data_19230 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 19230 _Entry.Title ; Solution structure of Hdm2 with engineered cyclotide ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2013-05-07 _Entry.Accession_date 2013-05-07 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype 'NMR, 10 STRUCTURES' _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 Subhabrata Majumder . . . 19230 2 Yanbin Ji . . . 19230 3 Melissa Millard . . . 19230 4 Radikha Borra . . . 19230 5 Tao Bi . . . 19230 6 Ahmed Elnagar . Y. . 19230 7 Nouri Neamati . . . 19230 8 Julio Camarero . A. . 19230 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 19230 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'Hdm2 oncoprotein' . 19230 'MCoTI-I cyclotide' . 19230 'p53 tumor suppressor' . 19230 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 19230 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 147 19230 '15N chemical shifts' 121 19230 '1H chemical shifts' 581 19230 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 . . 2013-08-08 2013-05-07 update BMRB 'update entry citation' 19230 1 . . 2013-07-29 2013-05-07 original author 'original release' 19230 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2M86 'BMRB Entry Tracking System' 19230 stop_ save_ ############### # Citations # ############### save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 19230 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 23848581 _Citation.Full_citation . _Citation.Title 'In Vivo Activation of the p53 Tumor Suppressor Pathway by an Engineered Cyclotide.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Am. Chem. Soc.' _Citation.Journal_name_full 'Journal of the American Chemical Society' _Citation.Journal_volume 135 _Citation.Journal_issue 31 _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 11623 _Citation.Page_last 11633 _Citation.Year 2013 _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 Yanbin Ji . . . 19230 1 2 Subhabrata Majumder . . . 19230 1 3 Melissa Millard . . . 19230 1 4 Radhika Borra . . . 19230 1 5 Tao Bi . . . 19230 1 6 Ahmed Elnagar . Y. . 19230 1 7 Nouri Neamati . . . 19230 1 8 Alexander Shekhtman . . . 19230 1 9 Julio Camarero . A. . 19230 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 19230 _Assembly.ID 1 _Assembly.Name Hdm2 _Assembly.BMRB_code . _Assembly.Number_of_components 2 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 Hdm2 1 $Hdm2 B . yes native no no . . . 19230 1 2 MCo-PMI 2 $MCo-PMI A . no native no no . . . 19230 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 Hdm2 1 CYS 38 38 SG . 1 Hdm2 1 CYS 50 50 SG . Hdm2 38 CYS SG . Hdm2 50 CYS SG 19230 1 2 disulfide single . 1 Hdm2 1 CYS 32 32 SG . 1 Hdm2 1 CYS 44 44 SG . Hdm2 32 CYS SG . Hdm2 44 CYS SG 19230 1 3 disulfide single . 1 Hdm2 1 CYS 25 25 SG . 1 Hdm2 1 CYS 42 42 SG . Hdm2 25 CYS SG . Hdm2 42 CYS SG 19230 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Hdm2 _Entity.Sf_category entity _Entity.Sf_framecode Hdm2 _Entity.Entry_ID 19230 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Hdm2 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID B _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; SGSGASKAPTSFAEYWNLLS AGGVCPKILQRCRRDSDCPG ACICRGNGYCG ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details 'This is an engineered cyclotide based on MCoTI-I., cyclic-pseudo-peptide' _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 51 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 5291.016 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2013-12-02 loop_ _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 no PDB 2M86 . "Solution Structure Of Hdm2 With Engineered Cyclotide" . . . . . 100.00 51 100.00 100.00 9.12e-28 . . . . 19230 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 1 SER . 19230 1 2 2 GLY . 19230 1 3 3 SER . 19230 1 4 4 GLY . 19230 1 5 5 ALA . 19230 1 6 6 SER . 19230 1 7 7 LYS . 19230 1 8 8 ALA . 19230 1 9 9 PRO . 19230 1 10 10 THR . 19230 1 11 11 SER . 19230 1 12 12 PHE . 19230 1 13 13 ALA . 19230 1 14 14 GLU . 19230 1 15 15 TYR . 19230 1 16 16 TRP . 19230 1 17 17 ASN . 19230 1 18 18 LEU . 19230 1 19 19 LEU . 19230 1 20 20 SER . 19230 1 21 21 ALA . 19230 1 22 22 GLY . 19230 1 23 23 GLY . 19230 1 24 24 VAL . 19230 1 25 25 CYS . 19230 1 26 26 PRO . 19230 1 27 27 LYS . 19230 1 28 28 ILE . 19230 1 29 29 LEU . 19230 1 30 30 GLN . 19230 1 31 31 ARG . 19230 1 32 32 CYS . 19230 1 33 33 ARG . 19230 1 34 34 ARG . 19230 1 35 35 ASP . 19230 1 36 36 SER . 19230 1 37 37 ASP . 19230 1 38 38 CYS . 19230 1 39 39 PRO . 19230 1 40 40 GLY . 19230 1 41 41 ALA . 19230 1 42 42 CYS . 19230 1 43 43 ILE . 19230 1 44 44 CYS . 19230 1 45 45 ARG . 19230 1 46 46 GLY . 19230 1 47 47 ASN . 19230 1 48 48 GLY . 19230 1 49 49 TYR . 19230 1 50 50 CYS . 19230 1 51 51 GLY . 19230 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 . SER 1 1 19230 1 . GLY 2 2 19230 1 . SER 3 3 19230 1 . GLY 4 4 19230 1 . ALA 5 5 19230 1 . SER 6 6 19230 1 . LYS 7 7 19230 1 . ALA 8 8 19230 1 . PRO 9 9 19230 1 . THR 10 10 19230 1 . SER 11 11 19230 1 . PHE 12 12 19230 1 . ALA 13 13 19230 1 . GLU 14 14 19230 1 . TYR 15 15 19230 1 . TRP 16 16 19230 1 . ASN 17 17 19230 1 . LEU 18 18 19230 1 . LEU 19 19 19230 1 . SER 20 20 19230 1 . ALA 21 21 19230 1 . GLY 22 22 19230 1 . GLY 23 23 19230 1 . VAL 24 24 19230 1 . CYS 25 25 19230 1 . PRO 26 26 19230 1 . LYS 27 27 19230 1 . ILE 28 28 19230 1 . LEU 29 29 19230 1 . GLN 30 30 19230 1 . ARG 31 31 19230 1 . CYS 32 32 19230 1 . ARG 33 33 19230 1 . ARG 34 34 19230 1 . ASP 35 35 19230 1 . SER 36 36 19230 1 . ASP 37 37 19230 1 . CYS 38 38 19230 1 . PRO 39 39 19230 1 . GLY 40 40 19230 1 . ALA 41 41 19230 1 . CYS 42 42 19230 1 . ILE 43 43 19230 1 . CYS 44 44 19230 1 . ARG 45 45 19230 1 . GLY 46 46 19230 1 . ASN 47 47 19230 1 . GLY 48 48 19230 1 . TYR 49 49 19230 1 . CYS 50 50 19230 1 . GLY 51 51 19230 1 stop_ save_ save_MCo-PMI _Entity.Sf_category entity _Entity.Sf_framecode MCo-PMI _Entity.Entry_ID 19230 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name MCo-PMI _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; LVRPKPLLLKLLKSVGAQKD TYTMKEVLFYLGQYIMTKRL YDEKQQHIVYCSNDLLGDLF GVPSFSVKEHRKIYTMIYRN LVV ; _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 83 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state . _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 9814.753 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-29 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 15945 . human_mdm2_N-terminal_domain . . . . . 100.00 114 100.00 100.00 1.22e-52 . . . . 19230 2 2 no BMRB 18755 . entity_1 . . . . . 100.00 124 98.80 98.80 6.59e-50 . . . . 19230 2 3 no BMRB 2410 . "N-terminal domain of the human murine double minute clone 2 protein" . . . . . 100.00 119 100.00 100.00 8.76e-53 . . . . 19230 2 4 no BMRB 6612 . HDM2 . . . . . 100.00 119 100.00 100.00 8.76e-53 . . . . 19230 2 5 no PDB 1RV1 . "Crystal Structure Of Human Mdm2 With An Imidazoline Inhibitor" . . . . . 100.00 85 98.80 98.80 3.13e-51 . . . . 19230 2 6 no PDB 1T4E . "Structure Of Human Mdm2 In Complex With A Benzodiazepine Inhibitor" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 7 no PDB 1T4F . "Structure Of Human Mdm2 In Complex With An Optimized P53 Peptide" . . . . . 100.00 110 100.00 100.00 8.22e-53 . . . . 19230 2 8 no PDB 1YCR . "Mdm2 Bound To The Transactivation Domain Of P53" . . . . . 100.00 109 100.00 100.00 6.70e-53 . . . . 19230 2 9 no PDB 1Z1M . "Nmr Structure Of Unliganded Mdm2" . . . . . 100.00 119 100.00 100.00 8.76e-53 . . . . 19230 2 10 no PDB 2AXI . "Hdm2 In Complex With A Beta-hairpin" . . . . . 100.00 115 100.00 100.00 9.66e-53 . . . . 19230 2 11 no PDB 2GV2 . "Mdm2 In Complex With An 8-Mer P53 Peptide Analogue" . . . . . 100.00 110 100.00 100.00 8.22e-53 . . . . 19230 2 12 no PDB 2LZG . "Nmr Structure Of Mdm2 (6-125) With Pip-1" . . . . . 100.00 125 100.00 100.00 5.78e-53 . . . . 19230 2 13 no PDB 2M86 . "Solution Structure Of Hdm2 With Engineered Cyclotide" . . . . . 100.00 129 100.00 100.00 1.08e-52 . . . . 19230 2 14 no PDB 2RUH . "Chemical Shift Assignments For Mip And Mdm2 In Bound State" . . . . . 92.77 131 98.70 100.00 3.31e-47 . . . . 19230 2 15 no PDB 3EQS . "Crystal Structure Of Human Mdm2 In Complex With A 12-Mer Peptide Inhibitor" . . . . . 100.00 85 100.00 100.00 3.43e-52 . . . . 19230 2 16 no PDB 3G03 . "Structure Of Human Mdm2 In Complex With High Affinity Peptide" . . . . . 100.00 109 100.00 100.00 8.51e-53 . . . . 19230 2 17 no PDB 3IUX . "Crystal Structure Of Human Mdm2 In Complex With A Potent Miniature Protein Inhibitor (18-Residues)" . . . . . 100.00 85 100.00 100.00 3.43e-52 . . . . 19230 2 18 no PDB 3IWY . "Crystal Structure Of Human Mdm2 Complexed With D-peptide (12 Residues)" . . . . . 100.00 85 100.00 100.00 3.43e-52 . . . . 19230 2 19 no PDB 3JZK . "Crystal Structure Of Mdm2 With Chromenotriazolopyrimidine 1" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 20 no PDB 3JZR . "Human Mdm2 Liganded With A 12mer Peptide Inhibitor (Pdi6w)" . . . . . 100.00 110 100.00 100.00 8.22e-53 . . . . 19230 2 21 no PDB 3JZS . "Human Mdm2 Liganded With A 12mer Peptide Inhibitor (Pdiq)" . . . . . 100.00 86 100.00 100.00 3.10e-52 . . . . 19230 2 22 no PDB 3LBK . "Structure Of Human Mdm2 Protein In Complex With A Small Molecule Inhibitor" . . . . . 100.00 95 98.80 98.80 2.02e-51 . . . . 19230 2 23 no PDB 3LBL . "Structure Of Human Mdm2 Protein In Complex With Mi-63-Analog" . . . . . 100.00 95 100.00 100.00 2.24e-52 . . . . 19230 2 24 no PDB 3LNJ . "Crystal Structure Of Human Mdm2 In Complex With D-Peptide Inhibitor (Dpmi-Alpha)" . . . . . 100.00 85 100.00 100.00 3.43e-52 . . . . 19230 2 25 no PDB 3LNZ . "Crystal Structure Of Human Mdm2 With A 12-Mer Peptide Inhibitor Pmi (N8a Mutant)" . . . . . 100.00 85 100.00 100.00 3.43e-52 . . . . 19230 2 26 no PDB 3TJ2 . "Structure Of A Novel Submicromolar Mdm2 Inhibitor" . . . . . 100.00 95 100.00 100.00 2.24e-52 . . . . 19230 2 27 no PDB 3TPX . "Crystal Structure Of Human Mdm2 In Complex With A Trifluoromethylated D-peptide Inhibitor" . . . . . 100.00 85 100.00 100.00 3.43e-52 . . . . 19230 2 28 no PDB 3TU1 . "Exhaustive Fluorine Scanning Towards Potent P53-Mdm2 Antagonist" . . . . . 100.00 108 100.00 100.00 8.08e-53 . . . . 19230 2 29 no PDB 3V3B . "Structure Of The Stapled P53 Peptide Bound To Mdm2" . . . . . 100.00 88 100.00 100.00 2.76e-52 . . . . 19230 2 30 no PDB 3VBG . "Structure Of Hdm2 With Dimer Inducing Indolyl Hydantoin Ro-2443" . . . . . 100.00 85 98.80 98.80 3.13e-51 . . . . 19230 2 31 no PDB 3VZV . "Crystal Structure Of Human Mdm2 With A Dihydroimidazothiazole Inhibitor" . . . . . 100.00 87 98.80 98.80 2.76e-51 . . . . 19230 2 32 no PDB 3W69 . "Crystal Structure Of Human Mdm2 With A Dihydroimidazothiazole Inhibitor" . . . . . 100.00 87 98.80 98.80 2.76e-51 . . . . 19230 2 33 no PDB 4DIJ . "The Central Valine Concept Provides An Entry In A New Class Of Non Peptide Inhibitors Of The P53-Mdm2 Interaction" . . . . . 