data_18509 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18509 _Entry.Title ; Structure and chemical shifts of Cu(I),Zn(II) superoxide dismutase by solid-state NMR ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-06-08 _Entry.Accession_date 2012-06-08 _Entry.Last_release_date 2012-08-29 _Entry.Original_release_date 2012-08-29 _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 SOLID-STATE _Entry.Details 'Solid-state NMR structure using paramagnetic restraints' _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 Michael Knight . J. . 18509 2 Andrew Pell . J. . 18509 3 Ivano Bertini . . . 18509 4 Isabella Felli . C. . 18509 5 Leonardo Gonnelli . . . 18509 6 Roberta Pierattelli . . . 18509 7 Torsten Herrmann . . . 18509 8 Lyndon Emsley . . . 18509 9 Guido Pintacuda . . . 18509 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' . 18509 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID Metalloprotein . 18509 Microcrystalline . 18509 Paramagnetic . 18509 Protein . 18509 'Solid-state NMR' . 18509 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18509 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 245 18509 '15N chemical shifts' 136 18509 '1H chemical shifts' 136 18509 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2012-08-29 2012-06-08 original author . 18509 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2LU5 'BMRB Entry Tracking System' 18509 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18509 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22723345 _Citation.Full_citation . _Citation.Title 'Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.' _Citation.Journal_name_full . _Citation.Journal_volume 109 _Citation.Journal_issue 28 _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 11095 _Citation.Page_last 11100 _Citation.Year 2012 _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 Michael Knight . J. . 18509 1 2 Andrew Pell . J. . 18509 1 3 Ivano Bertini . . . 18509 1 4 Isabella Felli . C. . 18509 1 5 Leonardo Gonnelli . . . 18509 1 6 Roberta Pierattelli . . . 18509 1 7 Torsten Herrmann . . . 18509 1 8 Lyndon Emsley . . . 18509 1 9 Guido Pintacuda . . . 18509 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18509 _Assembly.ID 1 _Assembly.Name 'Cu(I),Zn(II) superoxide dismutase' _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 Superoxide_dismutase_C6A/C111S_thermostable_mutant 1 $Superoxide_dismutase_C6A-C111S_thermostable_mutant A . yes native no no . . . 18509 1 2 CU2 2 $CU B . yes native no no . . . 18509 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Superoxide_dismutase_C6A-C111S_thermostable_mutant _Entity.Sf_category entity _Entity.Sf_framecode Superoxide_dismutase_C6A-C111S_thermostable_mutant _Entity.Entry_ID 18509 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Superoxide_dismutase_C6A-C111S_thermostable_mutant _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 ; ATKAVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIE DSVISLSGDHSIIGRTLVVH EKADDLGKGGNEESTKTGNA GSRLACGVIGIAQ ; _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 153 _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 15779.566 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 15711 . SOD1 . . . . . 100.00 153 98.04 98.69 2.09e-100 . . . . 18509 1 2 no BMRB 15712 . SOD1 . . . . . 100.00 153 97.39 98.04 1.37e-99 . . . . 18509 1 3 no BMRB 15713 . SOD1 . . . . . 100.00 153 97.39 98.04 2.41e-99 . . . . 18509 1 4 no BMRB 15714 . SOD1 . . . . . 100.00 153 97.39 98.04 2.49e-99 . . . . 18509 1 5 no BMRB 18708 . SUPEROXIDE_DISMUTASE_CU-ZN . . . . . 100.00 153 100.00 100.00 4.22e-103 . . . . 18509 1 6 no BMRB 18968 . SOD1 . . . . . 100.00 153 98.04 98.69 2.09e-100 . . . . 18509 1 7 no BMRB 19962 . L126Z-sod1 . . . . . 81.70 125 98.40 98.40 5.89e-81 . . . . 18509 1 8 no BMRB 26570 . SOD1 . . . . . 100.00 153 100.00 100.00 4.22e-103 . . . . 18509 1 9 no BMRB 4202 . "Superoxide Dismutase" . . . . . 100.00 153 98.04 98.69 2.46e-100 . . . . 18509 1 10 no PDB 1AZV . "Familial Als Mutant G37r Cuznsod (Human)" . . . . . 100.00 153 98.04 98.04 1.35e-100 . . . . 18509 1 11 no PDB 1BA9 . "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" . . . . . 99.35 153 98.03 98.68 1.14e-99 . . . . 18509 1 12 no PDB 1DSW . "The Solution Structure Of A Monomeric, Reduced Form Of Human Copper, Zinc Superoxide Dismutase Bearing The Same Charge As The N" . . . . . 99.35 153 97.37 97.37 5.19e-98 . . . . 18509 1 13 no PDB 1FUN . "Superoxide Dismutase Mutant With Lys 136 Replaced By Glu, Cys 6 Replaced By Ala And Cys 111 Replaced By Ser (K136e, C6a, C111s)" . . . . . 100.00 153 99.35 100.00 1.39e-102 . . . . 18509 1 14 no PDB 1HL4 . "The Structure Of Apo Type Human Cu, Zn Superoxide Dismutase" . . . . . 100.00 154 98.69 98.69 1.26e-101 . . . . 