 . 1 . . . . 188 LEU C . 7003 1 739 . 1 1 174 174 LEU CA C 13 51.217 0.087 . 1 . . . . 188 LEU CA . 7003 1 740 . 1 1 174 174 LEU CB C 13 39.051 0.021 . 1 . . . . 188 LEU CB . 7003 1 741 . 1 1 174 174 LEU N N 15 125.811 0.500 . 1 . . . . 188 LEU N . 7003 1 742 . 1 1 175 175 HIS H H 1 8.204 0.001 . 1 . . . . 189 HIS H . 7003 1 743 . 1 1 175 175 HIS C C 13 176.860 0.011 . 1 . . . . 189 HIS C . 7003 1 744 . 1 1 175 175 HIS CA C 13 52.898 0.021 . 1 . . . . 189 HIS CA . 7003 1 745 . 1 1 175 175 HIS CB C 13 25.468 0.021 . 1 . . . . 189 HIS CB . 7003 1 746 . 1 1 175 175 HIS N N 15 125.210 0.500 . 1 . . . . 189 HIS N . 7003 1 747 . 1 1 176 176 LEU H H 1 7.884 0.100 . 1 . . . . 190 LEU H . 7003 1 748 . 1 1 176 176 LEU C C 13 174.456 0.074 . 1 . . . . 190 LEU C . 7003 1 749 . 1 1 176 176 LEU CA C 13 53.360 0.500 . 1 . . . . 190 LEU CA . 7003 1 750 . 1 1 176 176 LEU CB C 13 38.722 0.021 . 1 . . . . 190 LEU CB . 7003 1 751 . 1 1 176 176 LEU N N 15 123.616 0.500 . 1 . . . . 190 LEU N . 7003 1 752 . 1 1 177 177 LYS H H 1 8.324 0.100 . 1 . . . . 191 LYS H . 7003 1 753 . 1 1 177 177 LYS C C 13 174.054 0.094 . 1 . . . . 191 LYS C . 7003 1 754 . 1 1 177 177 LYS CA C 13 54.250 0.087 . 1 . . . . 191 LYS CA . 7003 1 755 . 1 1 177 177 LYS CB C 13 31.007 0.021 . 1 . . . . 191 LYS CB . 7003 1 756 . 1 1 177 177 LYS N N 15 120.504 0.500 . 1 . . . . 191 LYS N . 7003 1 757 . 1 1 178 178 GLU H H 1 8.892 0.004 . 1 . . . . 192 GLU H . 7003 1 758 . 1 1 178 178 GLU C C 13 176.031 0.170 . 1 . . . . 192 GLU C . 7003 1 759 . 1 1 178 178 GLU CA C 13 56.854 0.021 . 1 . . . . 192 GLU CA . 7003 1 760 . 1 1 178 178 GLU CB C 13 26.820 0.500 . 1 . . . . 192 GLU CB . 7003 1 761 . 1 1 178 178 GLU N N 15 120.616 0.500 . 1 . . . . 192 GLU N . 7003 1 762 . 1 1 179 179 ASP H H 1 8.254 0.004 . 1 . . . . 193 ASP H . 7003 1 763 . 1 1 179 179 ASP C C 13 174.931 0.138 . 1 . . . . 193 ASP C . 7003 1 764 . 1 1 179 179 ASP CA C 13 50.755 0.500 . 1 . . . . 193 ASP CA . 7003 1 765 . 1 1 179 179 ASP CB C 13 36.743 0.500 . 1 . . . . 193 ASP CB . 7003 1 766 . 1 1 179 179 ASP N N 15 113.265 0.500 . 1 . . . . 193 ASP N . 7003 1 767 . 1 1 180 180 GLN H H 1 7.746 0.003 . 1 . . . . 194 GLN H . 7003 1 768 . 1 1 180 180 GLN C C 13 176.368 0.082 . 1 . . . . 194 GLN C . 7003 1 769 . 1 1 180 180 GLN CA C 13 51.283 0.500 . 1 . . . . 194 GLN CA . 