100.00 96 98.80 98.80 1.86e-51 . . . . 19230 2 34 no PDB 4ERE . "Crystal Structure Of Mdm2 (17-111) In Complex With Compound 23" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 35 no PDB 4ERF . "Crystal Structure Of Mdm2 (17-111) In Complex With Compound 29 (Am- 8553)" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 36 no PDB 4HBM . "Ordering Of The N Terminus Of Human Mdm2 By Small Molecule Inhibitors" . . . . . 100.00 120 100.00 100.00 5.97e-53 . . . . 19230 2 37 no PDB 4HFZ . "Crystal Structure Of An Mdm2/p53 Peptide Complex" . . . . . 100.00 109 97.59 97.59 2.18e-51 . . . . 19230 2 38 no PDB 4HG7 . "Crystal Structure Of An Mdm2/nutlin-3a Complex" . . . . . 98.80 97 97.56 97.56 3.12e-50 . . . . 19230 2 39 no PDB 4JV7 . "Co-crystal Structure Of Mdm2 With Inhibitor (2s,5r,6s)-2-benzyl-5,6- Bis(4-bromophenyl)-4-methylmorpholin-3-one" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 40 no PDB 4JV9 . "Co-crystal Structure Of Mdm2 With Inhibitor (2s,5r,6s)-2-benzyl-5,6- Bis(4-chlorophenyl)-4-methylmorpholin-3-one" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 41 no PDB 4JVE . "Co-crystal Structure Of Mdm2 With Inhibitor (2r,3e)-2-[(2s,3r,6s)-2,3- Bis(4-chlorophenyl)-6-(4-fluorobenzyl)-5-oxomorpholin-4-" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 42 no PDB 4JVR . "Co-crystal Structure Of Mdm2 With Inhibitor (2's,3r,4's,5'r)-n-(2- Aminoethyl)-6-chloro-4'-(3-chloro-2-fluorophenyl)-2'-(2,2- D" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 43 no PDB 4JWR . "Co-crystal Structure Of Mdm2 With Inhibitor {(2s,5r,6s)-6-(3- Chlorophenyl)-5-(4-chlorophenyl)-4-[(2s)-1-hydroxybutan-2-yl]-3- " . . . . . 100.00 95 100.00 100.00 2.03e-52 . . . . 19230 2 44 no PDB 4MDN . "Structure Of A Novel Submicromolar Mdm2 Inhibitor" . . . . . 100.00 94 100.00 100.00 2.27e-52 . . . . 19230 2 45 no PDB 4MDQ . "Structure Of A Novel Submicromolar Mdm2 Inhibitor" . . . . . 100.00 86 100.00 100.00 3.20e-52 . . . . 19230 2 46 no PDB 4OAS . "Co-crystal Structure Of Mdm2 (17-111) In Complex With Compound 25" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 47 no PDB 4OBA . "Co-crystal Structure Of Mdm2 With Inhibitor Compound 4" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 48 no PDB 4OCC . "Co-crystal Structure Of Mdm2(17-111) In Complex With Compound 48" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 49 no PDB 4ODE . "Co-crystal Structure Of Mdm2 With Inhibitor Compound 4" . . . . . 100.00 105 100.00 100.00 1.53e-52 . . . . 19230 2 50 no PDB 4ODF . "Co-crystal Structure Of Mdm2 With Inhibitor Compound 47" . . . . . 100.00 105 100.00 100.00 1.53e-52 . . . . 19230 2 51 no PDB 4OGN . "Co-crystal Structure Of Mdm2 With Inhbitor Compound 3" . . . . . 100.00 105 100.00 100.00 1.53e-52 . . . . 19230 2 52 no PDB 4OGT . "Co-crystal Structure Of Mdm2 With Inhbitor Compound 46" . . . . . 100.00 105 100.00 100.00 1.53e-52 . . . . 19230 2 53 no PDB 4OGV . "Co-crystal Structure Of Mdm2 With Inhibitor Compound 49" . . . . . 100.00 95 100.00 100.00 2.03e-52 . . . . 19230 2 54 no PDB 4OQ3 . "Tetra-substituted Imidazoles As A New Class Of Inhibitors Of The P53- Mdm2 Interaction" . . . . . 100.00 96 98.80 98.80 1.86e-51 . . . . 19230 2 55 no PDB 4QO4 . "Co-crystal Structure Of Mdm2 (17-111) With Compound 16, {(3r,5r,6s)-5- (3-chlorophenyl)-6-(4-chlorophenyl)-1-[(1s)-1-(6-cyclopr" . . . . . 100.00 96 100.00 100.00 2.43e-52 . . . . 19230 2 56 no PDB 4UMN . "Structure Of A Stapled Peptide Antagonist Bound To Nutlin- Resistant Mdm2" . . . . . 100.00 120 98.80 98.80 3.56e-52 . . . . 19230 2 57 no PDB 4WT2 . "Co-crystal Structure Of Mdm2 In Complex With Am-7209" . . . . . 100.00 105 100.00 100.00 1.53e-52 . . . . 19230 2 58 no DBJ BAB11975 . "MDM2 [Canis lupus familiaris]" . . . . . 100.00 487 98.80 100.00 7.81e-51 . . . . 19230 2 59 no DBJ BAC78209 . "double minute 2 protein MDM2 [Felis catus]" . . . . . 100.00 491 98.80 100.00 8.33e-51 . . . . 19230 2 60 no DBJ BAF83030 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 491 100.00 100.00 3.58e-51 . . . . 19230 2 61 no DBJ BAJ17752 . "Mdm2 p53 binding protein homolog [synthetic construct]" . . . . . 100.00 497 100.00 100.00 3.94e-51 . . . . 19230 2 62 no EMBL CAA78055 . "p53 associated [Homo sapiens]" . . . . . 100.00 491 100.00 100.00 3.58e-51 . . . . 19230 2 63 no EMBL CAD23251 . "MDM2 isoform KB9 [Homo sapiens]" . . . . . 100.00 243 100.00 100.00 1.07e-51 . . . . 19230 2 64 no EMBL CAD36959 . "p53-binding protein [Homo sapiens]" . . . . . 100.00 166 100.00 100.00 4.37e-52 . . . . 19230 2 65 no EMBL CAH89564 . "hypothetical protein [Pongo abelii]" . . . . . 100.00 497 100.00 100.00 3.94e-51 . . . . 19230 2 66 no EMBL CAP16708 . "MDM2 protein [Homo sapiens]" . . . . . 100.00 413 100.00 100.00 8.62e-52 . . . . 19230 2 67 no GB AAA60568 . "p53 associated [Homo sapiens]" . . . . . 100.00 491 100.00 100.00 3.58e-51 . . . . 19230 2 68 no GB AAF28866 . "double minute 2 protein [Equus caballus]" . . . . . 100.00 491 98.80 100.00 8.33e-51 . . . . 19230 2 69 no GB AAF67833 . "Mdm2 [Canis lupus familiaris]" . . . . . 100.00 484 98.80 100.00 7.44e-51 . . . . 19230 2 70 no GB AAG42840 . "MDM2 [Canis lupus familiaris]" . . . . . 100.00 487 98.80 100.00 7.81e-51 . . . . 19230 2 71 no GB AAG42841 . "MDM2 alpha [Canis lupus familiaris]" . . . . . 57.83 426 100.00 100.00 1.92e-25 . . . . 19230 2 72 no PRF 1814460A . "p53-associated protein" . . . . . 100.00 491 100.00 100.00 3.58e-51 . . . . 19230 2 73 no REF NP_001003103 . "E3 ubiquitin-protein ligase Mdm2 [Canis lupus familiaris]" . . . . . 100.00 487 98.80 100.00 7.81e-51 . . . . 19230 2 74 no REF NP_001009346 . "E3 ubiquitin-protein ligase Mdm2 [Felis catus]" . . . . . 100.00 491 98.80 100.00 8.33e-51 . . . . 19230 2 75 no REF NP_001092577 . "E3 ubiquitin-protein ligase Mdm2 [Bos taurus]" . . . . . 100.00 492 98.80 100.00 8.46e-51 . . . . 19230 2 76 no REF NP_001098773 . "E3 ubiquitin-protein ligase Mdm2 [Sus scrofa]" . . . . . 100.00 491 97.59 98.80 3.51e-50 . . . . 19230 2 77 no REF NP_001124685 . "E3 ubiquitin-protein ligase Mdm2 [Pongo abelii]" . . . . . 100.00 497 100.00 100.00 3.94e-51 . . . . 19230 2 78 no SP P56950 . "RecName: Full=E3 ubiquitin-protein ligase Mdm2; AltName: Full=Double minute 2 protein; Short=Cdm2; AltName: Full=p53-binding pr" . . . . . 100.00 487 98.80 100.00 7.81e-51 . . . . 19230 2 79 no SP P56951 . "RecName: Full=E3 ubiquitin-protein ligase Mdm2; AltName: Full=Double minute 2 protein; Short=Edm2; AltName: Full=p53-binding pr" . . . . . 100.00 491 98.80 100.00 8.33e-51 . . . . 19230 2 80 no SP Q00987 . "RecName: Full=E3 ubiquitin-protein ligase Mdm2; AltName: Full=Double minute 2 protein; Short=Hdm2; AltName: Full=Oncoprotein Md" . . . . . 100.00 491 100.00 100.00 3.58e-51 . . . . 19230 2 81 no SP Q7YRZ8 . "RecName: Full=E3 ubiquitin-protein ligase Mdm2; AltName: Full=Double minute 2 protein; AltName: Full=p53-binding protein Mdm2 [" . . . . . 100.00 491 98.80 100.00 8.33e-51 . . . . 19230 2 82 no TPG DAA29805 . "TPA: MDM2-like protein [Bos taurus]" . . . . . 100.00 492 97.59 100.00 3.18e-50 . . . . 19230 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 92 LEU . 19230 2 2 93 VAL . 19230 2 3 94 ARG . 19230 2 4 95 PRO . 19230 2 5 96 LYS . 19230 2 6 97 PRO . 19230 2 7 98 LEU . 19230 2 8 99 LEU . 19230 2 9 100 LEU . 19230 2 10 101 LYS . 19230 2 11 102 LEU . 19230 2 12 103 LEU . 19230 2 13 104 LYS . 19230 2 14 105 SER . 19230 2 15 106 VAL . 19230 2 16 107 GLY . 19230 2 17 108 ALA . 19230 2 18 109 GLN . 19230 2 19 110 LYS . 19230 2 20 111 ASP . 19230 2 21 112 THR . 19230 2 22 113 TYR . 19230 2 23 114 THR . 19230 2 24 115 MET . 19230 2 25 116 LYS . 19230 2 26 117 GLU . 19230 2 27 118 VAL . 19230 2 28 119 LEU . 19230 2 29 120 PHE . 19230 2 30 121 TYR . 19230 2 31 122 LEU . 19230 2 32 123 GLY . 19230 2 33 124 GLN . 19230 2 34 125 TYR . 19230 2 35 126 ILE . 19230 2 36 127 MET . 19230 2 37 128 THR . 19230 2 38 129 LYS . 19230 2 39 130 ARG . 19230 2 40 131 LEU . 19230 2 41 132 TYR . 19230 2 42 133 ASP . 19230 2 43 134 GLU . 19230 2 44 135 LYS . 19230 2 45 136 GLN . 19230 2 46 137 GLN . 19230 2 47 138 HIS . 19230 2 48 139 ILE . 19230 2 49 140 VAL . 19230 2 50 141 TYR . 19230 2 51 142 CYS . 19230 2 52 143 SER . 19230 2 53 144 ASN . 19230 2 54 145 ASP . 19230 2 55 146 LEU . 19230 2 56 147 LEU . 19230 2 57 148 GLY . 19230 2 58 149 ASP . 19230 2 59 150 LEU . 19230 2 60 151 PHE . 19230 2 61 152 GLY . 19230 2 62 153 VAL . 19230 2 63 154 PRO . 19230 2 64 155 SER . 19230 2 65 156 PHE . 19230 2 66 157 SER . 19230 2 67 158 VAL . 19230 2 68 159 LYS . 19230 2 69 160 GLU . 19230 2 70 161 HIS . 19230 2 71 162 ARG . 19230 2 72 163 LYS . 19230 2 73 164 ILE . 19230 2 74 165 TYR . 19230 2 75 166 THR . 19230 2 76 167 MET . 19230 2 77 168 ILE . 19230 2 78 169 TYR . 19230 2 79 170 ARG . 19230 2 80 171 ASN . 19230 2 81 172 LEU . 19230 2 82 173 VAL . 19230 2 83 174 VAL . 19230 2 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . LEU 1 1 19230 2 . VAL 2 2 19230 2 . ARG 3 3 19230 2 . PRO 4 4 19230 2 . LYS 5 5 19230 2 . PRO 6 6 19230 2 . LEU 7 7 19230 2 . LEU 8 8 19230 2 . LEU 9 9 19230 2 . LYS 10 10 19230 2 . LEU 11 11 19230 2 . LEU 12 12 19230 2 . LYS 13 13 19230 2 . SER 14 14 19230 2 . VAL 15 15 19230 2 . GLY 16 16 19230 2 . ALA 17 17 19230 2 . GLN 18 18 19230 2 . LYS 19 19 19230 2 . ASP 20 20 19230 2 . THR 21 21 19230 2 . TYR 22 22 19230 2 . THR 23 23 19230 2 . MET 24 24 19230 2 . LYS 25 25 19230 2 . GLU 26 26 19230 2 . VAL 27 27 19230 2 . LEU 28 28 19230 2 . PHE 29 29 19230 2 . TYR 30 30 19230 2 . LEU 31 31 19230 2 . GLY 32 32 19230 2 . GLN 33 33 19230 2 . TYR 34 34 19230 2 . ILE 35 35 19230 2 . MET 36 36 19230 2 . THR 37 37 19230 2 . LYS 38 38 19230 2 . ARG 39 39 19230 2 . LEU 40 40 19230 2 . TYR 41 41 19230 2 . ASP 42 42 19230 2 . GLU 43 43 19230 2 . LYS 44 44 19230 2 . GLN 45 45 19230 2 . GLN 46 46 19230 2 . HIS 47 47 19230 2 . ILE 48 48 19230 2 . VAL 49 49 19230 2 . TYR 50 50 19230 2 . CYS 51 51 19230 2 . SER 52 52 19230 2 . ASN 53 53 19230 2 . ASP 54 54 19230 2 . LEU 55 55 19230 2 . LEU 56 56 19230 2 . GLY 57 57 19230 2 . ASP 58 58 19230 2 . LEU 59 59 19230 2 . PHE 60 60 19230 2 . GLY 61 61 19230 2 . VAL 62 62 19230 2 . PRO 63 63 19230 2 . SER 64 64 19230 2 . PHE 65 65 19230 2 . SER 66 66 19230 2 . VAL 67 67 19230 2 . LYS 68 68 19230 2 . GLU 69 69 19230 2 . HIS 70 70 19230 2 . ARG 71 71 19230 2 . LYS 72 72 19230 2 . ILE 73 73 19230 2 . TYR 74 74 19230 2 . THR 75 75 19230 2 . MET 76 76 19230 2 . ILE 77 77 19230 2 . TYR 78 78 19230 2 . ARG 79 79 19230 2 . ASN 80 80 19230 2 . LEU 81 81 19230 2 . VAL 82 82 19230 2 . VAL 83 83 19230 2 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 19230 _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 $Hdm2 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 19230 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 19230 _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 2 $MCo-PMI . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pTXB1 . . . . . . 