18509 1 15 no PDB 1HL5 . "The Structure Of Holo Type Human Cu, Zn Superoxide Dismutase" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18509 1 16 no PDB 1KMG . "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" . . . . . 100.00 153 98.04 98.69 2.46e-100 . . . . 18509 1 17 no PDB 1L3N . "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" . . . . . 100.00 153 100.00 100.00 4.22e-103 . . . . 18509 1 18 no PDB 1MFM . "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" . . . . . 100.00 153 98.04 98.69 2.46e-100 . . . . 18509 1 19 no PDB 1N18 . "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" . . . . . 100.00 154 100.00 100.00 3.36e-103 . . . . 18509 1 20 no PDB 1N19 . "Structure Of The Hsod A4v Mutant" . . . . . 100.00 154 99.35 99.35 1.40e-102 . . . . 18509 1 21 no PDB 1OEZ . "Zn His46arg Mutant Of Human Cu, Zn Superoxide Dismutase" . . . . . 100.00 153 98.04 98.04 1.11e-100 . . . . 18509 1 22 no PDB 1OZT . "Crystal Structure Of Apo-H46r Familial Als Mutant Human Cu, Zn Superoxide Dismutase (Cuznsod) To 2.5a Resolution" . . . . . 100.00 153 98.04 98.04 1.11e-100 . . . . 18509 1 23 no PDB 1OZU . "Crystal Structure Of Familial Als Mutant S134n Of Human Cu, Zn Superoxide Dismutase (Cuznsod) To 1.3a Resolution" . . . . . 100.00 153 98.04 98.69 4.29e-101 . . . . 18509 1 24 no PDB 1P1V . "Crystal Structure Of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125h To 1.4a" . . . . . 100.00 153 98.04 98.04 1.66e-100 . . . . 18509 1 25 no PDB 1PTZ . "Crystal Structure Of The Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43r" . . . . . 100.00 153 99.35 99.35 2.98e-102 . . . . 18509 1 26 no PDB 1PU0 . "Structure Of Human Cu,Zn Superoxide Dismutase" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18509 1 27 no PDB 1RK7 . "Solution Structure Of Apo Cu,Zn Superoxide Dismutase: Role Of Metal Ions In Protein Folding" . . . . . 100.00 153 98.04 98.69 2.46e-100 . . . . 18509 1 28 no PDB 1SOS . "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" . . . . . 100.00 154 100.00 100.00 4.36e-103 . . . . 18509 1 29 no PDB 1SPD . "Amyotrophic Lateral Sclerosis And Structural Defects In Cu,Zn Superoxide Dismutase" . . . . . 100.00 154 98.69 98.69 1.26e-101 . . . . 18509 1 30 no PDB 1UXL . "I113t Mutant Of Human Sod1" . . . . . 100.00 153 98.04 98.04 6.42e-101 . . . . 18509 1 31 no PDB 1UXM . "A4v Mutant Of Human Sod1" . . . . . 100.00 153 98.04 98.04 5.76e-101 . . . . 18509 1 32 no PDB 2AF2 . "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" . . . . . 100.00 153 100.00 100.00 4.22e-103 . . . . 18509 1 33 no PDB 2C9S . "1.24 Angstroms Resolution Structure Of Zn-Zn Human Superoxide Dismutase" . . . . . 100.00 153 98.69 98.69 1.17e-101 . . . . 18509 1 34 no PDB 2C9U . "1.24 Angstroms Resolution Structure Of As-Isolated Cu-Zn Human Superoxide Dismutase" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18509 1 35 no PDB 2C9V . "Atomic Resolution Structure Of Cu-Zn Human Superoxide Dismutase" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18509 1 36 no PDB 2GBT . "C6aC111A CUZN SUPEROXIDE DISMUTASE" . . . . . 100.00 153 99.35 100.00 9.89e-103 . . . . 18509 1 37 no PDB 2GBU . "C6a/c111a/c57a/c146a Apo Cuzn Superoxide Dismutase" . . . . . 100.00 153 98.04 98.69 1.21e-100 . . . . 18509 1 38 no PDB 2GBV . "C6aC111AC57AC146A HOLO CUZN SUPEROXIDE DISMUTASE" . . . . . 100.00 153 98.04 98.69 1.21e-100 . . . . 18509 1 39 no PDB 2LU5 . "Structure And Chemical Shifts Of Cu(I),Zn(Ii) Superoxide Dismutase By Solid-State Nmr" . . . . . 100.00 153 100.00 100.00 4.22e-103 . . . . 18509 1 40 no PDB 2MP3 . "Truncated L126z-sod1 In Dpc Micelle" . . . . . 81.70 132 98.40 98.40 1.75e-80 . . . . 18509 1 41 no PDB 2NNX . "Crystal Structure Of The H46r, H48q Double Mutant Of Human [cu-Zn] Superoxide Dismutase" . . . . . 100.00 154 97.39 97.39 6.95e-100 . . . . 18509 1 42 no PDB 2R27 . "Constitutively Zinc-Deficient Mutant Of Human Superoxide Dismutase (Sod), C6a, H80s, H83s, C111s" . . . . . 100.00 154 98.69 98.69 1.49e-101 . . . . 18509 1 43 no PDB 2V0A . "Atomic Resolution Crystal Structure Of Human Superoxide Dismutase" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18509 1 44 no PDB 2VR6 . "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.3 A Resolution" . . . . . 100.00 153 98.04 98.04 1.35e-100 . . . . 18509 1 45 no PDB 2VR7 . "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.58 A Resolution" . . . . . 100.00 154 98.04 98.04 1.40e-100 . . . . 18509 1 46 no PDB 2VR8 . "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.36 A Resolution" . . . . . 100.00 154 98.04 98.04 1.35e-100 . . . . 18509 1 47 no PDB 2WKO . "Structure Of Metal Loaded Pathogenic Sod1 Mutant G93a" . . . . . 100.00 154 98.04 98.04 4.89e-101 . . . . 18509 1 48 no PDB 2WYT . "1.0 A Resolution Structure Of L38v Sod1 Mutant" . . . . . 100.00 153 98.04 98.69 4.01e-101 . . . . 