7003 1 770 . 1 1 180 180 GLN CB C 13 24.743 0.021 . 1 . . . . 194 GLN CB . 7003 1 771 . 1 1 180 180 GLN N N 15 118.638 0.500 . 1 . . . . 194 GLN N . 7003 1 772 . 1 1 181 181 THR H H 1 7.299 0.004 . 1 . . . . 195 THR H . 7003 1 773 . 1 1 181 181 THR C C 13 174.946 0.108 . 1 . . . . 195 THR C . 7003 1 774 . 1 1 181 181 THR CA C 13 61.569 0.500 . 1 . . . . 195 THR CA . 7003 1 775 . 1 1 181 181 THR CB C 13 65.657 0.087 . 1 . . . . 195 THR CB . 7003 1 776 . 1 1 181 181 THR N N 15 106.525 0.500 . 1 . . . . 195 THR N . 7003 1 777 . 1 1 182 182 GLU H H 1 8.743 0.003 . 1 . . . . 196 GLU H . 7003 1 778 . 1 1 182 182 GLU C C 13 175.740 0.107 . 1 . . . . 196 GLU C . 7003 1 779 . 1 1 182 182 GLU CA C 13 55.931 0.021 . 1 . . . . 196 GLU CA . 7003 1 780 . 1 1 182 182 GLU CB C 13 25.633 0.087 . 1 . . . . 196 GLU CB . 7003 1 781 . 1 1 182 182 GLU N N 15 124.008 0.500 . 1 . . . . 196 GLU N . 7003 1 782 . 1 1 183 183 TYR H H 1 6.531 0.003 . 1 . . . . 197 TYR H . 7003 1 783 . 1 1 183 183 TYR C C 13 180.812 0.116 . 1 . . . . 197 TYR C . 7003 1 784 . 1 1 183 183 TYR CA C 13 57.118 0.021 . 1 . . . . 197 TYR CA . 7003 1 785 . 1 1 183 183 TYR CB C 13 34.370 0.021 . 1 . . . . 197 TYR CB . 7003 1 786 . 1 1 183 183 TYR N N 15 114.749 0.500 . 1 . . . . 197 TYR N . 7003 1 787 . 1 1 184 184 LEU H H 1 7.168 0.006 . 1 . . . . 198 LEU H . 7003 1 788 . 1 1 184 184 LEU C C 13 175.816 0.108 . 1 . . . . 198 LEU C . 7003 1 789 . 1 1 184 184 LEU CA C 13 50.689 0.500 . 1 . . . . 198 LEU CA . 7003 1 790 . 1 1 184 184 LEU CB C 13 39.150 0.500 . 1 . . . . 198 LEU CB . 7003 1 791 . 1 1 184 184 LEU N N 15 111.046 0.500 . 1 . . . . 198 LEU N . 7003 1 792 . 1 1 185 185 GLU H H 1 7.176 0.001 . 1 . . . . 199 GLU H . 7003 1 793 . 1 1 185 185 GLU C C 13 175.289 0.500 . 1 . . . . 199 GLU C . 7003 1 794 . 1 1 185 185 GLU CA C 13 52.250 0.500 . 1 . . . . 199 GLU CA . 7003 1 795 . 1 1 185 185 GLU CB C 13 27.128 0.500 . 1 . . . . 199 GLU CB . 7003 1 796 . 1 1 185 185 GLU N N 15 116.547 0.500 . 1 . . . . 199 GLU N . 7003 1 797 . 1 1 186 186 GLU C C 13 174.916 0.500 . 1 . . . . 200 GLU C . 7003 1 798 . 1 1 186 186 GLU CA C 13 57.767 0.500 . 1 . . . . 200 GLU CA . 7003 1 799 . 1 1 186 186 GLU CB C 13 26.777 0.500 . 1 . . . . 200 GLU CB . 7003 1 800 . 1 1 187 187 ARG H H 1 8.759 0.001 . 1 . . . . 201 ARG H . 7003 1 801 . 