19230 1 2 1 $Hdm2 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pet28a . . . . . . 19230 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 19230 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 MCo-PMI 'natural abundance' . . 2 $MCo-PMI . . 0.2 . . mM . . . . 19230 1 2 Hdm2 '[U-99% 13C; U-99% 15N]' . . 1 $Hdm2 . . 0.2 . . mM . . . . 19230 1 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 19230 1 4 D2O 'natural abundance' . . . . . . 10 . . % . . . . 19230 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 19230 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 MCo-PMI '[U-99% 15N]' . . 2 $MCo-PMI . . 0.2 . . mM . . . . 19230 2 2 Hdm2 'natural abundance' . . 1 $Hdm2 . . 0.2 . . mM . . . . 19230 2 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 19230 2 4 D2O 'natural abundance' . . . . . . 10 . . % . . . . 19230 2 stop_ save_ save_Sample_3 _Sample.Sf_category sample _Sample.Sf_framecode Sample_3 _Sample.Entry_ID 19230 _Sample.ID 3 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 MCo-PMI 'natural abundance' . . 2 $MCo-PMI . . 0.2 . . mM . . . . 19230 3 2 Hdm2 'natural abundance' . . 1 $Hdm2 . . 0.2 . . mM . . . . 19230 3 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 19230 3 4 D2O 'natural abundance' . . . . . . 10 . . % . . . . 19230 3 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 19230 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.133 . M 19230 1 pH 6.5 . pH 19230 1 pressure 1 . atm 19230 1 temperature 300 . K 19230 1 stop_ save_ ############################ # Computer software used # ############################ save_CHRMM _Software.Sf_category software _Software.Sf_framecode CHRMM _Software.Entry_ID 19230 _Software.ID 1 _Software.Name CHRMM _Software.Version 36 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'CHARMM-Karplus M.' . . 19230 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 19230 1 stop_ save_ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 19230 _Software.ID 2 _Software.Name CYANA _Software.Version 2.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 19230 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 19230 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 19230 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 19230 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 700 . . . 19230 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 19230 _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 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 2 '2D 1H-15N HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 3 '2D 1H-13C HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 4 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 5 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 6 '2D 1H-1H NOESY' no . . . . . . . . . . 3 $Sample_3 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 7 '3D 1H-13C NOESY aliphatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 8 '3D 1H-15N NOESY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 9 '3D 1H-15N TOCSY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 10 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 11 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 12 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 13 '2D 1H-1H TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19230 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 19230 _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 acetate 'methyl carbon' . . . . ppm 21.03 na indirect 1 . . . . . . . . . 19230 1 H 1 DSS 'methyl protons' . . . . ppm 0 external direct 1 . . . . . . . . . 19230 1 N 15 urea nitrogen . . . . ppm 73.4 na indirect 1 . . . . . . . . . 19230 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 19230 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 4 '3D 1H-15N NOESY' . . . 19230 1 5 '3D 1H-15N TOCSY' . . . 19230 1 7 '3D 1H-13C NOESY aliphatic' . . . 19230 1 8 '3D 1H-15N NOESY' . . . 19230 1 9 '3D 1H-15N TOCSY' . . . 19230 1 10 '3D HNCA' . . . 19230 1 11 '3D HN(CO)CA' . . . 19230 1 12 '3D HNCACB' . . . 19230 1 13 '2D 1H-1H TOCSY' . . . 19230 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 1 1 SER H H 1 8.648 0.020 . 1 . . . B 1 SER H . 19230 1 2 . 1 1 1 1 SER HA H 1 4.482 0.020 . 1 . . . B 1 SER HA . 19230 1 3 . 1 1 1 1 SER HB2 H 1 4.020 0.020 . 2 . . . B 1 SER HB2 . 19230 1 4 . 1 1 1 1 SER HB3 H 1 3.740 0.020 . 2 . . . B 1 SER HB3 . 19230 1 5 . 1 1 1 1 SER N N 15 115.471 0.300 . 1 . . . B 1 SER N . 19230 1 6 . 1 1 2 2 GLY H H 1 8.891 0.020 . 1 . . . B 2 GLY H . 19230 1 7 . 1 1 2 2 GLY HA2 H 1 3.709 0.020 . 2 . . . B 2 GLY HA2 . 19230 1 8 . 1 1 2 2 GLY HA3 H 1 4.003 0.020 . 2 . . . B 2 GLY HA3 . 19230 1 9 . 1 1 2 2 GLY N N 15 110.844 0.300 . 1 . . . B 2 GLY N . 19230 1 10 . 1 1 3 3 SER H H 1 8.320 0.020 . 1 . . . B 3 SER H . 19230 1 11 . 1 1 3 3 SER HA H 1 4.235 0.020 . 1 . . . B 3 SER HA . 19230 1 12 . 1 1 3 3 SER HB2 H 1 3.647 0.020 . 2 . . . B 3 SER QB . 19230 1 13 . 1 1 3 3 SER HB3 H 1 3.647 0.020 . 2 . . . B 3 SER QB . 19230 1 14 . 1 1 3 3 SER N N 15 115.464 0.300 . 1 . . . B 3 SER N . 19230 1 15 . 1 1 4 4 GLY H H 1 8.571 0.020 . 1 . . . B 4 GLY H . 19230 1 16 . 1 1 4 4 GLY HA2 H 1 3.585 0.020 . 2 . . . B 4 GLY QA . 19230 1 17 . 1 1 4 4 GLY HA3 H 1 3.585 0.020 . 2 . . . B 4 GLY QA . 19230 1 18 . 1 1 4 4 GLY N N 15 107.189 0.300 . 1 . . . B 4 GLY N . 19230 1 19 . 1 1 5 5 ALA H H 1 9.225 0.020 . 1 . . . B 5 ALA H . 19230 1 20 . 1 1 5 5 ALA HA H 1 3.585 0.020 . 1 . . . B 5 ALA HA . 19230 1 21 . 1 1 5 5 ALA HB1 H 1 1.297 0.020 . 1 . . . B 5 ALA QB . 19230 1 22 . 1 1 5 5 ALA HB2 H 1 1.297 0.020 . 1 . . . B 5 ALA QB . 19230 1 23 . 1 1 5 5 ALA HB3 H 1 1.297 0.020 . 1 . . . B 5 ALA QB . 19230 1 24 . 1 1 5 5 ALA N N 15 122.629 0.300 . 1 . . . B 5 ALA N . 19230 1 25 . 1 1 6 6 SER H H 1 8.291 0.020 . 1 . . . B 6 SER H . 19230 1 26 . 1 1 6 6 SER HA H 1 4.127 0.020 . 1 . . . B 6 SER HA . 19230 1 27 . 1 1 6 6 SER HB2 H 1 3.462 0.020 . 2 . . . B 6 SER QB . 19230 1 28 . 1 1 6 6 SER HB3 H 1 3.462 0.020 . 2 . . . B 6 SER QB . 19230 1 29 . 1 1 6 6 SER N N 15 119.024 0.300 . 1 . . . B 6 SER N . 19230 1 30 . 1 1 7 7 LYS H H 1 8.321 0.020 . 1 . . . B 7 LYS H . 19230 1 31 . 1 1 7 7 LYS HA H 1 4.266 0.020 . 1 . . . B 7 LYS HA . 19230 1 32 . 1 1 7 7 LYS HB2 H 1 2.318 0.020 . 2 . . . B 7 LYS QB . 19230 1 33 . 1 1 7 7 LYS HB3 H 1 2.318 0.020 . 2 . . . B 7 LYS QB . 19230 1 34 . 1 1 7 7 LYS HG2 H 1 1.050 0.020 . 2 . . . B 7 LYS QG . 19230 1 35 . 1 1 7 7 LYS HG3 H 1 1.050 0.020 . 2 . . . B 7 LYS QG . 19230 1 36 . 1 1 7 7 LYS N N 15 127.760 0.300 . 1 . . . B 7 LYS N . 19230 1 37 . 1 1 8 8 ALA H H 1 8.200 0.020 . 1 . . . B 8 ALA H . 19230 1 38 . 1 1 8 8 ALA HA H 1 4.219 0.020 . 1 . . . B 8 ALA HA . 19230 1 39 . 1 1 8 8 ALA HB1 H 1 1.034 0.020 . 1 . . . B 8 ALA QB . 19230 1 40 . 1 1 8 8 ALA HB2 H 1 1.034 0.020 . 1 . . . B 8 ALA QB . 19230 1 41 . 1 1 8 8 ALA HB3 H 1 1.034 0.020 . 1 . . . B 8 ALA QB . 19230 1 42 . 1 1 8 8 ALA N N 15 125.595 0.300 . 1 . . . B 8 ALA N . 19230 1 43 . 1 1 10 10 THR H H 1 8.107 0.020 . 1 . . . B 10 THR H . 19230 1 44 . 1 1 10 10 THR HA H 1 4.080 0.020 . 1 . . . B 10 THR HA . 19230 1 45 . 1 1 10 10 THR HB H 1 3.632 0.020 . 1 . . . B 10 THR HB . 19230 1 46 . 1 1 10 10 THR N N 15 111.647 0.300 . 1 . . . B 10 THR N . 19230 1 47 . 1 1 11 11 SER H H 1 8.216 0.020 . 1 . . . B 11 SER H . 19230 1 48 . 1 1 11 11 SER HA H 1 4.157 0.020 . 1 . . . B 11 SER HA . 19230 1 49 . 1 1 11 11 SER HB2 H 1 3.616 0.020 . 2 . . . B 11 SER QB . 19230 1 50 . 1 1 11 11 SER HB3 H 1 3.616 0.020 . 2 . . . B 11 SER QB . 19230 1 51 . 1 1 11 11 SER N N 15 115.520 0.300 . 1 . . . B 11 SER N . 19230 1 52 . 1 1 12 12 PHE H H 1 8.877 0.020 . 1 . . . B 12 PHE H . 19230 1 53 . 1 1 12 12 PHE HA H 1 4.018 0.020 . 1 . . . B 12 PHE HA . 19230 1 54 . 1 1 12 12 PHE HB2 H 1 3.060 0.020 . 2 . . . B 12 PHE QB . 19230 1 55 . 1 1 12 12 PHE HB3 H 1 3.060 0.020 . 2 . . . B 12 PHE QB . 19230 1 56 . 1 1 12 12 PHE N N 15 123.128 0.300 . 1 . . . B 12 PHE N . 19230 1 57 . 1 1 13 13 ALA H H 1 8.068 0.020 . 1 . . . B 13 ALA H . 19230 1 58 . 1 1 13 13 ALA HA H 1 4.157 0.020 . 1 . . . B 13 ALA HA . 19230 1 59 . 1 1 13 13 ALA HB1 H 1 1.189 0.020 . 1 . . . B 13 ALA QB . 19230 1 60 . 1 1 13 13 ALA HB2 H 1 1.189 0.020 . 1 . . . B 13 ALA QB . 19230 1 61 . 1 1 13 13 ALA HB3 H 1 1.189 0.020 . 1 . . . B 13 ALA QB . 19230 1 62 . 1 1 13 13 ALA N N 15 123.710 0.300 . 1 . . . B 13 ALA N . 19230 1 63 . 1 1 14 14 GLU H H 1 7.934 0.020 . 1 . . . B 14 GLU H . 19230 1 64 . 1 1 14 14 GLU HA H 1 4.142 0.020 . 1 . . . B 14 GLU HA . 19230 1 65 . 1 1 14 14 GLU HB2 H 1 1.576 0.020 . 2 . . . B 14 GLU HB2 . 19230 1 66 . 1 1 14 14 GLU HB3 H 1 1.189 0.020 . 2 . . . B 14 GLU HB3 . 19230 1 67 . 1 1 14 14 GLU N N 15 122.703 0.300 . 1 . . . B 14 GLU N . 19230 1 68 . 1 1 15 15 TYR H H 1 7.394 0.020 . 1 . . . B 15 TYR H . 19230 1 69 . 1 1 15 15 TYR HA H 1 4.343 0.020 . 1 . . . B 15 TYR HA . 19230 1 70 . 1 1 15 15 TYR HB2 H 1 2.936 0.020 . 2 . . . B 15 TYR QB . 19230 1 71 . 1 1 15 15 TYR HB3 H 1 2.936 0.020 . 2 . . . B 15 TYR QB . 19230 1 72 . 1 1 15 15 TYR N N 15 116.589 0.300 . 1 . . . B 15 TYR N . 19230 1 73 . 1 1 16 16 TRP H H 1 7.996 0.020 . 1 . . . B 16 TRP H . 19230 1 74 . 1 1 16 16 TRP HA H 1 4.034 0.020 . 1 . . . B 16 TRP HA . 19230 1 75 . 1 1 16 16 TRP HB2 H 1 2.627 0.020 . 2 . . . B 16 TRP QB . 19230 1 76 . 1 1 16 16 TRP HB3 H 1 2.627 0.020 . 2 . . . B 16 TRP QB . 19230 1 77 . 1 1 16 16 TRP N N 15 118.490 0.300 . 1 . . . B 16 TRP N . 19230 1 78 . 1 1 17 17 ASN H H 1 8.470 0.020 . 1 . . . B 17 ASN H . 19230 1 79 . 1 1 17 17 ASN HA H 1 4.328 0.020 . 1 . . . B 17 ASN HA . 19230 1 80 . 1 1 17 17 ASN N N 15 110.763 0.300 . 1 . . . B 17 ASN N . 19230 1 81 . 1 1 18 18 LEU H H 1 8.449 0.020 . 1 . . . B 18 LEU H . 19230 1 82 . 1 1 18 18 LEU HA H 1 3.771 0.020 . 1 . . . B 18 LEU HA . 19230 1 83 . 1 1 18 18 LEU N N 15 111.233 0.300 . 1 . . . B 18 LEU N . 19230 1 84 . 1 1 19 19 LEU H H 1 7.456 0.020 . 1 . . . B 19 LEU H . 19230 1 85 . 1 1 19 19 LEU HA H 1 4.018 0.020 . 1 . . . B 19 LEU HA . 19230 1 86 . 1 1 19 19 LEU HB2 H 1 1.792 0.020 . 2 . . . B 19 LEU QB . 19230 1 87 . 1 1 19 19 LEU HB3 H 1 1.792 0.020 . 2 . . . B 19 LEU QB . 19230 1 88 . 1 1 19 19 LEU N N 15 113.116 0.300 . 1 . . . B 19 LEU N . 19230 1 89 . 1 1 20 20 SER H H 1 8.003 0.020 . 1 . . . B 20 SER H . 19230 1 90 . 1 1 20 20 SER HA H 1 3.972 0.020 . 1 . . . B 20 SER HA . 19230 1 91 . 1 1 20 20 SER N N 15 111.251 0.300 . 1 . . . B 20 SER N . 19230 1 92 . 1 1 21 21 ALA H H 1 7.442 0.020 . 1 . . . B 21 ALA H . 19230 1 93 . 1 1 21 21 ALA HA H 1 4.111 0.020 . 1 . . . B 21 ALA HA . 19230 1 94 . 1 1 21 21 ALA HB1 H 1 1.220 0.020 . 1 . . . B 21 ALA QB . 19230 1 95 . 1 1 21 21 ALA HB2 H 1 1.220 0.020 . 1 . . . B 21 ALA QB . 19230 1 96 . 1 1 21 21 ALA HB3 H 1 1.220 0.020 . 1 . . . B 21 ALA QB . 19230 1 97 . 1 1 21 21 ALA N N 15 123.375 0.300 . 1 . . . B 21 ALA N . 19230 1 98 . 1 1 22 22 GLY H H 1 7.879 0.020 . 1 . . . B 22 GLY H . 19230 1 99 . 1 1 22 22 GLY HA2 H 1 3.740 0.020 . 