18509 1 49 no PDB 2WYZ . "L38v Sod1 Mutant Complexed With Ump" . . . . . 100.00 153 98.04 98.69 4.29e-101 . . . . 18509 1 50 no PDB 2WZ0 . "L38v Sod1 Mutant Complexed With Aniline." . . . . . 100.00 153 98.04 98.69 4.01e-101 . . . . 18509 1 51 no PDB 2WZ5 . "L38v Sod1 Mutant Complexed With L-Methionine" . . . . . 100.00 153 98.04 98.69 4.01e-101 . . . . 18509 1 52 no PDB 2WZ6 . "G93a Sod1 Mutant Complexed With Quinazoline" . . . . . 100.00 153 98.04 98.04 4.73e-101 . . . . 18509 1 53 no PDB 2XJK . "Monomeric Human Cu,Zn Superoxide Dismutase" . . . . . 100.00 153 98.04 98.69 2.09e-100 . . . . 18509 1 54 no PDB 2ZKW . "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group P21" . . . . . 100.00 159 98.04 98.04 1.27e-100 . . . . 18509 1 55 no PDB 2ZKX . "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group I212121" . . . . . 100.00 159 98.04 98.04 1.27e-100 . . . . 18509 1 56 no PDB 2ZKY . "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G93a" . . . . . 100.00 159 98.04 98.04 4.50e-101 . . . . 18509 1 57 no PDB 3CQP . "Human Sod1 G85r Variant, Structure I" . . . . . 100.00 153 98.04 98.04 1.35e-100 . . . . 18509 1 58 no PDB 3CQQ . "Human Sod1 G85r Variant, Structure Ii" . . . . . 100.00 153 98.04 98.04 1.31e-100 . . . . 18509 1 59 no PDB 3ECU . "Crystal Structure Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18509 1 60 no PDB 3ECV . "Crystal Structure Of The Als-Related Pathological Mutant I113t Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" . . . . . 100.00 153 98.04 98.04 6.42e-101 . . . . 18509 1 61 no PDB 3ECW . "Crystal Structure Of The Als-Related Pathological Mutant T54r Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" . . . . . 100.00 153 98.04 98.04 1.00e-100 . . . . 18509 1 62 no PDB 3GQF . "Structural And Biophysical Properties Of The Pathogenic Sod1 Variant H46rH48Q" . . . . . 100.00 153 97.39 97.39 6.72e-100 . . . . 18509 1 63 no PDB 3GZO . "Human Sod1 G93a Variant" . . . . . 100.00 154 98.04 98.04 4.89e-101 . . . . 18509 1 64 no PDB 3GZP . "Human Sod1 G93a Metal-Free Variant" . . . . . 100.00 153 98.04 98.04 4.73e-101 . . . . 18509 1 65 no PDB 3GZQ . "Human Sod1 A4v Metal-Free Variant" . . . . . 100.00 154 98.04 98.04 5.95e-101 . . . . 18509 1 66 no PDB 3H2P . "Human Sod1 D124v Variant" . . . . . 100.00 153 98.04 98.04 1.83e-100 . . . . 18509 1 67 no PDB 3H2Q . "Human Sod1 H80r Variant, P21 Crystal Form" . . . . . 100.00 153 98.04 98.04 1.11e-100 . . . . 18509 1 68 no PDB 3K91 . "Polysulfane Bridge In Cu-Zn Superoxide Dismutase" . . . . . 100.00 153 97.39 97.39 6.72e-100 . . . . 18509 1 69 no PDB 3KH3 . "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P212121 Crystal Form Cont" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18509 1 70 no PDB 3KH4 . "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P6522 Crystal Form Contai" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18509 1 71 no PDB 3QQD . "Human Sod1 H80r Variant, P212121 Crystal Form" . . . . . 100.00 154 98.04 98.04 1.24e-100 . . . . 18509 1 72 no PDB 3RE0 . "Crystal Structure Of Human Apo Cu,zn Superoxide Dismutase (sod1) Complexed With Cisplatin" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18509 1 73 no PDB 3T5W . "2me Modified Human Sod1" . . . . . 100.00 153 98.69 98.69 1.17e-101 . . . . 18509 1 74 no PDB 4A7G . "Structure Of Human I113t Sod1 Mutant Complexed With 4- Methylpiperazin-1-yl)quinazoline In The P21 Space Group." . . . . . 100.00 153 98.04 98.04 6.42e-101 . . . . 18509 1 75 no PDB 4A7Q . "Structure Of Human I113t Sod1 Mutant Complexed With 4-(4- Methyl-1,4-diazepan-1-yl)quinazoline In The P21 Space Group." . . . . . 100.00 153 98.04 98.04 6.42e-101 . . . . 18509 1 76 no PDB 4A7S . "Structure Of Human I113t Sod1 Mutant Complexed With 5- Fluorouridine In The P21 Space Group" . . . . . 100.00 153 98.04 98.04 6.42e-101 . . . . 18509 1 77 no PDB 4A7T . "Structure Of Human I113t Sod1 Mutant Complexed With Isoproteranol In The P21 Space Group" . . . . . 100.00 153 98.04 98.04 6.42e-101 . . . . 18509 1 78 no PDB 4A7U . "Structure Of Human I113t Sod1 Complexed With Adrenaline In The P21 Space Group." . . . . . 100.00 153 98.04 98.04 6.42e-101 . . . . 18509 1 79 no PDB 4A7V . "Structure Of Human I113t Sod1 Mutant Complexed With Dopamine In The P21 Space Group" . . . . . 100.00 153 98.04 98.04 6.42e-101 . . . . 18509 1 80 no PDB 4B3E . "Structure Of Copper-Zinc Superoxide Dismutase Complexed With Bicarbonate." . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 81 no PDB 4BCY . "Monomeric Human Cu,zn Superoxide Dismutase, Mutation H43f" . . . . . 100.00 153 97.39 98.04 3.99e-99 . . . . 18509 1 82 no PDB 4FF9 . "Crystal Structure Of Cysteinylated Wt Sod1" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18509 1 83 no PDB 4MCM . "Human Sod1 C57s Mutant, As-isolated" . . . . . 