1 1 187 187 ARG C C 13 173.962 0.062 . 1 . . . . 201 ARG C . 7003 1 802 . 1 1 187 187 ARG CA C 13 56.821 0.500 . 1 . . . . 201 ARG CA . 7003 1 803 . 1 1 187 187 ARG CB C 13 26.589 0.021 . 1 . . . . 201 ARG CB . 7003 1 804 . 1 1 187 187 ARG N N 15 116.176 0.500 . 1 . . . . 201 ARG N . 7003 1 805 . 1 1 188 188 ARG H H 1 6.644 0.001 . 1 . . . . 202 ARG H . 7003 1 806 . 1 1 188 188 ARG C C 13 174.223 0.095 . 1 . . . . 202 ARG C . 7003 1 807 . 1 1 188 188 ARG CA C 13 54.250 0.500 . 1 . . . . 202 ARG CA . 7003 1 808 . 1 1 188 188 ARG CB C 13 27.380 0.021 . 1 . . . . 202 ARG CB . 7003 1 809 . 1 1 188 188 ARG N N 15 119.436 0.500 . 1 . . . . 202 ARG N . 7003 1 810 . 1 1 189 189 ILE H H 1 7.987 0.003 . 1 . . . . 203 ILE H . 7003 1 811 . 1 1 189 189 ILE C C 13 174.284 0.035 . 1 . . . . 203 ILE C . 7003 1 812 . 1 1 189 189 ILE CA C 13 62.953 0.500 . 1 . . . . 203 ILE CA . 7003 1 813 . 1 1 189 189 ILE CB C 13 35.029 0.021 . 1 . . . . 203 ILE CB . 7003 1 814 . 1 1 189 189 ILE N N 15 117.727 0.500 . 1 . . . . 203 ILE N . 7003 1 815 . 1 1 190 190 LYS H H 1 8.313 0.100 . 1 . . . . 204 LYS H . 7003 1 816 . 1 1 190 190 LYS C C 13 172.909 0.094 . 1 . . . . 204 LYS C . 7003 1 817 . 1 1 190 190 LYS CA C 13 57.810 0.087 . 1 . . . . 204 LYS CA . 7003 1 818 . 1 1 190 190 LYS CB C 13 29.260 0.500 . 1 . . . . 204 LYS CB . 7003 1 819 . 1 1 190 190 LYS N N 15 116.761 0.500 . 1 . . . . 204 LYS N . 7003 1 820 . 1 1 191 191 GLU H H 1 7.580 0.100 . 1 . . . . 205 GLU H . 7003 1 821 . 1 1 191 191 GLU C C 13 173.340 0.131 . 1 . . . . 205 GLU C . 7003 1 822 . 1 1 191 191 GLU CA C 13 56.459 0.021 . 1 . . . . 205 GLU CA . 7003 1 823 . 1 1 191 191 GLU CB C 13 26.292 0.500 . 1 . . . . 205 GLU CB . 7003 1 824 . 1 1 191 191 GLU N N 15 118.594 0.500 . 1 . . . . 205 GLU N . 7003 1 825 . 1 1 192 192 ILE H H 1 7.753 0.002 . 1 . . . . 206 ILE H . 7003 1 826 . 1 1 192 192 ILE C C 13 173.751 0.129 . 1 . . . . 206 ILE C . 7003 1 827 . 1 1 192 192 ILE CA C 13 62.690 0.087 . 1 . . . . 206 ILE CA . 7003 1 828 . 1 1 192 192 ILE CB C 13 35.326 0.219 . 1 . . . . 206 ILE CB . 7003 1 829 . 1 1 192 192 ILE N N 15 121.133 0.500 . 1 . . . . 206 ILE N . 7003 1 830 . 1 1 193 193 VAL H H 1 8.262 0.002 . 1 . . . . 207 VAL H . 7003 1 831 . 1 1 193 193 VAL C C 13 173.858 0.129 . 1 . . . . 207 VAL C . 7003 1 832 . 1 1 193 193 VAL CA C 13 64.009 0.218 . 