2 . . . B 22 GLY QA . 19230 1 100 . 1 1 22 22 GLY HA3 H 1 3.740 0.020 . 2 . . . B 22 GLY QA . 19230 1 101 . 1 1 22 22 GLY N N 15 106.566 0.300 . 1 . . . B 22 GLY N . 19230 1 102 . 1 1 23 23 GLY H H 1 8.033 0.020 . 1 . . . B 23 GLY H . 19230 1 103 . 1 1 23 23 GLY HA2 H 1 3.740 0.020 . 2 . . . B 23 GLY QA . 19230 1 104 . 1 1 23 23 GLY HA3 H 1 3.740 0.020 . 2 . . . B 23 GLY QA . 19230 1 105 . 1 1 23 23 GLY N N 15 107.532 0.300 . 1 . . . B 23 GLY N . 19230 1 106 . 1 1 24 24 VAL H H 1 7.950 0.020 . 1 . . . B 24 VAL H . 19230 1 107 . 1 1 24 24 VAL HA H 1 3.987 0.020 . 1 . . . B 24 VAL HA . 19230 1 108 . 1 1 24 24 VAL HB H 1 1.807 0.020 . 1 . . . B 24 VAL HB . 19230 1 109 . 1 1 24 24 VAL HG11 H 1 0.648 0.020 . 2 . . . B 24 VAL QQG . 19230 1 110 . 1 1 24 24 VAL HG12 H 1 0.648 0.020 . 2 . . . B 24 VAL QQG . 19230 1 111 . 1 1 24 24 VAL HG13 H 1 0.648 0.020 . 2 . . . B 24 VAL QQG . 19230 1 112 . 1 1 24 24 VAL HG21 H 1 0.648 0.020 . 2 . . . B 24 VAL QQG . 19230 1 113 . 1 1 24 24 VAL HG22 H 1 0.648 0.020 . 2 . . . B 24 VAL QQG . 19230 1 114 . 1 1 24 24 VAL HG23 H 1 0.648 0.020 . 2 . . . B 24 VAL QQG . 19230 1 115 . 1 1 24 24 VAL N N 15 117.804 0.300 . 1 . . . B 24 VAL N . 19230 1 116 . 1 1 25 25 CYS H H 1 8.748 0.020 . 1 . . . B 25 CYS H . 19230 1 117 . 1 1 25 25 CYS HA H 1 4.961 0.020 . 1 . . . B 25 CYS HA . 19230 1 118 . 1 1 25 25 CYS HB2 H 1 2.565 0.020 . 2 . . . B 25 CYS HB2 . 19230 1 119 . 1 1 25 25 CYS HB3 H 1 2.900 0.020 . 2 . . . B 25 CYS HB3 . 19230 1 120 . 1 1 25 25 CYS N N 15 125.300 0.300 . 1 . . . B 25 CYS N . 19230 1 121 . 1 1 26 26 PRO HA H 1 4.420 0.020 . 1 . . . B 26 PRO HA . 19230 1 122 . 1 1 26 26 PRO HB2 H 1 2.360 0.020 . 2 . . . B 26 PRO HB2 . 19230 1 123 . 1 1 26 26 PRO HB3 H 1 1.900 0.020 . 2 . . . B 26 PRO HB3 . 19230 1 124 . 1 1 26 26 PRO HG2 H 1 2.050 0.020 . 2 . . . B 26 PRO HG2 . 19230 1 125 . 1 1 26 26 PRO HG3 H 1 1.980 0.020 . 2 . . . B 26 PRO HG3 . 19230 1 126 . 1 1 26 26 PRO HD2 H 1 3.890 0.020 . 2 . . . B 26 PRO HD2 . 19230 1 127 . 1 1 26 26 PRO HD3 H 1 3.890 0.020 . 2 . . . B 26 PRO HD3 . 19230 1 128 . 1 1 27 27 LYS H H 1 8.125 0.020 . 1 . . . B 27 LYS H . 19230 1 129 . 1 1 27 27 LYS HA H 1 4.096 0.020 . 1 . . . B 27 LYS HA . 19230 1 130 . 1 1 27 27 LYS HB2 H 1 1.622 0.020 . 2 . . . B 27 LYS HB2 . 19230 1 131 . 1 1 27 27 LYS HB3 H 1 1.890 0.020 . 2 . . . B 27 LYS HB3 . 19230 1 132 . 1 1 27 27 LYS HG2 H 1 1.520 0.020 . 2 . . . B 27 LYS HG2 . 19230 1 133 . 1 1 27 27 LYS HG3 H 1 1.420 0.020 . 2 . . . B 27 LYS HG3 . 19230 1 134 . 1 1 27 27 LYS HD2 H 1 1.740 0.020 . 2 . . . B 27 LYS HD2 . 19230 1 135 . 1 1 27 27 LYS HD3 H 1 1.740 0.020 . 2 . . . B 27 LYS HD3 . 19230 1 136 . 1 1 27 27 LYS HE2 H 1 3.040 0.020 . 2 . . . B 27 LYS HE2 . 19230 1 137 . 1 1 27 27 LYS HE3 H 1 3.040 0.020 . 2 . . . B 27 LYS HE3 . 19230 1 138 . 1 1 27 27 LYS N N 15 120.668 0.300 . 1 . . . B 27 LYS N . 19230 1 139 . 1 1 28 28 ILE H H 1 7.550 0.020 . 1 . . . B 28 ILE H . 19230 1 140 . 1 1 28 28 ILE HA H 1 4.204 0.020 . 1 . . . B 28 ILE HA . 19230 1 141 . 1 1 28 28 ILE HB H 1 1.653 0.020 . 1 . . . B 28 ILE HB . 19230 1 142 . 1 1 28 28 ILE HG12 H 1 1.390 0.020 . 2 . . . B 28 ILE HG12 . 19230 1 143 . 1 1 28 28 ILE HG13 H 1 1.120 0.020 . 2 . . . B 28 ILE HG13 . 19230 1 144 . 1 1 28 28 ILE N N 15 121.619 0.300 . 1 . . . B 28 ILE N . 19230 1 145 . 1 1 29 29 LEU H H 1 8.593 0.020 . 1 . . . B 29 LEU H . 19230 1 146 . 1 1 29 29 LEU HA H 1 4.358 0.020 . 1 . . . B 29 LEU HA . 19230 1 147 . 1 1 29 29 LEU HB2 H 1 1.560 0.020 . 2 . . . B 29 LEU HB2 . 19230 1 148 . 1 1 29 29 LEU HB3 H 1 1.550 0.020 . 2 . . . B 29 LEU HB3 . 19230 1 149 . 1 1 29 29 LEU HG H 1 1.297 0.020 . 1 . . . B 29 LEU HG . 19230 1 150 . 1 1 29 29 LEU N N 15 128.057 0.300 . 1 . . . B 29 LEU N . 19230 1 151 . 1 1 30 30 GLN H H 1 8.817 0.020 . 1 . . . B 30 GLN H . 19230 1 152 . 1 1 30 30 GLN HA H 1 4.358 0.020 . 1 . . . B 30 GLN HA . 19230 1 153 . 1 1 30 30 GLN HB2 H 1 1.916 0.020 . 2 . . . B 30 GLN HB2 . 19230 1 154 . 1 1 30 30 GLN HB3 H 1 1.390 0.020 . 2 . . . B 30 GLN HB3 . 19230 1 155 . 1 1 30 30 GLN HG2 H 1 2.287 0.020 . 2 . . . B 30 GLN QG . 19230 1 156 . 1 1 30 30 GLN HG3 H 1 2.287 0.020 . 2 . . . B 30 GLN QG . 19230 1 157 . 1 1 30 30 GLN N N 15 126.353 0.300 . 1 . . . B 30 GLN N . 19230 1 158 . 1 1 31 31 ARG H H 1 8.659 0.020 . 1 . . . B 31 ARG H . 19230 1 159 . 1 1 31 31 ARG HA H 1 4.266 0.020 . 1 . . . B 31 ARG HA . 19230 1 160 . 1 1 31 31 ARG HB2 H 1 1.436 0.020 . 2 . . . B 31 ARG QB . 19230 1 161 . 1 1 31 31 ARG HB3 H 1 1.436 0.020 . 2 . . . B 31 ARG QB . 19230 1 162 . 1 1 31 31 ARG N N 15 127.641 0.300 . 1 . . . B 31 ARG N . 19230 1 163 . 1 1 32 32 CYS H H 1 8.149 0.020 . 1 . . . B 32 CYS H . 19230 1 164 . 1 1 32 32 CYS HA H 1 4.940 0.020 . 1 . . . B 32 CYS HA . 19230 1 165 . 1 1 32 32 CYS HB2 H 1 3.250 0.020 . 2 . . . B 32 CYS HB2 . 19230 1 166 . 1 1 32 32 CYS HB3 H 1 2.980 0.020 . 2 . . . B 32 CYS HB3 . 19230 1 167 . 1 1 32 32 CYS N N 15 126.180 0.300 . 1 . . . B 32 CYS N . 19230 1 168 . 1 1 33 33 ARG H H 1 7.952 0.020 . 1 . . . B 33 ARG H . 19230 1 169 . 1 1 33 33 ARG HA H 1 4.575 0.020 . 1 . . . B 33 ARG HA . 19230 1 170 . 1 1 33 33 ARG HB2 H 1 1.930 0.020 . 2 . . . B 33 ARG HB2 . 19230 1 171 . 1 1 33 33 ARG HB3 H 1 1.545 0.020 . 2 . . . B 33 ARG HB3 . 19230 1 172 . 1 1 33 33 ARG HG2 H 1 1.680 0.020 . 2 . . . B 33 ARG HG2 . 19230 1 173 . 1 1 33 33 ARG HG3 H 1 1.680 0.020 . 2 . . . B 33 ARG HG3 . 19230 1 174 . 1 1 33 33 ARG HD2 H 1 3.200 0.020 . 2 . . . B 33 ARG HD2 . 19230 1 175 . 1 1 33 33 ARG HD3 H 1 3.240 0.020 . 2 . . . B 33 ARG HD3 . 19230 1 176 . 1 1 33 33 ARG HE H 1 7.320 0.020 . 1 . . . B 33 ARG HE . 19230 1 177 . 1 1 33 33 ARG N N 15 117.135 0.300 . 1 . . . B 33 ARG N . 19230 1 178 . 1 1 34 34 ARG H H 1 9.221 0.020 . 1 . . . B 34 ARG H . 19230 1 179 . 1 1 34 34 ARG HA H 1 4.266 0.020 . 1 . . . B 34 ARG HA . 19230 1 180 . 1 1 34 34 ARG HB2 H 1 2.070 0.020 . 2 . . . B 34 ARG HB2 . 19230 1 181 . 1 1 34 34 ARG HB3 H 1 1.576 0.020 . 2 . . . B 34 ARG HB3 . 19230 1 182 . 1 1 34 34 ARG HG2 H 1 1.610 0.020 . 2 . . . B 34 ARG HG2 . 19230 1 183 . 1 1 34 34 ARG HG3 H 1 1.510 0.020 . 2 . . . B 34 ARG HG3 . 19230 1 184 . 1 1 34 34 ARG HD2 H 1 3.200 0.020 . 2 . . . B 34 ARG HD2 . 19230 1 185 . 1 1 34 34 ARG HD3 H 1 3.200 0.020 . 2 . . . B 34 ARG HD3 . 19230 1 186 . 1 1 34 34 ARG HE H 1 7.190 0.020 . 1 . . . B 34 ARG HE . 19230 1 187 . 1 1 34 34 ARG N N 15 117.368 0.300 . 1 . . . B 34 ARG N . 19230 1 188 . 1 1 35 35 ASP H H 1 9.062 0.020 . 1 . . . B 35 ASP H . 19230 1 189 . 1 1 35 35 ASP HA H 1 4.559 0.020 . 1 . . . B 35 ASP HA . 19230 1 190 . 1 1 35 35 ASP HB2 H 1 2.256 0.020 . 2 . . . B 35 ASP HB2 . 19230 1 191 . 1 1 35 35 ASP HB3 H 1 3.020 0.020 . 2 . . . B 35 ASP HB3 . 19230 1 192 . 1 1 35 35 ASP N N 15 124.250 0.300 . 1 . . . B 35 ASP N . 19230 1 193 . 1 1 36 36 SER H H 1 8.009 0.020 . 1 . . . B 36 SER H . 19230 1 194 . 1 1 36 36 SER HA H 1 3.957 0.020 . 1 . . . B 36 SER HA . 19230 1 195 . 1 1 36 36 SER HB2 H 1 3.864 0.020 . 2 . . . B 36 SER HB2 . 19230 1 196 . 1 1 36 36 SER HB3 H 1 3.020 0.020 . 2 . . . B 36 SER HB3 . 19230 1 197 . 1 1 36 36 SER N N 15 111.255 0.300 . 1 . . . B 36 SER N . 19230 1 198 . 1 1 37 37 ASP H H 1 7.592 0.020 . 1 . . . B 37 ASP H . 19230 1 199 . 1 1 37 37 ASP HA H 1 4.374 0.020 . 1 . . . B 37 ASP HA . 19230 1 200 . 1 1 37 37 ASP HB2 H 1 2.101 0.020 . 2 . . . B 37 ASP HB2 . 19230 1 201 . 1 1 37 37 ASP HB3 H 1 3.080 0.020 . 2 . . . B 37 ASP HB3 . 19230 1 202 . 1 1 37 37 ASP N N 15 120.379 0.300 . 1 . . . B 37 ASP N . 19230 1 203 . 1 1 38 38 CYS H H 1 7.686 0.020 . 1 . . . B 38 CYS H . 19230 1 204 . 1 1 38 38 CYS HA H 1 4.668 0.020 . 1 . . . B 38 CYS HA . 19230 1 205 . 1 1 38 38 CYS HB2 H 1 2.900 0.020 . 2 . . . B 38 CYS HB2 . 19230 1 206 . 1 1 38 38 CYS HB3 H 1 2.581 0.020 . 2 . . . B 38 CYS HB3 . 19230 1 207 . 1 1 38 38 CYS N N 15 117.086 0.300 . 1 . . . B 38 CYS N . 19230 1 208 . 1 1 39 39 PRO HA H 1 4.670 0.020 . 1 . . . B 39 PRO HA . 19230 1 209 . 1 1 39 39 PRO HB2 H 1 2.320 0.020 . 2 . . . B 39 PRO HB2 . 19230 1 210 . 1 1 39 39 PRO HB3 H 1 1.980 0.020 . 2 . . . B 39 PRO HB3 . 19230 1 211 . 1 1 39 39 PRO HG2 H 1 2.130 0.020 . 2 . . . B 39 PRO HG2 . 19230 1 212 . 1 1 39 39 PRO HG3 H 1 2.080 0.020 . 2 . . . B 39 PRO HG3 . 19230 1 213 . 1 1 39 39 PRO HD2 H 1 3.790 0.020 . 2 . . . B 39 PRO HD2 . 19230 1 214 . 1 1 39 39 PRO HD3 H 1 3.480 0.020 . 2 . . . B 39 PRO HD3 . 19230 1 215 . 1 1 40 40 GLY H H 1 8.425 0.020 . 1 . . . B 40 GLY H . 19230 1 216 . 1 1 40 40 GLY HA2 H 1 3.632 0.020 . 2 . . . B 40 GLY HA2 . 19230 1 217 . 1 1 40 40 GLY HA3 H 1 3.800 0.020 . 2 . . . B 40 GLY HA3 . 19230 1 218 . 1 1 40 40 GLY N N 15 107.269 0.300 . 1 . . . B 40 GLY N . 19230 1 219 . 1 1 41 41 ALA H H 1 8.198 0.020 . 1 . . . B 41 ALA H . 19230 1 220 . 1 1 41 41 ALA HA H 1 4.219 0.020 . 1 . . . B 41 ALA HA . 19230 1 221 . 1 1 41 41 ALA HB1 H 1 1.034 0.020 . 1 . . . B 41 ALA QB . 19230 1 222 . 1 1 41 41 ALA HB2 H 1 1.034 0.020 . 1 . . . B 41 ALA QB . 19230 1 223 . 1 1 41 41 ALA HB3 H 1 1.034 0.020 . 1 . . . B 41 ALA QB . 19230 1 224 . 1 1 41 41 ALA N N 15 125.640 0.300 . 1 . . . B 41 ALA N . 19230 1 225 . 1 1 42 42 CYS H H 1 8.167 0.020 . 1 . . . B 42 CYS H . 19230 1 226 . 1 1 42 42 CYS HA H 1 4.358 0.020 . 1 . . . B 42 CYS HA . 19230 1 227 . 1 1 42 42 CYS HB2 H 1 3.260 0.020 . 2 . . . B 42 CYS HB2 . 19230 1 228 . 1 1 42 42 CYS HB3 H 1 3.260 0.020 . 2 . . . B 42 CYS HB3 . 19230 1 229 . 1 1 42 42 CYS N N 15 117.393 0.300 . 1 . . . B 42 CYS N . 19230 1 230 . 1 1 43 43 ILE H H 1 8.879 0.020 . 1 . . . B 43 ILE H . 19230 1 231 . 1 1 43 43 ILE HA H 1 4.250 0.020 . 1 . . . B 43 ILE HA . 19230 1 232 . 1 1 43 43 ILE HB H 1 2.209 0.020 . 1 . . . B 43 ILE HB . 19230 1 233 . 1 1 43 43 ILE HG12 H 1 1.120 0.020 . 2 . . . B 43 ILE HG12 . 19230 1 234 . 1 1 43 43 ILE HG13 H 1 1.020 0.020 . 2 . . . B 43 ILE HG13 . 19230 1 235 . 1 1 43 43 ILE N N 15 114.105 0.300 . 1 . . . B 43 ILE N . 19230 1 236 . 1 1 44 44 CYS H H 1 9.260 0.020 . 1 . . . B 44 CYS H . 19230 1 237 . 1 1 44 44 CYS HA H 1 4.745 0.020 . 1 . . . B 44 CYS HA . 19230 1 238 . 1 1 44 44 CYS HB2 H 1 2.256 0.020 . 2 . . . B 44 CYS HB2 . 19230 1 239 . 1 1 44 44 CYS HB3 H 1 2.642 0.020 . 2 . . . B 44 CYS HB3 . 19230 1 240 . 1 1 44 44 CYS N N 15 120.771 0.300 . 1 . . . B 44 CYS N . 19230 1 241 . 1 1 45 45 ARG H H 1 7.988 0.020 . 1 . . . B 45 ARG H . 19230 1 242 . 1 1 45 45 ARG HA H 1 4.111 0.020 . 1 . . . B 45 ARG HA . 19230 1 243 . 1 1 45 45 ARG HB2 H 1 2.318 0.020 . 2 . . . B 45 ARG HB2 . 19230 1 244 . 1 1 45 45 ARG HB3 H 1 2.110 0.020 . 2 . . . B 45 ARG HB3 . 19230 1 245 . 1 1 45 45 ARG HG2 H 1 1.800 0.020 . 2 . . . B 45 ARG HG2 . 19230 1 246 . 1 1 45 45 ARG HG3 H 1 1.421 0.020 . 2 . . . B 45 ARG HG3 . 19230 1 247 . 1 1 45 45 ARG HD2 H 1 3.300 0.020 . 2 . . . B 45 ARG HD2 . 19230 1 248 . 1 1 45 45 ARG HD3 H 1 3.300 0.020 . 2 . . . B 45 ARG HD3 . 19230 1 249 . 1 1 45 45 ARG N N 15 128.339 0.300 . 1 . . . B 45 ARG N . 19230 1 250 . 1 1 46 46 GLY H H 1 8.891 0.020 . 1 . . . B 46 GLY H . 19230 1 251 . 