100.00 153 98.04 98.04 3.16e-100 . . . . 18509 1 84 no PDB 4MCN . "Human Sod1 C57s Mutant, Metal-free" . . . . . 100.00 153 98.04 98.04 3.16e-100 . . . . 18509 1 85 no PDB 4OH2 . "Crystal Structure Of Cu/zn Superoxide Dismutase I149t" . . . . . 100.00 153 99.35 99.35 1.67e-102 . . . . 18509 1 86 no DBJ BAA14373 . "unnamed protein product [Schizosaccharomyces pombe]" . . . . . 98.69 179 98.68 98.68 4.70e-100 . . . . 18509 1 87 no DBJ BAC20345 . "Cu,Zn-superoxide dismutase [Pan troglodytes]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 88 no DBJ BAG35052 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 89 no DBJ BAG73767 . "superoxide dismutase 1, soluble [synthetic construct]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 90 no EMBL CAA26182 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 91 no EMBL CAG29351 . "SOD1 [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 92 no EMBL CAG46542 . "SOD1 [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 93 no GB AAA72747 . "CuZn superoxide dismutase [synthetic construct]" . . . . . 100.00 154 100.00 100.00 3.36e-103 . . . . 18509 1 94 no GB AAA80237 . "HSOD-GlyProGly-A+, partial [synthetic construct]" . . . . . 100.00 171 100.00 100.00 1.23e-102 . . . . 18509 1 95 no GB AAB05661 . "Cu/Zn-superoxide dismutase [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 96 no GB AAB05662 . "Cu/Zn-superoxide dismutase [Homo sapiens]" . . . . . 100.00 154 98.04 98.04 1.46e-100 . . . . 18509 1 97 no GB AAB27818 . "Cu,Zn superoxide dismutase, SOD=SOD1 gene product {A to V single-site mutation} [human, Peptide Mutant, 153 aa]" . . . . . 100.00 153 98.04 98.04 5.76e-101 . . . . 18509 1 98 no REF NP_000445 . "superoxide dismutase [Cu-Zn] [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 99 no REF NP_001009025 . "superoxide dismutase [Cu-Zn] [Pan troglodytes]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 100 no REF XP_003813274 . "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 101 no REF XP_004062735 . "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" . . . . . 100.00 154 98.04 98.04 9.02e-101 . . . . 18509 1 102 no REF XP_004062736 . "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" . . . . . 100.00 154 98.04 98.04 9.02e-101 . . . . 18509 1 103 no SP P00441 . "RecName: Full=Superoxide dismutase [Cu-Zn]; AltName: Full=Superoxide dismutase 1; Short=hSod1" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 1 104 no SP P60052 . "RecName: Full=Superoxide dismutase [Cu-Zn]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18509 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 . ALA . 18509 1 2 . THR . 18509 1 3 . LYS . 18509 1 4 . ALA . 18509 1 5 . VAL . 18509 1 6 . ALA . 18509 1 7 . VAL . 18509 1 8 . LEU . 18509 1 9 . LYS . 18509 1 10 . GLY . 18509 1 11 . ASP . 18509 1 12 . GLY . 18509 1 13 . PRO . 18509 1 14 . VAL . 18509 1 15 . GLN . 18509 1 16 . GLY . 18509 1 17 . ILE . 18509 1 18 . ILE . 18509 1 19 . ASN . 18509 1 20 . PHE . 18509 1 21 . GLU . 18509 1 22 . GLN . 18509 1 23 . LYS . 18509 1 24 . GLU . 18509 1 25 . SER . 18509 1 26 . ASN . 18509 1 27 . GLY . 18509 1 28 . PRO . 18509 1 29 . VAL . 18509 1 30 . LYS . 18509 1 31 . VAL . 18509 1 32 . TRP . 18509 1 33 . GLY . 18509 1 34 . SER . 18509 1 35 . ILE . 18509 1 36 . LYS . 18509 1 37 . GLY . 18509 1 38 . LEU . 18509 1 39 . THR . 18509 1 40 . GLU . 18509 1 41 . GLY . 18509 1 42 . LEU . 18509 1 43 . HIS . 18509 1 44 . GLY . 18509 1 45 . PHE . 18509 1 46 . HIS . 18509 1 47 . VAL . 18509 1 48 . HIS . 18509 1 49 . GLU . 18509 1 50 . PHE . 18509 1 51 . GLY . 18509 1 52 . ASP . 18509 1 53 . ASN . 18509 1 54 . THR . 18509 1 55 . ALA . 18509 1 56 . GLY . 18509 1 57 . CYS . 18509 1 58 . THR . 18509 1 59 . SER . 18509 1 60 . ALA . 18509 1 61 . GLY . 18509 1 62 . PRO . 18509 1 63 . HIS . 18509 1 64 . PHE . 18509 1 65 . ASN . 18509 1 66 . PRO . 18509 1 67 . LEU . 18509 1 68 . SER . 18509 1 69 . ARG . 18509 1 70 . LYS . 18509 1 71 . HIS . 18509 1 72 . GLY . 18509 1 73 . GLY . 18509 1 74 . PRO . 18509 1 75 . LYS . 18509 1 76 . ASP . 18509 1 77 . GLU . 18509 1 78 . GLU . 18509 1 79 . ARG . 18509 1 80 . HIS . 18509 1 81 . VAL . 18509 1 82 . GLY . 18509 1 83 . ASP . 18509 1 84 . LEU . 18509 1 85 . GLY . 18509 1 86 . ASN . 18509 1 87 . VAL . 18509 1 88 . THR . 18509 1 89 . ALA . 18509 1 90 . ASP . 18509 1 91 . LYS . 18509 1 92 . ASP . 18509 1 93 . GLY . 18509 1 94 . VAL . 18509 1 95 . ALA . 18509 1 96 . ASP . 18509 1 97 . VAL . 18509 1 98 . SER . 18509 1 99 . ILE . 18509 1 100 . GLU . 18509 1 101 . ASP . 18509 1 102 . SER . 18509 1 103 . VAL . 18509 1 104 . ILE . 18509 1 105 . SER . 18509 1 106 . LEU . 18509 1 107 . SER . 18509 1 108 . GLY . 18509 1 109 . ASP . 18509 1 110 . HIS . 18509 1 111 . SER . 18509 1 112 . ILE . 18509 1 113 . ILE . 18509 1 114 . GLY . 18509 1 115 . ARG . 18509 1 116 . THR . 18509 1 117 . LEU . 