1 . . . . 207 VAL CA . 7003 1 833 . 1 1 193 193 VAL CB C 13 28.798 0.500 . 1 . . . . 207 VAL CB . 7003 1 834 . 1 1 193 193 VAL N N 15 120.695 0.500 . 1 . . . . 207 VAL N . 7003 1 835 . 1 1 194 194 LYS H H 1 7.786 0.002 . 1 . . . . 208 LYS H . 7003 1 836 . 1 1 194 194 LYS C C 13 174.445 0.112 . 1 . . . . 208 LYS C . 7003 1 837 . 1 1 194 194 LYS CA C 13 56.096 0.500 . 1 . . . . 208 LYS CA . 7003 1 838 . 1 1 194 194 LYS CB C 13 29.260 0.086 . 1 . . . . 208 LYS CB . 7003 1 839 . 1 1 194 194 LYS N N 15 118.773 0.500 . 1 . . . . 208 LYS N . 7003 1 840 . 1 1 195 195 LYS H H 1 7.382 0.002 . 1 . . . . 209 LYS H . 7003 1 841 . 1 1 195 195 LYS C C 13 173.916 0.032 . 1 . . . . 209 LYS C . 7003 1 842 . 1 1 195 195 LYS CA C 13 55.997 0.021 . 1 . . . . 209 LYS CA . 7003 1 843 . 1 1 195 195 LYS CB C 13 30.545 0.500 . 1 . . . . 209 LYS CB . 7003 1 844 . 1 1 195 195 LYS N N 15 116.446 0.500 . 1 . . . . 209 LYS N . 7003 1 845 . 1 1 196 196 HIS H H 1 7.709 0.004 . 1 . . . . 210 HIS H . 7003 1 846 . 1 1 196 196 HIS C C 13 174.867 0.131 . 1 . . . . 210 HIS C . 7003 1 847 . 1 1 196 196 HIS CA C 13 54.579 0.500 . 1 . . . . 210 HIS CA . 7003 1 848 . 1 1 196 196 HIS CB C 13 30.941 0.500 . 1 . . . . 210 HIS CB . 7003 1 849 . 1 1 196 196 HIS N N 15 113.389 0.500 . 1 . . . . 210 HIS N . 7003 1 850 . 1 1 197 197 SER H H 1 8.051 0.004 . 1 . . . . 211 SER H . 7003 1 851 . 1 1 197 197 SER C C 13 176.724 0.500 . 1 . . . . 211 SER C . 7003 1 852 . 1 1 197 197 SER CA C 13 56.206 0.500 . 1 . . . . 211 SER CA . 7003 1 853 . 1 1 197 197 SER CB C 13 61.085 0.500 . 1 . . . . 211 SER CB . 7003 1 854 . 1 1 197 197 SER N N 15 115.558 0.500 . 1 . . . . 211 SER N . 7003 1 855 . 1 1 201 201 GLY C C 13 179.470 0.500 . 1 . . . . 215 GLY C . 7003 1 856 . 1 1 201 201 GLY CA C 13 43.195 0.500 . 1 . . . . 215 GLY CA . 7003 1 857 . 1 1 202 202 TYR H H 1 6.619 0.100 . 1 . . . . 216 TYR H . 7003 1 858 . 1 1 202 202 TYR C C 13 180.296 0.500 . 1 . . . . 216 TYR C . 7003 1 859 . 1 1 202 202 TYR CA C 13 53.173 0.500 . 1 . . . . 216 TYR CA . 7003 1 860 . 1 1 202 202 TYR CB C 13 38.007 0.500 . 1 . . . . 216 TYR CB . 7003 1 861 . 1 1 202 202 TYR N N 15 117.795 0.500 . 1 . . . . 216 TYR N . 7003 1 862 . 1 1 203 203 PRO C C 13 176.901 0.500 . 1 . . . . 217 PRO C . 7003 1 863 . 1 1 203 203 PRO CA C 13 60.669 0.500 . 1 . . . . 217 PRO CA . 