1 1 46 46 GLY HA2 H 1 3.740 0.020 . 2 . . . B 46 GLY HA2 . 19230 1 252 . 1 1 46 46 GLY HA3 H 1 3.740 0.020 . 2 . . . B 46 GLY HA3 . 19230 1 253 . 1 1 46 46 GLY N N 15 108.569 0.300 . 1 . . . B 46 GLY N . 19230 1 254 . 1 1 47 47 ASN H H 1 7.648 0.020 . 1 . . . B 47 ASN H . 19230 1 255 . 1 1 47 47 ASN HA H 1 4.482 0.020 . 1 . . . B 47 ASN HA . 19230 1 256 . 1 1 47 47 ASN HB2 H 1 3.230 0.020 . 2 . . . B 47 ASN HB2 . 19230 1 257 . 1 1 47 47 ASN HB3 H 1 2.920 0.020 . 2 . . . B 47 ASN HB3 . 19230 1 258 . 1 1 47 47 ASN HD21 H 1 7.306 0.020 . 2 . . . B 47 ASN HD21 . 19230 1 259 . 1 1 47 47 ASN HD22 H 1 6.928 0.020 . 2 . . . B 47 ASN HD22 . 19230 1 260 . 1 1 47 47 ASN N N 15 115.750 0.300 . 1 . . . B 47 ASN N . 19230 1 261 . 1 1 48 48 GLY H H 1 8.275 0.020 . 1 . . . B 48 GLY H . 19230 1 262 . 1 1 48 48 GLY HA2 H 1 3.802 0.020 . 2 . . . B 48 GLY HA2 . 19230 1 263 . 1 1 48 48 GLY HA3 H 1 3.508 0.020 . 2 . . . B 48 GLY HA3 . 19230 1 264 . 1 1 48 48 GLY N N 15 107.292 0.300 . 1 . . . B 48 GLY N . 19230 1 265 . 1 1 49 49 TYR H H 1 7.170 0.020 . 1 . . . B 49 TYR H . 19230 1 266 . 1 1 49 49 TYR HA H 1 5.054 0.020 . 1 . . . B 49 TYR HA . 19230 1 267 . 1 1 49 49 TYR HB2 H 1 2.503 0.020 . 2 . . . B 49 TYR HB2 . 19230 1 268 . 1 1 49 49 TYR HB3 H 1 2.905 0.020 . 2 . . . B 49 TYR HB3 . 19230 1 269 . 1 1 49 49 TYR HD1 H 1 6.930 0.020 . 3 . . . B 49 TYR HD1 . 19230 1 270 . 1 1 49 49 TYR HD2 H 1 6.930 0.020 . 3 . . . B 49 TYR HD2 . 19230 1 271 . 1 1 49 49 TYR HE1 H 1 6.760 0.020 . 3 . . . B 49 TYR HE1 . 19230 1 272 . 1 1 49 49 TYR HE2 H 1 6.760 0.020 . 3 . . . B 49 TYR HE2 . 19230 1 273 . 1 1 49 49 TYR N N 15 116.570 0.300 . 1 . . . B 49 TYR N . 19230 1 274 . 1 1 50 50 CYS H H 1 8.631 0.020 . 1 . . . B 50 CYS H . 19230 1 275 . 1 1 50 50 CYS HA H 1 5.286 0.020 . 1 . . . B 50 CYS HA . 19230 1 276 . 1 1 50 50 CYS HB2 H 1 3.214 0.020 . 2 . . . B 50 CYS HB2 . 19230 1 277 . 1 1 50 50 CYS HB3 H 1 2.860 0.020 . 2 . . . B 50 CYS HB3 . 19230 1 278 . 1 1 50 50 CYS N N 15 119.842 0.300 . 1 . . . B 50 CYS N . 19230 1 279 . 1 1 51 51 GLY H H 1 9.644 0.020 . 1 . . . B 51 GLY H . 19230 1 280 . 1 1 51 51 GLY HA2 H 1 4.281 0.020 . 2 . . . B 51 GLY HA2 . 19230 1 281 . 1 1 51 51 GLY HA3 H 1 3.771 0.020 . 2 . . . B 51 GLY HA3 . 19230 1 282 . 1 1 51 51 GLY N N 15 109.310 0.300 . 1 . . . B 51 GLY N . 19230 1 283 . 2 2 1 1 LEU H H 1 8.466 0.020 . 1 . . . A 92 LEU H . 19230 1 284 . 2 2 1 1 LEU HA H 1 4.218 0.020 . 1 . . . A 92 LEU HA . 19230 1 285 . 2 2 1 1 LEU HB2 H 1 1.553 0.020 . 2 . . . A 92 LEU HB2 . 19230 1 286 . 2 2 1 1 LEU HB3 H 1 1.894 0.020 . 2 . . . A 92 LEU HB3 . 19230 1 287 . 2 2 1 1 LEU HG H 1 1.197 0.020 . 1 . . . A 92 LEU HG . 19230 1 288 . 2 2 1 1 LEU CA C 13 51.393 0.300 . 1 . . . A 92 LEU CA . 19230 1 289 . 2 2 1 1 LEU CB C 13 40.770 0.300 . 1 . . . A 92 LEU CB . 19230 1 290 . 2 2 1 1 LEU N N 15 127.583 0.300 . 1 . . . A 92 LEU N . 19230 1 291 . 2 2 2 2 VAL H H 1 9.616 0.020 . 1 . . . A 93 VAL H . 19230 1 292 . 2 2 2 2 VAL HA H 1 4.326 0.020 . 1 . . . A 93 VAL HA . 19230 1 293 . 2 2 2 2 VAL HB H 1 1.971 0.020 . 1 . . . A 93 VAL HB . 19230 1 294 . 2 2 2 2 VAL CA C 13 55.881 0.300 . 1 . . . A 93 VAL CA . 19230 1 295 . 2 2 2 2 VAL CB C 13 33.232 0.300 . 1 . . . A 93 VAL CB . 19230 1 296 . 2 2 2 2 VAL N N 15 114.915 0.300 . 1 . . . A 93 VAL N . 19230 1 297 . 2 2 3 3 ARG H H 1 9.257 0.020 . 1 . . . A 94 ARG H . 19230 1 298 . 2 2 3 3 ARG HA H 1 4.373 0.020 . 1 . . . A 94 ARG HA . 19230 1 299 . 2 2 3 3 ARG HB2 H 1 1.816 0.020 . 2 . . . A 94 ARG HB2 . 19230 1 300 . 2 2 3 3 ARG HB3 H 1 1.816 0.020 . 2 . . . A 94 ARG HB3 . 19230 1 301 . 2 2 3 3 ARG HG2 H 1 1.460 0.020 . 2 . . . A 94 ARG HG2 . 19230 1 302 . 2 2 3 3 ARG HG3 H 1 1.460 0.020 . 2 . . . A 94 ARG HG3 . 19230 1 303 . 2 2 3 3 ARG HD2 H 1 3.009 0.020 . 2 . . . A 94 ARG HD2 . 19230 1 304 . 2 2 3 3 ARG HD3 H 1 3.009 0.020 . 2 . . . A 94 ARG HD3 . 19230 1 305 . 2 2 3 3 ARG CA C 13 55.914 0.300 . 1 . . . A 94 ARG CA . 19230 1 306 . 2 2 3 3 ARG CB C 13 29.375 0.300 . 1 . . . A 94 ARG CB . 19230 1 307 . 2 2 3 3 ARG N N 15 121.764 0.300 . 1 . . . A 94 ARG N . 19230 1 308 . 2 2 4 4 PRO CA C 13 62.949 0.300 . 1 . . . A 95 PRO CA . 19230 1 309 . 2 2 4 4 PRO CB C 13 32.675 0.300 . 1 . . . A 95 PRO CB . 19230 1 310 . 2 2 5 5 LYS H H 1 8.312 0.020 . 1 . . . A 96 LYS H . 19230 1 311 . 2 2 5 5 LYS CA C 13 56.775 0.300 . 1 . . . A 96 LYS CA . 19230 1 312 . 2 2 5 5 LYS N N 15 123.281 0.300 . 1 . . . A 96 LYS N . 19230 1 313 . 2 2 6 6 PRO CA C 13 67.588 0.300 . 1 . . . A 97 PRO CA . 19230 1 314 . 2 2 6 6 PRO CB C 13 32.651 0.300 . 1 . . . A 97 PRO CB . 19230 1 315 . 2 2 7 7 LEU H H 1 8.755 0.020 . 1 . . . A 98 LEU H . 19230 1 316 . 2 2 7 7 LEU HA H 1 4.280 0.020 . 1 . . . A 98 LEU HA . 19230 1 317 . 2 2 7 7 LEU HB2 H 1 1.460 0.020 . 2 . . . A 98 LEU HB2 . 19230 1 318 . 2 2 7 7 LEU HB3 H 1 1.460 0.020 . 2 . . . A 98 LEU HB3 . 19230 1 319 . 2 2 7 7 LEU HG H 1 1.305 0.020 . 1 . . . A 98 LEU HG . 19230 1 320 . 2 2 7 7 LEU CA C 13 52.779 0.300 . 1 . . . A 98 LEU CA . 19230 1 321 . 2 2 7 7 LEU CB C 13 41.455 0.300 . 1 . . . A 98 LEU CB . 19230 1 322 . 2 2 7 7 LEU N N 15 120.796 0.300 . 1 . . . A 98 LEU N . 19230 1 323 . 2 2 8 8 LEU H H 1 8.505 0.020 . 1 . . . A 99 LEU H . 19230 1 324 . 2 2 8 8 LEU HA H 1 4.076 0.020 . 1 . . . A 99 LEU HA . 19230 1 325 . 2 2 8 8 LEU CA C 13 53.241 0.300 . 1 . . . A 99 LEU CA . 19230 1 326 . 2 2 8 8 LEU CB C 13 40.798 0.300 . 1 . . . A 99 LEU CB . 19230 1 327 . 2 2 8 8 LEU N N 15 120.182 0.300 . 1 . . . A 99 LEU N . 19230 1 328 . 2 2 9 9 LEU H H 1 8.356 0.020 . 1 . . . A 100 LEU H . 19230 1 329 . 2 2 9 9 LEU HA H 1 4.156 0.020 . 1 . . . A 100 LEU HA . 19230 1 330 . 2 2 9 9 LEU HB2 H 1 1.801 0.020 . 2 . . . A 100 LEU HB2 . 19230 1 331 . 2 2 9 9 LEU HB3 H 1 1.801 0.020 . 2 . . . A 100 LEU HB3 . 19230 1 332 . 2 2 9 9 LEU CA C 13 53.373 0.300 . 1 . . . A 100 LEU CA . 19230 1 333 . 2 2 9 9 LEU N N 15 121.221 0.300 . 1 . . . A 100 LEU N . 19230 1 334 . 2 2 10 10 LYS H H 1 7.701 0.020 . 1 . . . A 101 LYS H . 19230 1 335 . 2 2 10 10 LYS HA H 1 4.233 0.020 . 1 . . . A 101 LYS HA . 19230 1 336 . 2 2 10 10 LYS HB2 H 1 1.630 0.020 . 2 . . . A 101 LYS HB2 . 19230 1 337 . 2 2 10 10 LYS HB3 H 1 1.630 0.020 . 2 . . . A 101 LYS HB3 . 19230 1 338 . 2 2 10 10 LYS HG2 H 1 1.429 0.020 . 2 . . . A 101 LYS HG2 . 19230 1 339 . 2 2 10 10 LYS HG3 H 1 1.429 0.020 . 2 . . . A 101 LYS HG3 . 19230 1 340 . 2 2 10 10 LYS CA C 13 56.881 0.300 . 1 . . . A 101 LYS CA . 19230 1 341 . 2 2 10 10 LYS CB C 13 29.298 0.300 . 1 . . . A 101 LYS CB . 19230 1 342 . 2 2 10 10 LYS N N 15 117.869 0.300 . 1 . . . A 101 LYS N . 19230 1 343 . 2 2 11 11 LEU H H 1 7.304 0.020 . 1 . . . A 102 LEU H . 19230 1 344 . 2 2 11 11 LEU HG H 1 1.476 0.020 . 1 . . . A 102 LEU HG . 19230 1 345 . 2 2 11 11 LEU CA C 13 56.881 0.300 . 1 . . . A 102 LEU CA . 19230 1 346 . 2 2 11 11 LEU CB C 13 41.160 0.300 . 1 . . . A 102 LEU CB . 19230 1 347 . 2 2 11 11 LEU N N 15 120.929 0.300 . 1 . . . A 102 LEU N . 19230 1 348 . 2 2 12 12 LEU H H 1 8.108 0.020 . 1 . . . A 103 LEU H . 19230 1 349 . 2 2 12 12 LEU HA H 1 4.063 0.020 . 1 . . . A 103 LEU HA . 19230 1 350 . 2 2 12 12 LEU HB2 H 1 1.940 0.020 . 2 . . . A 103 LEU HB2 . 19230 1 351 . 2 2 12 12 LEU HB3 H 1 1.940 0.020 . 2 . . . A 103 LEU HB3 . 19230 1 352 . 2 2 12 12 LEU CA C 13 56.673 0.300 . 1 . . . A 103 LEU CA . 19230 1 353 . 2 2 12 12 LEU CB C 13 39.131 0.300 . 1 . . . A 103 LEU CB . 19230 1 354 . 2 2 12 12 LEU N N 15 119.513 0.300 . 1 . . . A 103 LEU N . 19230 1 355 . 2 2 13 13 LYS H H 1 8.618 0.020 . 1 . . . A 104 LYS H . 19230 1 356 . 2 2 13 13 LYS HA H 1 4.078 0.020 . 1 . . . A 104 LYS HA . 19230 1 357 . 2 2 13 13 LYS HB2 H 1 1.584 0.020 . 2 . . . A 104 LYS HB2 . 19230 1 358 . 2 2 13 13 LYS HB3 H 1 1.584 0.020 . 2 . . . A 104 LYS HB3 . 19230 1 359 . 2 2 13 13 LYS CA C 13 56.541 0.300 . 1 . . . A 104 LYS CA . 19230 1 360 . 2 2 13 13 LYS CB C 13 29.375 0.300 . 1 . . . A 104 LYS CB . 19230 1 361 . 2 2 13 13 LYS N N 15 118.036 0.300 . 1 . . . A 104 LYS N . 19230 1 362 . 2 2 14 14 SER H H 1 7.724 0.020 . 1 . . . A 105 SER H . 19230 1 363 . 2 2 14 14 SER HA H 1 4.249 0.020 . 1 . . . A 105 SER HA . 19230 1 364 . 2 2 14 14 SER HB2 H 1 3.567 0.020 . 2 . . . A 105 SER HB2 . 19230 1 365 . 2 2 14 14 SER HB3 H 1 3.567 0.020 . 2 . . . A 105 SER HB3 . 19230 1 366 . 2 2 14 14 SER CA C 13 58.851 0.300 . 1 . . . A 105 SER CA . 19230 1 367 . 2 2 14 14 SER CB C 13 60.831 0.300 . 1 . . . A 105 SER CB . 19230 1 368 . 2 2 14 14 SER N N 15 116.461 0.300 . 1 . . . A 105 SER N . 19230 1 369 . 2 2 15 15 VAL H H 1 7.106 0.020 . 1 . . . A 106 VAL H . 19230 1 370 . 2 2 15 15 VAL HA H 1 4.572 0.020 . 1 . . . A 106 VAL HA . 19230 1 371 . 2 2 15 15 VAL HB H 1 1.882 0.020 . 1 . . . A 106 VAL HB . 19230 1 372 . 2 2 15 15 VAL CA C 13 57.630 0.300 . 1 . . . A 106 VAL CA . 19230 1 373 . 2 2 15 15 VAL CB C 13 28.220 0.300 . 1 . . . A 106 VAL CB . 19230 1 374 . 2 2 15 15 VAL N N 15 112.682 0.300 . 1 . . . A 106 VAL N . 19230 1 375 . 2 2 16 16 GLY H H 1 7.339 0.020 . 1 . . . A 107 GLY H . 19230 1 376 . 2 2 16 16 GLY HA2 H 1 4.247 0.020 . 2 . . . A 107 GLY HA2 . 19230 1 377 . 2 2 16 16 GLY HA3 H 1 3.567 0.020 . 2 . . . A 107 GLY HA3 . 19230 1 378 . 2 2 16 16 GLY CA C 13 42.648 0.300 . 1 . . . A 107 GLY CA . 19230 1 379 . 2 2 16 16 GLY N N 15 105.947 0.300 . 1 . . . A 107 GLY N . 19230 1 380 . 2 2 17 17 ALA H H 1 7.207 0.020 . 1 . . . A 108 ALA H . 19230 1 381 . 2 2 17 17 ALA HA H 1 3.892 0.020 . 1 . . . A 108 ALA HA . 19230 1 382 . 2 2 17 17 ALA HB1 H 1 1.026 0.020 . 1 . . . A 108 ALA HB1 . 19230 1 383 . 2 2 17 17 ALA HB2 H 1 1.026 0.020 . 1 . . . A 108 ALA HB2 . 19230 1 384 . 2 2 17 17 ALA HB3 H 1 1.026 0.020 . 1 . . . A 108 ALA HB3 . 19230 1 385 . 2 2 17 17 ALA CA C 13 50.205 0.300 . 1 . . . A 108 ALA CA . 19230 1 386 . 2 2 17 17 ALA CB C 13 15.593 0.300 . 1 . . . A 108 ALA CB . 19230 1 387 . 2 2 17 17 ALA N N 15 124.763 0.300 . 1 . . . A 108 ALA N . 19230 1 388 . 2 2 18 18 GLN H H 1 8.638 0.020 . 1 . . . A 109 GLN H . 19230 1 389 . 2 2 18 18 GLN HA H 1 4.373 0.020 . 1 . . . A 109 GLN HA . 19230 1 390 . 2 2 18 18 GLN HB2 H 1 1.522 0.020 . 2 . . . A 109 GLN HB2 . 19230 1 391 . 2 2 18 18 GLN HB3 H 1 1.522 0.020 . 2 . . . A 109 GLN HB3 . 19230 1 392 . 2 2 18 18 GLN CA C 13 52.746 0.300 . 1 . . . A 109 GLN CA . 19230 1 393 . 2 2 18 18 GLN CB C 13 29.452 0.300 . 1 . . . A 109 GLN CB . 19230 1 394 . 2 2 18 18 GLN N N 15 117.687 0.300 . 1 . . . A 109 GLN N . 19230 1 395 . 2 2 19 19 LYS H H 1 7.191 0.020 . 1 . . . A 110 LYS H . 19230 1 396 . 2 2 19 19 LYS HA H 1 3.985 0.020 . 1 . . . A 110 LYS HA . 19230 1 397 . 2 2 19 19 LYS HB2 H 1 1.584 0.020 . 2 . . . A 110 LYS HB2 . 19230 1 398 . 2 2 19 19 LYS HB3 H 1 1.584 0.020 . 2 . . . A 110 LYS HB3 . 19230 1 399 . 2 2 19 19 LYS HG2 H 1 1.491 0.020 . 2 . . . A 110 LYS HG2 . 19230 1 400 . 2 2 19 19 LYS HG3 H 1 1.491 0.020 . 2 . . . A 110 LYS HG3 . 19230 1 401 . 2 2 19 19 LYS HE2 H 1 3.056 0.020 . 2 . . . A 110 LYS HE2 . 19230 1 402 . 2 2 19 19 LYS HE3 H 1 3.056 0.020 . 2 . . . A 110 LYS HE3 . 19230 1 403 . 