18509 1 118 . VAL . 18509 1 119 . VAL . 18509 1 120 . HIS . 18509 1 121 . GLU . 18509 1 122 . LYS . 18509 1 123 . ALA . 18509 1 124 . ASP . 18509 1 125 . ASP . 18509 1 126 . LEU . 18509 1 127 . GLY . 18509 1 128 . LYS . 18509 1 129 . GLY . 18509 1 130 . GLY . 18509 1 131 . ASN . 18509 1 132 . GLU . 18509 1 133 . GLU . 18509 1 134 . SER . 18509 1 135 . THR . 18509 1 136 . LYS . 18509 1 137 . THR . 18509 1 138 . GLY . 18509 1 139 . ASN . 18509 1 140 . ALA . 18509 1 141 . GLY . 18509 1 142 . SER . 18509 1 143 . ARG . 18509 1 144 . LEU . 18509 1 145 . ALA . 18509 1 146 . CYS . 18509 1 147 . GLY . 18509 1 148 . VAL . 18509 1 149 . ILE . 18509 1 150 . GLY . 18509 1 151 . ILE . 18509 1 152 . ALA . 18509 1 153 . GLN . 18509 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 . ALA 1 1 18509 1 . THR 2 2 18509 1 . LYS 3 3 18509 1 . ALA 4 4 18509 1 . VAL 5 5 18509 1 . ALA 6 6 18509 1 . VAL 7 7 18509 1 . LEU 8 8 18509 1 . LYS 9 9 18509 1 . GLY 10 10 18509 1 . ASP 11 11 18509 1 . GLY 12 12 18509 1 . PRO 13 13 18509 1 . VAL 14 14 18509 1 . GLN 15 15 18509 1 . GLY 16 16 18509 1 . ILE 17 17 18509 1 . ILE 18 18 18509 1 . ASN 19 19 18509 1 . PHE 20 20 18509 1 . GLU 21 21 18509 1 . GLN 22 22 18509 1 . LYS 23 23 18509 1 . GLU 24 24 18509 1 . SER 25 25 18509 1 . ASN 26 26 18509 1 . GLY 27 27 18509 1 . PRO 28 28 18509 1 . VAL 29 29 18509 1 . LYS 30 30 18509 1 . VAL 31 31 18509 1 . TRP 32 32 18509 1 . GLY 33 33 18509 1 . SER 34 34 18509 1 . ILE 35 35 18509 1 . LYS 36 36 18509 1 . GLY 37 37 18509 1 . LEU 38 38 18509 1 . THR 39 39 18509 1 . GLU 40 40 18509 1 . GLY 41 41 18509 1 . LEU 42 42 18509 1 . HIS 43 43 18509 1 . GLY 44 44 18509 1 . PHE 45 45 18509 1 . HIS 46 46 18509 1 . VAL 47 47 18509 1 . HIS 48 48 18509 1 . GLU 49 49 18509 1 . PHE 50 50 18509 1 . GLY 51 51 18509 1 . ASP 52 52 18509 1 . ASN 53 53 18509 1 . THR 54 54 18509 1 . ALA 55 55 18509 1 . GLY 56 56 18509 1 . CYS 57 57 18509 1 . THR 58 58 18509 1 . SER 59 59 18509 1 . ALA 60 60 18509 1 . GLY 61 61 18509 1 . PRO 62 62 18509 1 . HIS 63 63 18509 1 . PHE 64 64 18509 1 . ASN 65 65 18509 1 . PRO 66 66 18509 1 . LEU 67 67 18509 1 . SER 68 68 18509 1 . ARG 69 69 18509 1 . LYS 70 70 18509 1 . HIS 71 71 18509 1 . GLY 72 72 18509 1 . GLY 73 73 18509 1 . PRO 74 74 18509 1 . LYS 75 75 18509 1 . ASP 76 76 18509 1 . GLU 77 77 18509 1 . GLU 78 78 18509 1 . ARG 79 79 18509 1 . HIS 80 80 18509 1 . VAL 81 81 18509 1 . GLY 82 82 18509 1 . ASP 83 83 18509 1 . LEU 84 84 18509 1 . GLY 85 85 18509 1 . ASN 86 86 18509 1 . VAL 87 87 18509 1 . THR 88 88 18509 1 . ALA 89 89 18509 1 . ASP 90 90 18509 1 . LYS 91 91 18509 1 . ASP 92 92 18509 1 . GLY 93 93 18509 1 . VAL 94 94 18509 1 . ALA 95 95 18509 1 . ASP 96 96 18509 1 . VAL 97 97 18509 1 . SER 98 98 18509 1 . ILE 99 99 18509 1 . GLU 100 100 18509 1 . ASP 101 101 18509 1 . SER 102 102 18509 1 . VAL 103 103 18509 1 . ILE 104 104 18509 1 . SER 105 105 18509 1 . LEU 106 106 18509 1 . SER 107 107 18509 1 . GLY 108 108 18509 1 . ASP 109 109 18509 1 . HIS 110 110 18509 1 . SER 111 111 18509 1 . ILE 112 112 18509 1 . ILE 113 113 18509 1 . GLY 114 114 18509 1 . ARG 115 115 18509 1 . THR 116 116 18509 1 . LEU 117 117 18509 1 . VAL 118 118 18509 1 . VAL 119 119 18509 1 . HIS 120 120 18509 1 . GLU 121 121 18509 1 . LYS 122 122 18509 1 . ALA 123 123 18509 1 . ASP 124 124 18509 1 . ASP 125 125 18509 1 . LEU 126 126 18509 1 . GLY 127 127 18509 1 . LYS 128 128 18509 1 . GLY 129 129 18509 1 . GLY 130 130 18509 1 . ASN 131 131 18509 1 . GLU 132 132 18509 1 . GLU 133 133 18509 1 . SER 134 134 18509 1 . THR 135 135 18509 1 . LYS 136 136 18509 1 . THR 137 137 18509 1 . GLY 138 138 18509 1 . ASN 139 139 18509 1 . ALA 140 140 18509 1 . GLY 141 141 18509 1 . SER 142 142 18509 1 . ARG 143 143 18509 1 . LEU 144 144 18509 1 . ALA 145 145 18509 1 . CYS 146 146 18509 1 . GLY 147 147 18509 1 . VAL 148 148 18509 1 . ILE 149 149 18509 1 . GLY 150 150 18509 1 . ILE 151 151 18509 1 . ALA 152 152 18509 1 . GLN 153 153 18509 1 stop_ save_ save_CU _Entity.Sf_category entity _Entity.Sf_framecode CU _Entity.Entry_ID 18509 _Entity.ID 2 _Entity.BMRB_code CU _Entity.Name 'COPPER (II) ION' _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID CU _Entity.Nonpolymer_comp_label $chem_comp_CU _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components 1 _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 63.546 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'COPPER (II) ION' BMRB 18509 2 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID 'COPPER (II) ION' BMRB 18509 2 CU 'Three letter code' 18509 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 1 CU $chem_comp_CU 18509 2 stop_ loop_ _Entity_atom_list.ID _Entity_atom_list.Comp_index_ID _Entity_atom_list.Comp_ID _Entity_atom_list.Atom_ID _Entity_atom_list.Entry_ID _Entity_atom_list.Entity_ID 1 1 CU CU 18509 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 18509 _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 $Superoxide_dismutase_C6A-C111S_thermostable_mutant . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18509 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 18509 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $Superoxide_dismutase_C6A-C111S_thermostable_mutant . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pPHSOD1lac1 . . . . . . 18509 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_CU _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CU _Chem_comp.Entry_ID 18509 _Chem_comp.ID CU _Chem_comp.Provenance PDB _Chem_comp.Name 'COPPER (II) ION' _Chem_comp.Type NON-POLYMER _Chem_comp.BMRB_code CU _Chem_comp.PDB_code CU _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-04-05 _Chem_comp.Modified_date 2012-04-05 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CU _Chem_comp.Number_atoms_all 1 _Chem_comp.Number_atoms_nh 1 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/Cu/q+2 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Cu _Chem_comp.Formula_weight 63.546 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID [Cu++] SMILES CACTVS 3.341 18509 CU [Cu++] SMILES_CANONICAL CACTVS 3.341 18509 CU [Cu+2] SMILES ACDLabs 10.04 18509 CU [Cu+2] SMILES 'OpenEye OEToolkits' 1.5.0 18509 CU [Cu+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 18509 CU InChI=1S/Cu/q+2 InChI InChI 1.03 18509 CU JPVYNHNXODAKFH-UHFFFAOYSA-N InChIKey InChI 1.03 18509 CU stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID copper(2+) 'SYSTEMATIC NAME' ACDLabs 10.04 18509 CU 'copper(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 18509 CU stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID CU CU CU CU . CU . . N 2 . . . 0 no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 18509 CU stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18509 _Sample.ID 1 _Sample.Type 'polycrystalline powder' _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '100% H2O' _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 'Superoxide dismutase C6A/C111S thermostable mutant' '[U-13C; U-15N; U-2H]' . . 1 $Superoxide_dismutase_C6A-C111S_thermostable_mutant . . 3.5 . . mg . . . . 18509 1 2 'Sodium Citrate' 'natural abundance' . . . . . . 20 . . mM . . . . 18509 1 3 'Polyethylene Glycol 6000' 'natural abundance' . . . . . . .20 . . w/v . . . . 18509 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 18509 _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' 0.02 . M 18509 1 pH 5 . pH 18509 1 pressure 1 . atm 18509 1 temperature 286 . K 18509 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 18509 _Software.ID 1 _Software.Name CYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 18509 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 18509 1 stop_ save_ save_UNIO _Software.Sf_category software _Software.Sf_framecode UNIO _Software.Entry_ID 18509 _Software.ID 2 _Software.Name UNIO _Software.Version 2.5.0 _Software.Details 'Using ATNOS/CANDID module in UNIO for automated peak picking and cross peak assignment' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Herrmann, Guntert and Wuthrich' . . 18509 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18509 2 collection 18509 2 'peak picking' 18509 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 18509 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 850 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 18509 _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 . 850 . . . 18509 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 18509 _Experiment_list.ID 1 _Experiment_list.Details '60 kHz MAS was used for all experiments' loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D CP-HSQC' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18509 1 2 '2D R1_15N' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18509 1 3 '2D R1_13C' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18509 1 4 '2D (H)NHH_RFDR' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18509 1 5 '3D (H)CONH' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18509 1 6 '2D NCA' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18509 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 18509 _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 TMS 'methyl protons' . . . . ppm 0 external indirect . . . . . . . . . . 18509 1 H 1 TMS 'methyl protons' . . . . ppm 0 external direct 1 . . . . . . . . . 18509 1 N 15 TMS 'methyl protons' . . . . ppm 0 external indirect . . . . . . . . . . 18509 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 18509 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D CP-HSQC' . . . 18509 1 5 '3D (H)CONH' . . . 18509 1 6 '2D NCA' . . . 18509 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 2 2 THR C C 13 170.139 0.40 . 