7003 1 864 . 1 1 203 203 PRO CB C 13 29.019 0.500 . 1 . . . . 217 PRO CB . 7003 1 865 . 1 1 204 204 ILE H H 1 7.921 0.001 . 1 . . . . 218 ILE H . 7003 1 866 . 1 1 204 204 ILE C C 13 175.880 0.114 . 1 . . . . 218 ILE C . 7003 1 867 . 1 1 204 204 ILE CA C 13 57.448 0.500 . 1 . . . . 218 ILE CA . 7003 1 868 . 1 1 204 204 ILE CB C 13 37.040 0.087 . 1 . . . . 218 ILE CB . 7003 1 869 . 1 1 204 204 ILE N N 15 123.444 0.500 . 1 . . . . 218 ILE N . 7003 1 870 . 1 1 205 205 THR H H 1 8.584 0.004 . 1 . . . . 219 THR H . 7003 1 871 . 1 1 205 205 THR C C 13 179.946 0.153 . 1 . . . . 219 THR C . 7003 1 872 . 1 1 205 205 THR CA C 13 58.569 0.500 . 1 . . . . 219 THR CA . 7003 1 873 . 1 1 205 205 THR CB C 13 67.668 0.500 . 1 . . . . 219 THR CB . 7003 1 874 . 1 1 205 205 THR N N 15 122.978 0.500 . 1 . . . . 219 THR N . 7003 1 875 . 1 1 206 206 LEU H H 1 8.528 0.001 . 1 . . . . 220 LEU H . 7003 1 876 . 1 1 206 206 LEU C C 13 176.725 0.103 . 1 . . . . 220 LEU C . 7003 1 877 . 1 1 206 206 LEU CA C 13 51.414 0.087 . 1 . . . . 220 LEU CA . 7003 1 878 . 1 1 206 206 LEU CB C 13 40.601 0.087 . 1 . . . . 220 LEU CB . 7003 1 879 . 1 1 206 206 LEU N N 15 127.723 0.500 . 1 . . . . 220 LEU N . 7003 1 880 . 1 1 207 207 PHE H H 1 8.672 0.001 . 1 . . . . 221 PHE H . 7003 1 881 . 1 1 207 207 PHE C C 13 178.378 0.113 . 1 . . . . 221 PHE C . 7003 1 882 . 1 1 207 207 PHE CA C 13 54.612 0.500 . 1 . . . . 221 PHE CA . 7003 1 883 . 1 1 207 207 PHE CB C 13 37.271 0.021 . 1 . . . . 221 PHE CB . 7003 1 884 . 1 1 207 207 PHE N N 15 127.037 0.500 . 1 . . . . 221 PHE N . 7003 1 885 . 1 1 208 208 VAL H H 1 7.890 0.002 . 1 . . . . 222 VAL H . 7003 1 886 . 1 1 208 208 VAL C C 13 177.163 0.083 . 1 . . . . 222 VAL C . 7003 1 887 . 1 1 208 208 VAL CA C 13 58.734 0.500 . 1 . . . . 222 VAL CA . 7003 1 888 . 1 1 208 208 VAL CB C 13 30.677 0.500 . 1 . . . . 222 VAL CB . 7003 1 889 . 1 1 208 208 VAL N N 15 121.380 0.500 . 1 . . . . 222 VAL N . 7003 1 890 . 1 1 209 209 GLU H H 1 7.929 0.001 . 1 . . . . 223 GLU H . 7003 1 891 . 1 1 209 209 GLU C C 13 171.134 0.500 . 1 . . . . 223 GLU C . 7003 1 892 . 1 1 209 209 GLU CA C 13 55.547 0.500 . 1 . . . . 223 GLU CA . 7003 1 893 . 1 1 209 209 GLU CB C 13 28.512 0.500 . 1 . . . . 223 GLU CB . 7003 1 894 . 1 1 209 209 GLU N N 15 129.918 0.500 . 1 . . . . 223 GLU N . 7003 1 stop_ save_