2 2 19 19 LYS CA C 13 52.647 0.300 . 1 . . . A 110 LYS CA . 19230 1 404 . 2 2 19 19 LYS CB C 13 31.993 0.300 . 1 . . . A 110 LYS CB . 19230 1 405 . 2 2 19 19 LYS N N 15 118.004 0.300 . 1 . . . A 110 LYS N . 19230 1 406 . 2 2 20 20 ASP H H 1 8.375 0.020 . 1 . . . A 111 ASP H . 19230 1 407 . 2 2 20 20 ASP CA C 13 55.178 0.300 . 1 . . . A 111 ASP CA . 19230 1 408 . 2 2 20 20 ASP N N 15 120.877 0.300 . 1 . . . A 111 ASP N . 19230 1 409 . 2 2 21 21 THR H H 1 6.921 0.020 . 1 . . . A 112 THR H . 19230 1 410 . 2 2 21 21 THR HA H 1 4.497 0.020 . 1 . . . A 112 THR HA . 19230 1 411 . 2 2 21 21 THR HB H 1 4.280 0.020 . 1 . . . A 112 THR HB . 19230 1 412 . 2 2 21 21 THR HG21 H 1 1.181 0.020 . 1 . . . A 112 THR HG2 . 19230 1 413 . 2 2 21 21 THR HG22 H 1 1.181 0.020 . 1 . . . A 112 THR HG2 . 19230 1 414 . 2 2 21 21 THR HG23 H 1 1.181 0.020 . 1 . . . A 112 THR HG2 . 19230 1 415 . 2 2 21 21 THR CA C 13 57.828 0.300 . 1 . . . A 112 THR CA . 19230 1 416 . 2 2 21 21 THR CB C 13 68.643 0.300 . 1 . . . A 112 THR CB . 19230 1 417 . 2 2 21 21 THR N N 15 111.257 0.300 . 1 . . . A 112 THR N . 19230 1 418 . 2 2 22 22 TYR H H 1 8.707 0.020 . 1 . . . A 113 TYR H . 19230 1 419 . 2 2 22 22 TYR HA H 1 4.775 0.020 . 1 . . . A 113 TYR HA . 19230 1 420 . 2 2 22 22 TYR HB2 H 1 3.195 0.020 . 2 . . . A 113 TYR HB2 . 19230 1 421 . 2 2 22 22 TYR HB3 H 1 3.195 0.020 . 2 . . . A 113 TYR HB3 . 19230 1 422 . 2 2 22 22 TYR CA C 13 54.495 0.300 . 1 . . . A 113 TYR CA . 19230 1 423 . 2 2 22 22 TYR CB C 13 36.463 0.300 . 1 . . . A 113 TYR CB . 19230 1 424 . 2 2 22 22 TYR N N 15 120.011 0.300 . 1 . . . A 113 TYR N . 19230 1 425 . 2 2 23 23 THR H H 1 8.915 0.020 . 1 . . . A 114 THR H . 19230 1 426 . 2 2 23 23 THR HA H 1 4.404 0.020 . 1 . . . A 114 THR HA . 19230 1 427 . 2 2 23 23 THR HB H 1 3.892 0.020 . 1 . . . A 114 THR HB . 19230 1 428 . 2 2 23 23 THR HG21 H 1 1.181 0.020 . 1 . . . A 114 THR HG2 . 19230 1 429 . 2 2 23 23 THR HG22 H 1 1.181 0.020 . 1 . . . A 114 THR HG2 . 19230 1 430 . 2 2 23 23 THR HG23 H 1 1.181 0.020 . 1 . . . A 114 THR HG2 . 19230 1 431 . 2 2 23 23 THR CA C 13 57.729 0.300 . 1 . . . A 114 THR CA . 19230 1 432 . 2 2 23 23 THR CB C 13 68.181 0.300 . 1 . . . A 114 THR CB . 19230 1 433 . 2 2 23 23 THR N N 15 109.880 0.300 . 1 . . . A 114 THR N . 19230 1 434 . 2 2 24 24 MET H H 1 8.714 0.020 . 1 . . . A 115 MET H . 19230 1 435 . 2 2 24 24 MET HA H 1 4.249 0.020 . 1 . . . A 115 MET HA . 19230 1 436 . 2 2 24 24 MET CA C 13 53.670 0.300 . 1 . . . A 115 MET CA . 19230 1 437 . 2 2 24 24 MET CB C 13 31.800 0.300 . 1 . . . A 115 MET CB . 19230 1 438 . 2 2 24 24 MET N N 15 121.767 0.300 . 1 . . . A 115 MET N . 19230 1 439 . 2 2 25 25 LYS H H 1 8.458 0.020 . 1 . . . A 116 LYS H . 19230 1 440 . 2 2 25 25 LYS HA H 1 4.280 0.020 . 1 . . . A 116 LYS HA . 19230 1 441 . 2 2 25 25 LYS HB2 H 1 1.414 0.020 . 2 . . . A 116 LYS HB2 . 19230 1 442 . 2 2 25 25 LYS HB3 H 1 1.414 0.020 . 2 . . . A 116 LYS HB3 . 19230 1 443 . 2 2 25 25 LYS HG2 H 1 1.197 0.020 . 2 . . . A 116 LYS HG2 . 19230 1 444 . 2 2 25 25 LYS HG3 H 1 1.197 0.020 . 2 . . . A 116 LYS HG3 . 19230 1 445 . 2 2 25 25 LYS CA C 13 55.518 0.300 . 1 . . . A 116 LYS CA . 19230 1 446 . 2 2 25 25 LYS CB C 13 27.219 0.300 . 1 . . . A 116 LYS CB . 19230 1 447 . 2 2 25 25 LYS N N 15 116.611 0.300 . 1 . . . A 116 LYS N . 19230 1 448 . 2 2 26 26 GLU H H 1 8.098 0.020 . 1 . . . A 117 GLU H . 19230 1 449 . 2 2 26 26 GLU HA H 1 4.032 0.020 . 1 . . . A 117 GLU HA . 19230 1 450 . 2 2 26 26 GLU HB2 H 1 1.770 0.020 . 2 . . . A 117 GLU HB2 . 19230 1 451 . 2 2 26 26 GLU HB3 H 1 1.770 0.020 . 2 . . . A 117 GLU HB3 . 19230 1 452 . 2 2 26 26 GLU HG2 H 1 1.940 0.020 . 2 . . . A 117 GLU HG2 . 19230 1 453 . 2 2 26 26 GLU HG3 H 1 1.940 0.020 . 2 . . . A 117 GLU HG3 . 19230 1 454 . 2 2 26 26 GLU CA C 13 59.181 0.300 . 1 . . . A 117 GLU CA . 19230 1 455 . 2 2 26 26 GLU CB C 13 27.681 0.300 . 1 . . . A 117 GLU CB . 19230 1 456 . 2 2 26 26 GLU N N 15 121.352 0.300 . 1 . . . A 117 GLU N . 19230 1 457 . 2 2 27 27 VAL H H 1 8.249 0.020 . 1 . . . A 118 VAL H . 19230 1 458 . 2 2 27 27 VAL HA H 1 4.280 0.020 . 1 . . . A 118 VAL HA . 19230 1 459 . 2 2 27 27 VAL HB H 1 2.157 0.020 . 1 . . . A 118 VAL HB . 19230 1 460 . 2 2 27 27 VAL HG11 H 1 0.949 0.020 . 2 . . . A 118 VAL HG11 . 19230 1 461 . 2 2 27 27 VAL HG12 H 1 0.949 0.020 . 2 . . . A 118 VAL HG12 . 19230 1 462 . 2 2 27 27 VAL HG13 H 1 0.949 0.020 . 2 . . . A 118 VAL HG13 . 19230 1 463 . 2 2 27 27 VAL HG21 H 1 0.949 0.020 . 2 . . . A 118 VAL HG21 . 19230 1 464 . 2 2 27 27 VAL HG22 H 1 0.949 0.020 . 2 . . . A 118 VAL HG22 . 19230 1 465 . 2 2 27 27 VAL HG23 H 1 0.949 0.020 . 2 . . . A 118 VAL HG23 . 19230 1 466 . 2 2 27 27 VAL CA C 13 55.485 0.300 . 1 . . . A 118 VAL CA . 19230 1 467 . 2 2 27 27 VAL CB C 13 30.520 0.300 . 1 . . . A 118 VAL CB . 19230 1 468 . 2 2 27 27 VAL N N 15 119.299 0.300 . 1 . . . A 118 VAL N . 19230 1 469 . 2 2 28 28 LEU H H 1 8.398 0.020 . 1 . . . A 119 LEU H . 19230 1 470 . 2 2 28 28 LEU HA H 1 3.972 0.020 . 1 . . . A 119 LEU HA . 19230 1 471 . 2 2 28 28 LEU CA C 13 52.581 0.300 . 1 . . . A 119 LEU CA . 19230 1 472 . 2 2 28 28 LEU CB C 13 40.829 0.300 . 1 . . . A 119 LEU CB . 19230 1 473 . 2 2 28 28 LEU N N 15 120.244 0.300 . 1 . . . A 119 LEU N . 19230 1 474 . 2 2 29 29 PHE H H 1 8.061 0.020 . 1 . . . A 120 PHE H . 19230 1 475 . 2 2 29 29 PHE CA C 13 61.535 0.300 . 1 . . . A 120 PHE CA . 19230 1 476 . 2 2 29 29 PHE CB C 13 38.408 0.300 . 1 . . . A 120 PHE CB . 19230 1 477 . 2 2 29 29 PHE N N 15 121.826 0.300 . 1 . . . A 120 PHE N . 19230 1 478 . 2 2 30 30 TYR H H 1 8.508 0.020 . 1 . . . A 121 TYR H . 19230 1 479 . 2 2 30 30 TYR HA H 1 4.218 0.020 . 1 . . . A 121 TYR HA . 19230 1 480 . 2 2 30 30 TYR HB2 H 1 2.839 0.020 . 2 . . . A 121 TYR HB2 . 19230 1 481 . 2 2 30 30 TYR HB3 H 1 2.839 0.020 . 2 . . . A 121 TYR HB3 . 19230 1 482 . 2 2 30 30 TYR CA C 13 59.907 0.300 . 1 . . . A 121 TYR CA . 19230 1 483 . 2 2 30 30 TYR CB C 13 36.305 0.300 . 1 . . . A 121 TYR CB . 19230 1 484 . 2 2 30 30 TYR N N 15 119.025 0.300 . 1 . . . A 121 TYR N . 19230 1 485 . 2 2 31 31 LEU H H 1 8.674 0.020 . 1 . . . A 122 LEU H . 19230 1 486 . 2 2 31 31 LEU HA H 1 4.419 0.020 . 1 . . . A 122 LEU HA . 19230 1 487 . 2 2 31 31 LEU HB2 H 1 1.599 0.020 . 2 . . . A 122 LEU HB2 . 19230 1 488 . 2 2 31 31 LEU HB3 H 1 1.599 0.020 . 2 . . . A 122 LEU HB3 . 19230 1 489 . 2 2 31 31 LEU HG H 1 1.491 0.020 . 1 . . . A 122 LEU HG . 19230 1 490 . 2 2 31 31 LEU HD11 H 1 0.654 0.020 . 2 . . . A 122 LEU HD11 . 19230 1 491 . 2 2 31 31 LEU HD12 H 1 0.654 0.020 . 2 . . . A 122 LEU HD12 . 19230 1 492 . 2 2 31 31 LEU HD13 H 1 0.654 0.020 . 2 . . . A 122 LEU HD13 . 19230 1 493 . 2 2 31 31 LEU HD21 H 1 0.654 0.020 . 2 . . . A 122 LEU HD21 . 19230 1 494 . 2 2 31 31 LEU HD22 H 1 0.654 0.020 . 2 . . . A 122 LEU HD22 . 19230 1 495 . 2 2 31 31 LEU HD23 H 1 0.654 0.020 . 2 . . . A 122 LEU HD23 . 19230 1 496 . 2 2 31 31 LEU CA C 13 55.419 0.300 . 1 . . . A 122 LEU CA . 19230 1 497 . 2 2 31 31 LEU CB C 13 40.000 0.300 . 1 . . . A 122 LEU CB . 19230 1 498 . 2 2 31 31 LEU N N 15 120.471 0.300 . 1 . . . A 122 LEU N . 19230 1 499 . 2 2 32 32 GLY H H 1 8.013 0.020 . 1 . . . A 123 GLY H . 19230 1 500 . 2 2 32 32 GLY HA2 H 1 3.939 0.020 . 2 . . . A 123 GLY HA2 . 19230 1 501 . 2 2 32 32 GLY HA3 H 1 3.939 0.020 . 2 . . . A 123 GLY HA3 . 19230 1 502 . 2 2 32 32 GLY CA C 13 43.374 0.300 . 1 . . . A 123 GLY CA . 19230 1 503 . 2 2 32 32 GLY N N 15 106.532 0.300 . 1 . . . A 123 GLY N . 19230 1 504 . 2 2 33 33 GLN H H 1 7.508 0.020 . 1 . . . A 124 GLN H . 19230 1 505 . 2 2 33 33 GLN HA H 1 3.923 0.020 . 1 . . . A 124 GLN HA . 19230 1 506 . 2 2 33 33 GLN HB2 H 1 2.204 0.020 . 2 . . . A 124 GLN HB2 . 19230 1 507 . 2 2 33 33 GLN HB3 H 1 2.204 0.020 . 2 . . . A 124 GLN HB3 . 19230 1 508 . 2 2 33 33 GLN HG2 H 1 2.312 0.020 . 2 . . . A 124 GLN HG2 . 19230 1 509 . 2 2 33 33 GLN HG3 H 1 2.312 0.020 . 2 . . . A 124 GLN HG3 . 19230 1 510 . 2 2 33 33 GLN CA C 13 55.386 0.300 . 1 . . . A 124 GLN CA . 19230 1 511 . 2 2 33 33 GLN CB C 13 26.064 0.300 . 1 . . . A 124 GLN CB . 19230 1 512 . 2 2 33 33 GLN N N 15 118.850 0.300 . 1 . . . A 124 GLN N . 19230 1 513 . 2 2 34 34 TYR H H 1 8.441 0.020 . 1 . . . A 125 TYR H . 19230 1 514 . 2 2 34 34 TYR HA H 1 4.249 0.020 . 1 . . . A 125 TYR HA . 19230 1 515 . 2 2 34 34 TYR HB2 H 1 2.684 0.020 . 2 . . . A 125 TYR HB2 . 19230 1 516 . 2 2 34 34 TYR HB3 H 1 2.684 0.020 . 2 . . . A 125 TYR HB3 . 19230 1 517 . 2 2 34 34 TYR CA C 13 59.808 0.300 . 1 . . . A 125 TYR CA . 19230 1 518 . 2 2 34 34 TYR CB C 13 38.769 0.300 . 1 . . . A 125 TYR CB . 19230 1 519 . 2 2 34 34 TYR N N 15 123.374 0.300 . 1 . . . A 125 TYR N . 19230 1 520 . 2 2 35 35 ILE H H 1 8.587 0.020 . 1 . . . A 126 ILE H . 19230 1 521 . 2 2 35 35 ILE HA H 1 4.109 0.020 . 1 . . . A 126 ILE HA . 19230 1 522 . 2 2 35 35 ILE HB H 1 1.754 0.020 . 1 . . . A 126 ILE HB . 19230 1 523 . 2 2 35 35 ILE HG12 H 1 1.026 0.020 . 2 . . . A 126 ILE HG12 . 19230 1 524 . 2 2 35 35 ILE HG13 H 1 1.026 0.020 . 2 . . . A 126 ILE HG13 . 19230 1 525 . 2 2 35 35 ILE HD11 H 1 0.561 0.020 . 1 . . . A 126 ILE HD11 . 19230 1 526 . 2 2 35 35 ILE HD12 H 1 0.561 0.020 . 1 . . . A 126 ILE HD12 . 19230 1 527 . 2 2 35 35 ILE HD13 H 1 0.561 0.020 . 1 . . . A 126 ILE HD13 . 19230 1 528 . 2 2 35 35 ILE CA C 13 53.637 0.300 . 1 . . . A 126 ILE CA . 19230 1 529 . 2 2 35 35 ILE CB C 13 34.765 0.300 . 1 . . . A 126 ILE CB . 19230 1 530 . 2 2 35 35 ILE N N 15 121.486 0.300 . 1 . . . A 126 ILE N . 19230 1 531 . 2 2 36 36 MET H H 1 7.939 0.020 . 1 . . . A 127 MET H . 19230 1 532 . 2 2 36 36 MET HA H 1 4.280 0.020 . 1 . . . A 127 MET HA . 19230 1 533 . 2 2 36 36 MET HB2 H 1 2.064 0.020 . 2 . . . A 127 MET HB2 . 19230 1 534 . 2 2 36 36 MET HB3 H 1 1.956 0.020 . 2 . . . A 127 MET HB3 . 19230 1 535 . 2 2 36 36 MET HE1 H 1 1.584 0.020 . 1 . . . A 127 MET HE1 . 19230 1 536 . 2 2 36 36 MET HE2 H 1 1.584 0.020 . 1 . . . A 127 MET HE2 . 19230 1 537 . 2 2 36 36 MET HE3 H 1 1.584 0.020 . 1 . . . A 127 MET HE3 . 19230 1 538 . 2 2 36 36 MET CA C 13 56.863 0.300 . 1 . . . A 127 MET CA . 19230 1 539 . 2 2 36 36 MET CB C 13 30.838 0.300 . 1 . . . A 127 MET CB . 19230 1 540 . 2 2 36 36 MET N N 15 115.880 0.300 . 1 . . . A 127 MET N . 19230 1 541 . 2 2 37 37 THR H H 1 8.408 0.020 . 1 . . . A 128 THR H . 19230 1 542 . 2 2 37 37 THR HA H 1 4.280 0.020 . 1 . . . A 128 THR HA . 19230 1 543 . 2 2 37 37 THR HB H 1 3.768 0.020 . 1 . . . A 128 THR HB . 19230 1 544 . 2 2 37 37 THR HG21 H 1 1.135 0.020 . 1 . . . A 128 THR HG2 . 19230 1 545 . 2 2 37 37 THR HG22 H 1 1.135 0.020 . 1 . . . A 128 THR HG2 . 19230 1 546 . 2 2 37 37 THR HG23 H 1 1.135 0.020 . 1 . . . A 128 THR HG2 . 19230 1 547 . 2 2 37 37 THR CA C 13 63.241 0.300 . 1 . . . A 128 THR CA . 19230 1 548 . 2 2 37 37 THR CB C 13 65.948 0.300 . 1 . . . A 128 THR CB . 19230 1 549 . 2 2 37 37 THR N N 15 115.174 0.300 . 1 . . . A 128 THR N . 19230 1 550 . 2 2 38 38 LYS H H 1 7.373 0.020 . 1 . . . A 129 LYS H . 19230 1 551 . 2 2 38 38 LYS HA H 1 3.830 0.020 . 1 . . . A 129 LYS HA . 19230 1 552 . 