1 . . . A 2 THR C . 18509 1 2 . 1 1 3 3 LYS H H 1 8.666 0.02 . 1 . . . A 3 LYS H . 18509 1 3 . 1 1 3 3 LYS C C 13 171.607 0.40 . 1 . . . A 3 LYS C . 18509 1 4 . 1 1 3 3 LYS CA C 13 51.178 0.40 . 1 . . . A 3 LYS CA . 18509 1 5 . 1 1 3 3 LYS N N 15 123.998 0.40 . 1 . . . A 3 LYS N . 18509 1 6 . 1 1 4 4 ALA H H 1 9.116 0.02 . 1 . . . A 4 ALA H . 18509 1 7 . 1 1 4 4 ALA C C 13 172.145 0.40 . 1 . . . A 4 ALA C . 18509 1 8 . 1 1 4 4 ALA CA C 13 47.504 0.40 . 1 . . . A 4 ALA CA . 18509 1 9 . 1 1 4 4 ALA N N 15 123.295 0.40 . 1 . . . A 4 ALA N . 18509 1 10 . 1 1 5 5 VAL H H 1 9.545 0.02 . 1 . . . A 5 VAL H . 18509 1 11 . 1 1 5 5 VAL C C 13 167.836 0.40 . 1 . . . A 5 VAL C . 18509 1 12 . 1 1 5 5 VAL CA C 13 56.875 0.40 . 1 . . . A 5 VAL CA . 18509 1 13 . 1 1 5 5 VAL N N 15 121.466 0.40 . 1 . . . A 5 VAL N . 18509 1 14 . 1 1 6 6 ALA H H 1 9.177 0.02 . 1 . . . A 6 ALA H . 18509 1 15 . 1 1 6 6 ALA C C 13 171.607 0.40 . 1 . . . A 6 ALA C . 18509 1 16 . 1 1 6 6 ALA CA C 13 47.471 0.40 . 1 . . . A 6 ALA CA . 18509 1 17 . 1 1 6 6 ALA N N 15 125.984 0.40 . 1 . . . A 6 ALA N . 18509 1 18 . 1 1 7 7 VAL H H 1 9.116 0.02 . 1 . . . A 7 VAL H . 18509 1 19 . 1 1 7 7 VAL C C 13 172.244 0.40 . 1 . . . A 7 VAL C . 18509 1 20 . 1 1 7 7 VAL CA C 13 58.476 0.40 . 1 . . . A 7 VAL CA . 18509 1 21 . 1 1 7 7 VAL N N 15 123.600 0.40 . 1 . . . A 7 VAL N . 18509 1 22 . 1 1 8 8 LEU H H 1 8.916 0.02 . 1 . . . A 8 LEU H . 18509 1 23 . 1 1 8 8 LEU C C 13 172.557 0.40 . 1 . . . A 8 LEU C . 18509 1 24 . 1 1 8 8 LEU CA C 13 51.052 0.40 . 1 . . . A 8 LEU CA . 18509 1 25 . 1 1 8 8 LEU N N 15 126.455 0.40 . 1 . . . A 8 LEU N . 18509 1 26 . 1 1 9 9 LYS H H 1 8.315 0.02 . 1 . . . A 9 LYS H . 18509 1 27 . 1 1 9 9 LYS C C 13 172.509 0.40 . 1 . . . A 9 LYS C . 18509 1 28 . 1 1 9 9 LYS CA C 13 51.897 0.40 . 1 . . . A 9 LYS CA . 18509 1 29 . 1 1 9 9 LYS N N 15 120.820 0.40 . 1 . . . A 9 LYS N . 18509 1 30 . 1 1 10 10 GLY H H 1 8.968 0.02 . 1 . . . A 10 GLY H . 18509 1 31 . 1 1 10 10 GLY C C 13 169.847 0.40 . 1 . . . A 10 GLY C . 18509 1 32 . 1 1 10 10 GLY CA C 13 42.275 0.40 . 1 . . . A 10 GLY CA . 18509 1 33 . 1 1 10 10 GLY N N 15 111.249 0.40 . 1 . . . A 10 GLY N . 18509 1 34 . 1 1 11 11 ASP H H 1 8.745 0.02 . 1 . . . A 11 ASP H . 18509 1 35 . 1 1 11 11 ASP C C 13 173.132 0.40 . 1 . . . A 11 ASP C . 18509 1 36 . 1 1 11 11 ASP CA C 13 51.317 0.40 . 1 . . . A 11 ASP CA . 18509 1 37 . 1 1 11 11 ASP N N 15 120.904 0.40 . 1 . . . A 11 ASP N . 18509 1 38 . 1 1 12 12 GLY H H 1 7.985 0.02 . 1 . . . A 12 GLY H . 18509 1 39 . 1 1 12 12 GLY CA C 13 41.200 0.40 . 1 . . . A 12 GLY CA . 18509 1 40 . 1 1 12 12 GLY N N 15 109.862 0.40 . 1 . . . A 12 GLY N . 18509 1 41 . 1 1 13 13 PRO C C 13 173.640 0.40 . 1 . . . A 13 PRO C . 18509 1 42 . 1 1 14 14 VAL H H 1 7.476 0.02 . 1 . . . A 14 VAL H . 18509 1 43 . 1 1 14 14 VAL C C 13 172.804 0.40 . 1 . . . A 14 VAL C . 18509 1 44 . 1 1 14 14 VAL CA C 13 59.884 0.40 . 1 . . . A 14 VAL CA . 18509 1 45 . 1 1 14 14 VAL N N 15 120.414 0.40 . 1 . . . A 14 VAL N . 18509 1 46 . 1 1 15 15 GLN H H 1 7.938 0.02 . 1 . . . A 15 GLN H . 18509 1 47 . 1 1 15 15 GLN C C 13 171.168 0.40 . 1 . . . A 15 GLN C . 18509 1 48 . 1 1 15 15 GLN CA C 13 50.679 0.40 . 1 . . . A 15 GLN CA . 18509 1 49 . 1 1 15 15 GLN N N 15 122.664 0.40 . 1 . . . A 15 GLN N . 18509 1 50 . 1 1 16 16 GLY H H 1 8.288 0.02 . 1 . . . A 16 GLY H . 18509 1 51 . 1 1 16 16 GLY C C 13 167.726 0.40 . 1 . . . A 16 GLY C . 18509 1 52 . 1 1 16 16 GLY CA C 13 43.625 0.40 . 1 . . . A 16 GLY CA . 18509 1 53 . 1 1 16 16 GLY N N 15 107.018 0.40 . 1 . . . A 16 GLY N . 18509 1 54 . 1 1 17 17 ILE H H 1 7.948 0.02 . 1 . . . A 17 ILE H . 18509 1 55 . 1 1 17 17 ILE C C 13 171.194 0.40 . 1 . . . A 17 ILE C . 18509 1 56 . 1 1 17 17 ILE CA C 13 58.497 0.40 . 1 . . . A 17 ILE CA . 18509 1 57 . 1 1 17 17 ILE N N 15 120.248 0.40 . 1 . . . A 17 ILE N . 18509 1 58 . 1 1 18 18 ILE H H 1 8.725 0.02 . 1 . . . A 18 ILE H . 18509 1 59 . 1 1 18 18 ILE C C 13 168.889 0.40 . 1 . . . A 18 ILE C . 18509 1 60 . 1 1 18 18 ILE CA C 13 53.431 0.40 . 1 . . . A 18 ILE CA . 18509 1 61 . 1 1 18 18 ILE N N 15 125.851 0.40 . 1 . . . A 18 ILE N . 18509 1 62 . 1 1 19 19 ASN H H 1 8.727 0.02 . 1 . . . A 19 ASN H . 18509 1 63 . 1 1 19 19 ASN C C 13 168.903 0.40 . 1 . . . A 19 ASN C . 18509 1 64 . 1 1 19 19 ASN CA C 13 49.088 0.40 . 1 . . . A 19 ASN CA . 18509 1 65 . 1 1 19 19 ASN N N 15 123.256 0.40 . 1 . . . A 19 ASN N . 18509 1 66 . 1 1 20 20 PHE H H 1 8.399 0.02 . 1 . . . A 20 PHE H . 18509 1 67 . 1 1 20 20 PHE C C 13 173.219 0.40 . 1 . . . A 20 PHE C . 18509 1 68 . 1 1 20 20 PHE CA C 13 52.058 0.40 . 1 . . . A 20 PHE CA . 18509 1 69 . 1 1 20 20 PHE N N 15 113.849 0.40 . 1 . . . A 20 PHE N . 18509 1 70 . 1 1 21 21 GLU H H 1 9.526 0.02 . 1 . . . A 21 GLU H . 18509 1 71 . 1 1 21 21 GLU C C 13 170.280 0.40 . 1 . . . A 21 GLU C . 18509 1 72 . 