2 2 38 38 LYS HB2 H 1 1.770 0.020 . 2 . . . A 129 LYS HB2 . 19230 1 553 . 2 2 38 38 LYS HB3 H 1 1.770 0.020 . 2 . . . A 129 LYS HB3 . 19230 1 554 . 2 2 38 38 LYS HG2 H 1 1.569 0.020 . 2 . . . A 129 LYS HG2 . 19230 1 555 . 2 2 38 38 LYS HG3 H 1 1.569 0.020 . 2 . . . A 129 LYS HG3 . 19230 1 556 . 2 2 38 38 LYS CA C 13 53.449 0.300 . 1 . . . A 129 LYS CA . 19230 1 557 . 2 2 38 38 LYS CB C 13 28.297 0.300 . 1 . . . A 129 LYS CB . 19230 1 558 . 2 2 38 38 LYS N N 15 118.205 0.300 . 1 . . . A 129 LYS N . 19230 1 559 . 2 2 39 39 ARG H H 1 7.349 0.020 . 1 . . . A 130 ARG H . 19230 1 560 . 2 2 39 39 ARG HA H 1 4.001 0.020 . 1 . . . A 130 ARG HA . 19230 1 561 . 2 2 39 39 ARG HB2 H 1 1.553 0.020 . 2 . . . A 130 ARG HB2 . 19230 1 562 . 2 2 39 39 ARG HB3 H 1 1.553 0.020 . 2 . . . A 130 ARG HB3 . 19230 1 563 . 2 2 39 39 ARG HD2 H 1 3.071 0.020 . 2 . . . A 130 ARG HD2 . 19230 1 564 . 2 2 39 39 ARG HD3 H 1 3.071 0.020 . 2 . . . A 130 ARG HD3 . 19230 1 565 . 2 2 39 39 ARG CA C 13 53.449 0.300 . 1 . . . A 130 ARG CA . 19230 1 566 . 2 2 39 39 ARG CB C 13 28.500 0.300 . 1 . . . A 130 ARG CB . 19230 1 567 . 2 2 39 39 ARG N N 15 116.701 0.300 . 1 . . . A 130 ARG N . 19230 1 568 . 2 2 40 40 LEU H H 1 7.109 0.020 . 1 . . . A 131 LEU H . 19230 1 569 . 2 2 40 40 LEU HA H 1 4.063 0.020 . 1 . . . A 131 LEU HA . 19230 1 570 . 2 2 40 40 LEU HB2 H 1 1.801 0.020 . 2 . . . A 131 LEU HB2 . 19230 1 571 . 2 2 40 40 LEU HB3 H 1 1.801 0.020 . 2 . . . A 131 LEU HB3 . 19230 1 572 . 2 2 40 40 LEU HG H 1 1.584 0.020 . 1 . . . A 131 LEU HG . 19230 1 573 . 2 2 40 40 LEU CA C 13 52.053 0.300 . 1 . . . A 131 LEU CA . 19230 1 574 . 2 2 40 40 LEU CB C 13 35.280 0.300 . 1 . . . A 131 LEU CB . 19230 1 575 . 2 2 40 40 LEU N N 15 112.985 0.300 . 1 . . . A 131 LEU N . 19230 1 576 . 2 2 41 41 TYR H H 1 7.440 0.020 . 1 . . . A 132 TYR H . 19230 1 577 . 2 2 41 41 TYR HA H 1 4.326 0.020 . 1 . . . A 132 TYR HA . 19230 1 578 . 2 2 41 41 TYR HB2 H 1 3.180 0.020 . 2 . . . A 132 TYR HB2 . 19230 1 579 . 2 2 41 41 TYR HB3 H 1 3.180 0.020 . 2 . . . A 132 TYR HB3 . 19230 1 580 . 2 2 41 41 TYR CA C 13 55.947 0.300 . 1 . . . A 132 TYR CA . 19230 1 581 . 2 2 41 41 TYR CB C 13 38.550 0.300 . 1 . . . A 132 TYR CB . 19230 1 582 . 2 2 41 41 TYR N N 15 119.303 0.300 . 1 . . . A 132 TYR N . 19230 1 583 . 2 2 42 42 ASP H H 1 8.469 0.020 . 1 . . . A 133 ASP H . 19230 1 584 . 2 2 42 42 ASP HA H 1 4.590 0.020 . 1 . . . A 133 ASP HA . 19230 1 585 . 2 2 42 42 ASP HB2 H 1 1.971 0.020 . 2 . . . A 133 ASP HB2 . 19230 1 586 . 2 2 42 42 ASP HB3 H 1 1.971 0.020 . 2 . . . A 133 ASP HB3 . 19230 1 587 . 2 2 42 42 ASP CA C 13 50.380 0.300 . 1 . . . A 133 ASP CA . 19230 1 588 . 2 2 42 42 ASP CB C 13 36.536 0.300 . 1 . . . A 133 ASP CB . 19230 1 589 . 2 2 42 42 ASP N N 15 122.526 0.300 . 1 . . . A 133 ASP N . 19230 1 590 . 2 2 43 43 GLU H H 1 8.503 0.020 . 1 . . . A 134 GLU H . 19230 1 591 . 2 2 43 43 GLU HA H 1 4.140 0.020 . 1 . . . A 134 GLU HA . 19230 1 592 . 2 2 43 43 GLU HB2 H 1 1.692 0.020 . 2 . . . A 134 GLU HB2 . 19230 1 593 . 2 2 43 43 GLU HB3 H 1 1.692 0.020 . 2 . . . A 134 GLU HB3 . 19230 1 594 . 2 2 43 43 GLU CA C 13 55.518 0.300 . 1 . . . A 134 GLU CA . 19230 1 595 . 2 2 43 43 GLU CB C 13 28.836 0.300 . 1 . . . A 134 GLU CB . 19230 1 596 . 2 2 43 43 GLU N N 15 123.302 0.300 . 1 . . . A 134 GLU N . 19230 1 597 . 2 2 44 44 LYS H H 1 8.569 0.020 . 1 . . . A 135 LYS H . 19230 1 598 . 2 2 44 44 LYS HA H 1 4.388 0.020 . 1 . . . A 135 LYS HA . 19230 1 599 . 2 2 44 44 LYS HB2 H 1 1.906 0.020 . 2 . . . A 135 LYS HB2 . 19230 1 600 . 2 2 44 44 LYS HB3 H 1 1.940 0.020 . 2 . . . A 135 LYS HB3 . 19230 1 601 . 2 2 44 44 LYS HG2 H 1 1.259 0.020 . 2 . . . A 135 LYS HG2 . 19230 1 602 . 2 2 44 44 LYS HG3 H 1 1.259 0.020 . 2 . . . A 135 LYS HG3 . 19230 1 603 . 2 2 44 44 LYS CA C 13 56.640 0.300 . 1 . . . A 135 LYS CA . 19230 1 604 . 2 2 44 44 LYS CB C 13 33.687 0.300 . 1 . . . A 135 LYS CB . 19230 1 605 . 2 2 44 44 LYS N N 15 118.040 0.300 . 1 . . . A 135 LYS N . 19230 1 606 . 2 2 45 45 GLN H H 1 8.112 0.020 . 1 . . . A 136 GLN H . 19230 1 607 . 2 2 45 45 GLN HB2 H 1 1.850 0.020 . 2 . . . A 136 GLN HB2 . 19230 1 608 . 2 2 45 45 GLN HB3 H 1 1.569 0.020 . 2 . . . A 136 GLN HB3 . 19230 1 609 . 2 2 45 45 GLN HG2 H 1 1.925 0.020 . 2 . . . A 136 GLN HG2 . 19230 1 610 . 2 2 45 45 GLN HG3 H 1 1.925 0.020 . 2 . . . A 136 GLN HG3 . 19230 1 611 . 2 2 45 45 GLN CA C 13 54.000 0.300 . 1 . . . A 136 GLN CA . 19230 1 612 . 2 2 45 45 GLN CB C 13 28.346 0.300 . 1 . . . A 136 GLN CB . 19230 1 613 . 2 2 45 45 GLN N N 15 119.441 0.300 . 1 . . . A 136 GLN N . 19230 1 614 . 2 2 46 46 GLN H H 1 7.899 0.020 . 1 . . . A 137 GLN H . 19230 1 615 . 2 2 46 46 GLN HA H 1 3.923 0.020 . 1 . . . A 137 GLN HA . 19230 1 616 . 2 2 46 46 GLN HB2 H 1 2.002 0.020 . 2 . . . A 137 GLN HB2 . 19230 1 617 . 2 2 46 46 GLN HB3 H 1 2.002 0.020 . 2 . . . A 137 GLN HB3 . 19230 1 618 . 2 2 46 46 GLN CA C 13 54.538 0.300 . 1 . . . A 137 GLN CA . 19230 1 619 . 2 2 46 46 GLN CB C 13 27.758 0.300 . 1 . . . A 137 GLN CB . 19230 1 620 . 2 2 46 46 GLN N N 15 119.085 0.300 . 1 . . . A 137 GLN N . 19230 1 621 . 2 2 47 47 HIS H H 1 8.086 0.020 . 1 . . . A 138 HIS H . 19230 1 622 . 2 2 47 47 HIS HA H 1 3.985 0.020 . 1 . . . A 138 HIS HA . 19230 1 623 . 2 2 47 47 HIS HB2 H 1 2.777 0.020 . 2 . . . A 138 HIS HB2 . 19230 1 624 . 2 2 47 47 HIS HB3 H 1 2.777 0.020 . 2 . . . A 138 HIS HB3 . 19230 1 625 . 2 2 47 47 HIS CA C 13 54.627 0.300 . 1 . . . A 138 HIS CA . 19230 1 626 . 2 2 47 47 HIS CB C 13 26.027 0.300 . 1 . . . A 138 HIS CB . 19230 1 627 . 2 2 47 47 HIS N N 15 118.458 0.300 . 1 . . . A 138 HIS N . 19230 1 628 . 2 2 48 48 ILE H H 1 7.849 0.020 . 1 . . . A 139 ILE H . 19230 1 629 . 2 2 48 48 ILE HA H 1 4.249 0.020 . 1 . . . A 139 ILE HA . 19230 1 630 . 2 2 48 48 ILE HB H 1 1.940 0.020 . 1 . . . A 139 ILE HB . 19230 1 631 . 2 2 48 48 ILE HG12 H 1 0.871 0.020 . 2 . . . A 139 ILE HG12 . 19230 1 632 . 2 2 48 48 ILE HG13 H 1 0.871 0.020 . 2 . . . A 139 ILE HG13 . 19230 1 633 . 2 2 48 48 ILE CA C 13 53.274 0.300 . 1 . . . A 139 ILE CA . 19230 1 634 . 2 2 48 48 ILE CB C 13 36.382 0.300 . 1 . . . A 139 ILE CB . 19230 1 635 . 2 2 48 48 ILE N N 15 118.051 0.300 . 1 . . . A 139 ILE N . 19230 1 636 . 2 2 49 49 VAL H H 1 8.814 0.020 . 1 . . . A 140 VAL H . 19230 1 637 . 2 2 49 49 VAL HA H 1 4.171 0.020 . 1 . . . A 140 VAL HA . 19230 1 638 . 2 2 49 49 VAL HB H 1 1.925 0.020 . 1 . . . A 140 VAL HB . 19230 1 639 . 2 2 49 49 VAL HG11 H 1 0.856 0.020 . 2 . . . A 140 VAL HG11 . 19230 1 640 . 2 2 49 49 VAL HG12 H 1 0.856 0.020 . 2 . . . A 140 VAL HG12 . 19230 1 641 . 2 2 49 49 VAL HG13 H 1 0.856 0.020 . 2 . . . A 140 VAL HG13 . 19230 1 642 . 2 2 49 49 VAL CA C 13 59.438 0.300 . 1 . . . A 140 VAL CA . 19230 1 643 . 2 2 49 49 VAL CB C 13 32.507 0.300 . 1 . . . A 140 VAL CB . 19230 1 644 . 2 2 49 49 VAL N N 15 121.496 0.300 . 1 . . . A 140 VAL N . 19230 1 645 . 2 2 50 50 TYR H H 1 8.109 0.020 . 1 . . . A 141 TYR H . 19230 1 646 . 2 2 50 50 TYR HA H 1 4.249 0.020 . 1 . . . A 141 TYR HA . 19230 1 647 . 2 2 50 50 TYR HB2 H 1 2.730 0.020 . 2 . . . A 141 TYR HB2 . 19230 1 648 . 2 2 50 50 TYR HB3 H 1 2.730 0.020 . 2 . . . A 141 TYR HB3 . 19230 1 649 . 2 2 50 50 TYR CA C 13 59.247 0.300 . 1 . . . A 141 TYR CA . 19230 1 650 . 2 2 50 50 TYR CB C 13 39.462 0.300 . 1 . . . A 141 TYR CB . 19230 1 651 . 2 2 50 50 TYR N N 15 121.619 0.300 . 1 . . . A 141 TYR N . 19230 1 652 . 2 2 51 51 CYS H H 1 8.471 0.020 . 1 . . . A 142 CYS H . 19230 1 653 . 2 2 51 51 CYS CA C 13 55.976 0.300 . 1 . . . A 142 CYS CA . 19230 1 654 . 2 2 51 51 CYS CB C 13 29.482 0.300 . 1 . . . A 142 CYS CB . 19230 1 655 . 2 2 52 52 SER H H 1 7.658 0.020 . 1 . . . A 143 SER H . 19230 1 656 . 2 2 52 52 SER HA H 1 4.202 0.020 . 1 . . . A 143 SER HA . 19230 1 657 . 2 2 52 52 SER HB2 H 1 3.567 0.020 . 2 . . . A 143 SER HB2 . 19230 1 658 . 2 2 52 52 SER HB3 H 1 3.567 0.020 . 2 . . . A 143 SER HB3 . 19230 1 659 . 2 2 52 52 SER CA C 13 57.145 0.300 . 1 . . . A 143 SER CA . 19230 1 660 . 2 2 52 52 SER CB C 13 60.049 0.300 . 1 . . . A 143 SER CB . 19230 1 661 . 2 2 52 52 SER N N 15 116.148 0.300 . 1 . . . A 143 SER N . 19230 1 662 . 2 2 53 53 ASN H H 1 8.657 0.020 . 1 . . . A 144 ASN H . 19230 1 663 . 2 2 53 53 ASN HA H 1 4.404 0.020 . 1 . . . A 144 ASN HA . 19230 1 664 . 2 2 53 53 ASN HB2 H 1 1.987 0.020 . 2 . . . A 144 ASN HB2 . 19230 1 665 . 2 2 53 53 ASN HB3 H 1 1.987 0.020 . 2 . . . A 144 ASN HB3 . 19230 1 666 . 2 2 53 53 ASN CA C 13 55.528 0.300 . 1 . . . A 144 ASN CA . 19230 1 667 . 2 2 53 53 ASN CB C 13 38.538 0.300 . 1 . . . A 144 ASN CB . 19230 1 668 . 2 2 53 53 ASN N N 15 118.343 0.300 . 1 . . . A 144 ASN N . 19230 1 669 . 2 2 54 54 ASP H H 1 8.237 0.020 . 1 . . . A 145 ASP H . 19230 1 670 . 2 2 54 54 ASP CA C 13 52.690 0.300 . 1 . . . A 145 ASP CA . 19230 1 671 . 2 2 54 54 ASP CB C 13 39.616 0.300 . 1 . . . A 145 ASP CB . 19230 1 672 . 2 2 54 54 ASP N N 15 121.163 0.300 . 1 . . . A 145 ASP N . 19230 1 673 . 2 2 56 56 LEU H H 1 9.756 0.020 . 1 . . . A 147 LEU H . 19230 1 674 . 2 2 56 56 LEU HA H 1 4.388 0.020 . 1 . . . A 147 LEU HA . 19230 1 675 . 2 2 56 56 LEU HB2 H 1 1.522 0.020 . 2 . . . A 147 LEU HB2 . 19230 1 676 . 2 2 56 56 LEU HB3 H 1 1.522 0.020 . 2 . . . A 147 LEU HB3 . 19230 1 677 . 2 2 56 56 LEU HG H 1 1.119 0.020 . 1 . . . A 147 LEU HG . 19230 1 678 . 2 2 56 56 LEU HD11 H 1 0.515 0.020 . 2 . . . A 147 LEU HD11 . 19230 1 679 . 2 2 56 56 LEU HD12 H 1 0.515 0.020 . 2 . . . A 147 LEU HD12 . 19230 1 680 . 2 2 56 56 LEU HD13 H 1 0.515 0.020 . 2 . . . A 147 LEU HD13 . 19230 1 681 . 2 2 56 56 LEU HD21 H 1 0.515 0.020 . 2 . . . A 147 LEU HD21 . 19230 1 682 . 2 2 56 56 LEU HD22 H 1 0.515 0.020 . 2 . . . A 147 LEU HD22 . 19230 1 683 . 2 2 56 56 LEU HD23 H 1 0.515 0.020 . 2 . . . A 147 LEU HD23 . 19230 1 684 . 2 2 56 56 LEU CA C 13 55.155 0.300 . 1 . . . A 147 LEU CA . 19230 1 685 . 2 2 56 56 LEU CB C 13 40.107 0.300 . 1 . . . A 147 LEU CB . 19230 1 686 . 2 2 56 56 LEU N N 15 118.492 0.300 . 1 . . . A 147 LEU N . 19230 1 687 . 2 2 57 57 GLY H H 1 7.687 0.020 . 1 . . . A 148 GLY H . 19230 1 688 . 2 2 57 57 GLY HA2 H 1 4.156 0.020 . 2 . . . A 148 GLY HA2 . 19230 1 689 . 2 2 57 57 GLY HA3 H 1 3.614 0.020 . 2 . . . A 148 GLY HA3 . 19230 1 690 . 2 2 57 57 GLY CA C 13 44.991 0.300 . 1 . . . A 148 GLY CA . 19230 1 691 . 2 2 57 57 GLY N N 15 106.609 0.300 . 1 . . . A 148 GLY N . 19230 1 692 . 2 2 58 58 ASP H H 1 7.388 0.020 . 1 . . . A 149 ASP H . 19230 1 693 . 2 2 58 58 ASP HA H 1 4.249 0.020 . 1 . . . A 149 ASP HA . 19230 1 694 . 2 2 58 58 ASP HB2 H 1 2.905 0.020 . 2 . . . A 149 ASP HB2 . 19230 1 695 . 2 2 58 58 ASP HB3 H 1 2.576 0.020 . 2 . . . A 149 ASP HB3 . 19230 1 696 . 2 2 58 58 ASP CA C 13 53.868 0.300 . 1 . . . A 149 ASP CA . 19230 1 697 . 2 2 58 58 ASP CB C 13 37.539 0.300 . 1 . . . A 149 ASP CB . 19230 1 698 . 2 2 58 58 ASP N N 15 122.846 0.300 . 1 . . . A 149 ASP N . 19230 1 699 . 2 2 59 59 LEU H H 1 8.285 0.020 . 1 . . . A 150 LEU H . 19230 1 700 . 2 2 59 59 LEU HA H 1 4.311 0.020 . 1 . . . A 150 LEU HA . 19230 1 701 . 2 2 59 59 LEU HB2 H 1 2.018 0.020 . 2 . . . A 150 LEU HB2 . 19230 1 702 . 2 2 59 59 LEU HB3 H 1 2.018 0.020 . 2 . . . A 150 LEU HB3 . 19230 1 703 . 2 2 59 59 LEU CA C 13 55.528 0.300 . 1 . . . A 150 LEU CA . 19230 1 704 . 2 2 59 59 LEU CB C 13 36.767 0.300 . 1 . . . A 150 LEU CB . 19230 1 705 . 2 2 59 59 LEU N N 15 116.803 0.300 . 1 . . . A 150 LEU N . 19230 1 706 . 2 2 60 60 PHE H H 1 8.644 0.020 . 1 . . . A 151 PHE H . 19230 1 707 . 2 2 60 60 PHE HA H 1 4.419 0.020 . 1 . . . A 151 PHE HA . 19230 1 708 . 2 2 60 60 PHE HB2 H 1 2.622 0.020 . 2 . . . A 151 PHE HB2 . 19230 1 709 . 2 2 60 60 PHE HB3 H 1 2.622 0.020 . 2 . . . A 151 PHE HB3 . 19230 1 710 . 2 2 60 60 PHE CA C 13 52.845 0.300 . 1 . . . A 151 PHE CA . 19230 1 711 . 2 2 60 60 PHE CB C 13 35.386 0.300 . 1 . . . A 151 PHE CB . 19230 1 712 . 2 2 60 60 PHE N N 15 117.800 0.300 . 1 . . . A 151 PHE N . 19230 1 713 . 2 2 61 61 GLY H H 1 8.160 0.020 . 1 . . . A 152 GLY H . 19230 1 714 . 2 2 61 61 GLY HA2 H 1 4.311 0.020 . 2 . . . A 152 GLY HA2 . 19230 1 715 . 2 2 61 61 GLY HA3 H 1 3.846 0.020 . 2 . . . A 152 GLY HA3 . 19230 1 716 . 2 2 61 61 GLY CA C 13 43.605 0.300 . 1 . . . A 152 GLY CA . 19230 1 717 . 2 2 61 61 GLY N N 15 108.161 0.300 . 1 . . . A 152 GLY N . 19230 1 718 . 2 2 62 62 VAL H H 1 6.981 0.020 . 1 . . . A 153 VAL H . 19230 1 719 . 2 2 62 62 VAL HA H 1 3.861 0.020 . 1 . . . A 153 VAL HA . 19230 1 720 . 2 2 62 62 VAL HB H 1 1.940 0.020 . 1 . . . A 153 VAL HB . 19230 1 721 . 2 2 62 62 VAL HG11 H 1 0.670 0.020 . 2 . . . A 153 VAL HG11 . 19230 1 722 . 2 2 62 62 VAL HG12 H 1 0.670 0.020 . 2 . . . A 153 VAL HG12 . 19230 1 723 . 2 2 62 62 VAL HG13 H 1 0.670 0.020 . 2 . . . A 153 VAL HG13 . 19230 1 724 . 2 2 62 62 VAL HG21 H 1 0.670 0.020 . 2 . . . A 153 VAL HG21 . 19230 1 725 . 2 2 62 62 VAL HG22 H 1 0.670 0.020 . 2 . . . A 153 VAL HG22 . 19230 1 726 . 2 2 62 62 VAL HG23 H 1 0.670 0.020 . 2 . . . A 153 VAL HG23 . 19230 1 727 . 2 2 62 62 VAL CA C 13 54.142 0.300 . 1 . . . A 153 VAL CA . 19230 1 728 . 2 2 62 62 VAL CB C 13 32.070 0.300 . 1 . . . A 153 VAL CB . 19230 1 729 . 2 2 62 62 VAL N N 15 108.166 0.300 . 1 . . . A 153 VAL N . 19230 1 730 . 2 2 63 63 PRO CA C 13 63.330 0.300 . 1 . . . A 154 PRO CA . 19230 1 731 . 2 2 63 63 PRO CB C 13 32.114 0.300 . 1 . . . A 154 PRO CB . 19230 1 732 . 2 2 64 64 SER H H 1 7.205 0.020 . 1 . . . A 155 SER H . 19230 1 733 . 2 2 64 64 SER HA H 1 4.450 0.020 . 1 . . . A 155 SER HA . 19230 1 734 . 2 2 64 64 SER HB2 H 1 3.846 0.020 . 2 . . . A 155 SER HB2 . 19230 1 735 . 2 2 64 64 SER HB3 H 1 3.846 0.020 . 2 . . . A 155 SER HB3 . 19230 1 736 . 2 2 64 64 SER CA C 13 54.043 0.300 . 1 . . . A 155 SER CA . 19230 1 737 . 2 2 64 64 SER CB C 13 62.139 0.300 . 1 . . . A 155 SER CB . 19230 1 738 . 2 2 64 64 SER N N 15 111.507 0.300 . 1 . . . A 155 SER N . 19230 1 739 . 2 2 65 65 PHE H H 1 8.295 0.020 . 1 . . . A 156 PHE H . 19230 1 740 . 2 2 65 65 PHE HA H 1 4.109 0.020 . 1 . . . A 156 PHE HA . 19230 1 741 . 2 2 65 65 PHE HB2 H 1 2.281 0.020 . 2 . . . A 156 PHE HB2 . 19230 1 742 . 2 2 65 65 PHE HB3 H 1 2.281 0.020 . 2 . . . A 156 PHE HB3 . 19230 1 743 . 2 2 65 65 PHE CA C 13 53.736 0.300 . 1 . . . A 156 PHE CA . 19230 1 744 . 2 2 65 65 PHE CB C 13 37.208 0.300 . 1 . . . A 156 PHE CB . 19230 1 745 . 2 2 65 65 PHE N N 15 114.289 0.300 . 1 . . . A 156 PHE N . 19230 1 746 . 2 2 66 66 SER H H 1 8.632 0.020 . 1 . . . A 157 SER H . 19230 1 747 . 2 2 66 66 SER HA H 1 3.923 0.020 . 1 . . . A 157 SER HA . 19230 1 748 . 2 2 66 66 SER HB2 H 1 3.567 0.020 . 2 . . . A 157 SER HB2 . 19230 1 749 . 2 2 66 66 SER HB3 H 1 3.567 0.020 . 2 . . . A 157 SER HB3 . 19230 1 750 . 2 2 66 66 SER CA C 13 51.558 0.300 . 1 . . . A 157 SER CA . 19230 1 751 . 2 2 66 66 SER CB C 13 60.831 0.300 . 1 . . . A 157 SER CB . 19230 1 752 . 2 2 66 66 SER N N 15 111.907 0.300 . 1 . . . A 157 SER N . 19230 1 753 . 2 2 67 67 VAL H H 1 10.282 0.020 . 1 . . . A 158 VAL H . 19230 1 754 . 2 2 67 67 VAL HA H 1 3.970 0.020 . 1 . . . A 158 VAL HA . 19230 1 755 . 2 2 67 67 VAL HB H 1 1.770 0.020 . 1 . . . A 158 VAL HB . 19230 1 756 . 2 2 67 67 VAL HG11 H 1 0.654 0.020 . 2 . . . A 158 VAL HG11 . 19230 1 757 . 2 2 67 67 VAL HG12 H 1 0.654 0.020 . 2 . . . A 158 VAL HG12 . 19230 1 758 . 2 2 67 67 VAL HG13 H 1 0.654 0.020 . 2 . . . A 158 VAL HG13 . 19230 1 759 . 2 2 67 67 VAL HG21 H 1 0.654 0.020 . 2 . . . A 158 VAL HG21 . 19230 1 760 . 2 2 67 67 VAL HG22 H 1 0.654 0.020 . 2 . . . A 158 VAL HG22 . 19230 1 761 . 2 2 67 67 VAL HG23 H 1 0.654 0.020 . 2 . . . A 158 VAL HG23 . 19230 1 762 . 2 2 67 67 VAL CA C 13 60.922 0.300 . 1 . . . A 158 VAL CA . 19230 1 763 . 2 2 67 67 VAL CB C 13 29.340 0.300 . 1 . . . A 158 VAL CB . 19230 1 764 . 2 2 67 67 VAL N N 15 127.097 0.300 . 1 . . . A 158 VAL N . 19230 1 765 . 2 2 68 68 LYS H H 1 7.774 0.020 . 1 . . . A 159 LYS H . 19230 1 766 . 2 2 68 68 LYS HA H 1 4.094 0.020 . 1 . . . A 159 LYS HA . 19230 1 767 . 2 2 68 68 LYS HB2 H 1 1.863 0.020 . 2 . . . A 159 LYS HB2 . 19230 1 768 . 2 2 68 68 LYS HB3 H 1 1.863 0.020 . 2 . . . A 159 LYS HB3 . 19230 1 769 . 2 2 68 68 LYS HG2 H 1 1.321 0.020 . 2 . . . A 159 LYS HG2 . 19230 1 770 . 2 2 68 68 LYS HG3 H 1 1.321 0.020 . 2 . . . A 159 LYS HG3 . 19230 1 771 . 2 2 68 68 LYS CA C 13 55.683 0.300 . 1 . . . A 159 LYS CA . 19230 1 772 . 2 2 68 68 LYS CB C 13 29.837 0.300 . 1 . . . A 159 LYS CB . 19230 1 773 . 2 2 68 68 LYS N N 15 114.757 0.300 . 1 . . . A 159 LYS N . 19230 1 774 . 2 2 69 69 GLU H H 1 7.441 0.020 . 1 . . . A 160 GLU H . 19230 1 775 . 2 2 69 69 GLU HA H 1 4.264 0.020 . 1 . . . A 160 GLU HA . 19230 1 776 . 2 2 69 69 GLU HB2 H 1 1.925 0.020 . 2 . . . A 160 GLU HB2 . 19230 1 777 . 2 2 69 69 GLU HB3 H 1 1.925 0.020 . 2 . . . A 160 GLU HB3 . 19230 1 778 . 2 2 69 69 GLU CA C 13 55.990 0.300 . 1 . . . A 160 GLU CA . 19230 1 779 . 2 2 69 69 GLU CB C 13 28.220 0.300 . 1 . . . A 160 GLU CB . 19230 1 780 . 2 2 69 69 GLU N N 15 119.592 0.300 . 1 . . . A 160 GLU N . 19230 1 781 . 2 2 70 70 HIS H H 1 7.664 0.020 . 1 . . . A 161 HIS H . 19230 1 782 . 2 2 70 70 HIS HA H 1 4.574 0.020 . 1 . . . A 161 HIS HA . 19230 1 783 . 2 2 70 70 HIS HB2 H 1 2.963 0.020 . 2 . . . A 161 HIS HB2 . 19230 1 784 . 2 2 70 70 HIS HB3 H 1 2.963 0.020 . 2 . . . A 161 HIS HB3 . 19230 1 785 . 2 2 70 70 HIS CA C 13 56.937 0.300 . 1 . . . A 161 HIS CA . 19230 1 786 . 2 2 70 70 HIS CB C 13 29.529 0.300 . 1 . . . A 161 HIS CB . 19230 1 787 . 2 2 70 70 HIS N N 15 119.985 0.300 . 1 . . . A 161 HIS N . 19230 1 788 . 2 2 72 72 LYS H H 1 7.812 0.020 . 1 . . . A 163 LYS H . 19230 1 789 . 2 2 72 72 LYS HA H 1 4.001 0.020 . 1 . . . A 163 LYS HA . 19230 1 790 . 2 2 72 72 LYS HB2 H 1 1.739 0.020 . 2 . . . A 163 LYS HB2 . 19230 1 791 . 2 2 72 72 LYS HB3 H 1 1.739 0.020 . 2 . . . A 163 LYS HB3 . 19230 1 792 . 2 2 72 72 LYS HG2 H 1 1.429 0.020 . 2 . . . A 163 LYS HG2 . 19230 1 793 . 2 2 72 72 LYS HG3 H 1 1.429 0.020 . 2 . . . A 163 LYS HG3 . 19230 1 794 . 2 2 72 72 LYS HE2 H 1 2.786 0.020 . 2 . . . A 163 LYS HE2 . 19230 1 795 . 2 2 72 72 LYS HE3 H 1 2.529 0.020 . 2 . . . A 163 LYS HE3 . 19230 1 796 . 2 2 72 72 LYS CA C 13 56.706 0.300 . 1 . . . A 163 LYS CA . 19230 1 797 . 2 2 72 72 LYS CB C 13 29.452 0.300 . 1 . . . A 163 LYS CB . 19230 1 798 . 2 2 72 72 LYS N N 15 119.699 0.300 . 1 . . . A 163 LYS N . 19230 1 799 . 2 2 73 73 ILE H H 1 7.624 0.020 . 1 . . . A 164 ILE H . 19230 1 800 . 2 2 73 73 ILE HA H 1 4.249 0.020 . 1 . . . A 164 ILE HA . 19230 1 801 . 2 2 73 73 ILE HB H 1 1.770 0.020 . 1 . . . A 164 ILE HB . 19230 1 802 . 2 2 73 73 ILE HG12 H 1 1.383 0.020 . 2 . . . A 164 ILE HG12 . 19230 1 803 . 2 2 73 73 ILE HG13 H 1 1.383 0.020 . 2 . . . A 164 ILE HG13 . 19230 1 804 . 2 2 73 73 ILE CA C 13 61.723 0.300 . 1 . . . A 164 ILE CA . 19230 1 805 . 2 2 73 73 ILE CB C 13 33.687 0.300 . 1 . . . A 164 ILE CB . 19230 1 806 . 2 2 73 73 ILE N N 15 118.636 0.300 . 1 . . . A 164 ILE N . 19230 1 807 . 2 2 74 74 TYR H H 1 8.085 0.020 . 1 . . . A 165 TYR H . 19230 1 808 . 2 2 74 74 TYR HA H 1 4.249 0.020 . 1 . . . A 165 TYR HA . 19230 1 809 . 2 2 74 74 TYR HB2 H 1 2.777 0.020 . 2 . . . A 165 TYR HB2 . 19230 1 810 . 2 2 74 74 TYR HB3 H 1 2.777 0.020 . 2 . . . A 165 TYR HB3 . 19230 1 811 . 2 2 74 74 TYR CA C 13 60.468 0.300 . 1 . . . A 165 TYR CA . 19230 1 812 . 2 2 74 74 TYR CB C 13 34.303 0.300 . 1 . . . A 165 TYR CB . 19230 1 813 . 2 2 74 74 TYR N N 15 118.212 0.300 . 1 . . . A 165 TYR N . 19230 1 814 . 2 2 75 75 THR H H 1 8.057 0.020 . 1 . . . A 166 THR H . 19230 1 815 . 2 2 75 75 THR HA H 1 4.295 0.020 . 1 . . . A 166 THR HA . 19230 1 816 . 2 2 75 75 THR HB H 1 3.737 0.020 . 1 . . . A 166 THR HB . 19230 1 817 . 2 2 75 75 THR HG21 H 1 1.119 0.020 . 1 . . . A 166 THR HG2 . 19230 1 818 . 2 2 75 75 THR HG22 H 1 1.119 0.020 . 1 . . . A 166 THR HG2 . 19230 1 819 . 2 2 75 75 THR HG23 H 1 1.119 0.020 . 1 . . . A 166 THR HG2 . 19230 1 820 . 2 2 75 75 THR CA C 13 64.627 0.300 . 1 . . . A 166 THR CA . 19230 1 821 . 2 2 75 75 THR CB C 13 65.425 0.300 . 1 . . . A 166 THR CB . 19230 1 822 . 2 2 75 75 THR N N 15 114.656 0.300 . 1 . . . A 166 THR N . 19230 1 823 . 2 2 76 76 MET H H 1 7.508 0.020 . 1 . . . A 167 MET H . 19230 1 824 . 2 2 76 76 MET HA H 1 4.187 0.020 . 1 . . . A 167 MET HA . 19230 1 825 . 2 2 76 76 MET HB2 H 1 1.754 0.020 . 2 . . . A 167 MET HB2 . 19230 1 826 . 2 2 76 76 MET HB3 H 1 1.754 0.020 . 2 . . . A 167 MET HB3 . 19230 1 827 . 2 2 76 76 MET CA C 13 56.937 0.300 . 1 . . . A 167 MET CA . 19230 1 828 . 2 2 76 76 MET CB C 13 30.453 0.300 . 1 . . . A 167 MET CB . 19230 1 829 . 2 2 76 76 MET N N 15 119.968 0.300 . 1 . . . A 167 MET N . 19230 1 830 . 2 2 77 77 ILE H H 1 7.907 0.020 . 1 . . . A 168 ILE H . 19230 1 831 . 2 2 77 77 ILE CA C 13 63.934 0.300 . 1 . . . A 168 ILE CA . 19230 1 832 . 2 2 77 77 ILE CB C 13 39.154 0.300 . 1 . . . A 168 ILE CB . 19230 1 833 . 2 2 77 77 ILE N N 15 119.044 0.300 . 1 . . . A 168 ILE N . 19230 1 834 . 2 2 78 78 TYR H H 1 8.765 0.020 . 1 . . . A 169 TYR H . 19230 1 835 . 2 2 78 78 TYR HA H 1 4.744 0.020 . 1 . . . A 169 TYR HA . 19230 1 836 . 2 2 78 78 TYR HB2 H 1 2.374 0.020 . 2 . . . A 169 TYR HB2 . 19230 1 837 . 2 2 78 78 TYR HB3 H 1 2.374 0.020 . 2 . . . A 169 TYR HB3 . 19230 1 838 . 2 2 78 78 TYR CA C 13 59.214 0.300 . 1 . . . A 169 TYR CA . 19230 1 839 . 2 2 78 78 TYR CB C 13 34.611 0.300 . 1 . . . A 169 TYR CB . 19230 1 840 . 2 2 78 78 TYR N N 15 118.499 0.300 . 1 . . . A 169 TYR N . 19230 1 841 . 2 2 79 79 ARG H H 1 7.237 0.020 . 1 . . . A 170 ARG H . 19230 1 842 . 2 2 79 79 ARG HA H 1 4.218 0.020 . 1 . . . A 170 ARG HA . 19230 1 843 . 2 2 79 79 ARG HB2 H 1 1.599 0.020 . 2 . . . A 170 ARG HB2 . 19230 1 844 . 2 2 79 79 ARG HB3 H 1 1.599 0.020 . 2 . . . A 170 ARG HB3 . 19230 1 845 . 2 2 79 79 ARG HG2 H 1 1.104 0.020 . 2 . . . A 170 ARG HG2 . 19230 1 846 . 2 2 79 79 ARG HG3 H 1 1.104 0.020 . 2 . . . A 170 ARG HG3 . 19230 1 847 . 2 2 79 79 ARG CA C 13 55.617 0.300 . 1 . . . A 170 ARG CA . 19230 1 848 . 2 2 79 79 ARG CB C 13 27.681 0.300 . 1 . . . A 170 ARG CB . 19230 1 849 . 2 2 79 79 ARG N N 15 115.858 0.300 . 1 . . . A 170 ARG N . 19230 1 stop_ save_