1 1 21 21 GLU CA C 13 53.044 0.40 . 1 . . . A 21 GLU CA . 18509 1 73 . 1 1 21 21 GLU N N 15 121.454 0.40 . 1 . . . A 21 GLU N . 18509 1 74 . 1 1 22 22 GLN H H 1 9.305 0.02 . 1 . . . A 22 GLN H . 18509 1 75 . 1 1 22 22 GLN CA C 13 51.180 0.40 . 1 . . . A 22 GLN CA . 18509 1 76 . 1 1 22 22 GLN N N 15 130.340 0.40 . 1 . . . A 22 GLN N . 18509 1 77 . 1 1 23 23 LYS H H 1 9.088 0.02 . 1 . . . A 23 LYS H . 18509 1 78 . 1 1 23 23 LYS CA C 13 57.241 0.40 . 1 . . . A 23 LYS CA . 18509 1 79 . 1 1 23 23 LYS N N 15 128.657 0.40 . 1 . . . A 23 LYS N . 18509 1 80 . 1 1 24 24 GLU CA C 13 51.392 0.40 . 1 . . . A 24 GLU CA . 18509 1 81 . 1 1 25 25 SER CA C 13 58.078 0.40 . 1 . . . A 25 SER CA . 18509 1 82 . 1 1 27 27 GLY H H 1 8.032 0.02 . 1 . . . A 27 GLY H . 18509 1 83 . 1 1 27 27 GLY CA C 13 42.925 0.40 . 1 . . . A 27 GLY CA . 18509 1 84 . 1 1 27 27 GLY N N 15 108.125 0.40 . 1 . . . A 27 GLY N . 18509 1 85 . 1 1 28 28 PRO C C 13 173.128 0.40 . 1 . . . A 28 PRO C . 18509 1 86 . 1 1 29 29 VAL H H 1 9.089 0.02 . 1 . . . A 29 VAL H . 18509 1 87 . 1 1 29 29 VAL C C 13 172.198 0.40 . 1 . . . A 29 VAL C . 18509 1 88 . 1 1 29 29 VAL CA C 13 57.720 0.40 . 1 . . . A 29 VAL CA . 18509 1 89 . 1 1 29 29 VAL N N 15 121.267 0.40 . 1 . . . A 29 VAL N . 18509 1 90 . 1 1 30 30 LYS H H 1 9.200 0.02 . 1 . . . A 30 LYS H . 18509 1 91 . 1 1 30 30 LYS C C 13 172.098 0.40 . 1 . . . A 30 LYS C . 18509 1 92 . 1 1 30 30 LYS CA C 13 52.642 0.40 . 1 . . . A 30 LYS CA . 18509 1 93 . 1 1 30 30 LYS N N 15 127.589 0.40 . 1 . . . A 30 LYS N . 18509 1 94 . 1 1 31 31 VAL H H 1 9.282 0.02 . 1 . . . A 31 VAL H . 18509 1 95 . 1 1 31 31 VAL C C 13 172.244 0.40 . 1 . . . A 31 VAL C . 18509 1 96 . 1 1 31 31 VAL CA C 13 57.139 0.40 . 1 . . . A 31 VAL CA . 18509 1 97 . 1 1 31 31 VAL N N 15 126.037 0.40 . 1 . . . A 31 VAL N . 18509 1 98 . 1 1 32 32 TRP H H 1 8.983 0.02 . 1 . . . A 32 TRP H . 18509 1 99 . 1 1 32 32 TRP C C 13 170.156 0.40 . 1 . . . A 32 TRP C . 18509 1 100 . 1 1 32 32 TRP CA C 13 53.137 0.40 . 1 . . . A 32 TRP CA . 18509 1 101 . 1 1 32 32 TRP N N 15 125.414 0.40 . 1 . . . A 32 TRP N . 18509 1 102 . 1 1 33 33 GLY H H 1 8.360 0.02 . 1 . . . A 33 GLY H . 18509 1 103 . 1 1 33 33 GLY C C 13 168.400 0.40 . 1 . . . A 33 GLY C . 18509 1 104 . 1 1 33 33 GLY CA C 13 41.567 0.40 . 1 . . . A 33 GLY CA . 18509 1 105 . 1 1 33 33 GLY N N 15 107.848 0.40 . 1 . . . A 33 GLY N . 18509 1 106 . 1 1 34 34 SER H H 1 7.838 0.02 . 1 . . . A 34 SER H . 18509 1 107 . 1 1 34 34 SER C C 13 169.618 0.40 . 1 . . . A 34 SER C . 18509 1 108 . 1 1 34 34 SER CA C 13 53.875 0.40 . 1 . . . A 34 SER CA . 18509 1 109 . 1 1 34 34 SER N N 15 114.377 0.40 . 1 . . . A 34 SER N . 18509 1 110 . 1 1 35 35 ILE H H 1 8.496 0.02 . 1 . . . A 35 ILE H . 18509 1 111 . 1 1 35 35 ILE C C 13 169.713 0.40 . 1 . . . A 35 ILE C . 18509 1 112 . 1 1 35 35 ILE CA C 13 56.769 0.40 . 1 . . . A 35 ILE CA . 18509 1 113 . 1 1 35 35 ILE N N 15 123.149 0.40 . 1 . . . A 35 ILE N . 18509 1 114 . 1 1 36 36 LYS H H 1 9.091 0.02 . 1 . . . A 36 LYS H . 18509 1 115 . 1 1 36 36 LYS C C 13 172.260 0.40 . 1 . . . A 36 LYS C . 18509 1 116 . 1 1 36 36 LYS CA C 13 51.150 0.40 . 1 . . . A 36 LYS CA . 18509 1 117 . 1 1 36 36 LYS N N 15 123.803 0.40 . 1 . . . A 36 LYS N . 18509 1 118 . 1 1 37 37 GLY H H 1 8.237 0.02 . 1 . . . A 37 GLY H . 18509 1 119 . 1 1 37 37 GLY C C 13 171.641 0.40 . 1 . . . A 37 GLY C . 18509 1 120 . 1 1 37 37 GLY CA C 13 42.361 0.40 . 1 . . . A 37 GLY CA . 18509 1 121 . 1 1 37 37 GLY N N 15 105.495 0.40 . 1 . . . A 37 GLY N . 18509 1 122 . 1 1 38 38 LEU H H 1 8.156 0.02 . 1 . . . A 38 LEU H . 18509 1 123 . 1 1 38 38 LEU C C 13 174.112 0.40 . 1 . . . A 38 LEU C . 18509 1 124 . 1 1 38 38 LEU CA C 13 50.471 0.40 . 1 . . . A 38 LEU CA . 18509 1 125 . 1 1 38 38 LEU N N 15 120.966 0.40 . 1 . . . A 38 LEU N . 18509 1 126 . 1 1 39 39 THR H H 1 8.660 0.02 . 1 . . . A 39 THR H . 18509 1 127 . 1 1 39 39 THR C C 13 173.102 0.40 . 1 . . . A 39 THR C . 18509 1 128 . 1 1 39 39 THR CA C 13 58.194 0.40 . 1 . . . A 39 THR CA . 18509 1 129 . 1 1 39 39 THR N N 15 110.363 0.40 . 1 . . . A 39 THR N . 18509 1 130 . 1 1 40 40 GLU H H 1 8.804 0.02 . 1 . . . A 40 GLU H . 18509 1 131 . 1 1 40 40 GLU C C 13 173.134 0.40 . 1 . . . A 40 GLU C . 18509 1 132 . 1 1 40 40 GLU CA C 13 54.356 0.40 . 1 . . . A 40 GLU CA . 18509 1 133 . 1 1 40 40 GLU N N 15 125.818 0.40 . 1 . . . A 40 GLU N . 18509 1 134 . 1 1 41 41 GLY H H 1 8.763 0.02 . 1 . . . A 41 GLY H . 18509 1 135 . 1 1 41 41 GLY C C 13 170.046 0.40 . 1 . . . A 41 GLY C . 18509 1 136 . 1 1 41 41 GLY CA C 13 40.054 0.40 . 1 . . . A 41 GLY CA . 18509 1 137 . 1 1 41 41 GLY N N 15 113.875 0.40 . 1 . . . A 41 GLY N . 18509 1 138 . 1 1 42 42 LEU H H 1 8.313 0.02 . 1 . . . A 42 LEU H . 18509 1 139 . 1 1 42 42 LEU C C 13 174.218 0.40 . 1 . . . A 42 LEU C . 18509 1 140 . 1 1 42 42 LEU CA C 13 52.155 0.40 . 1 . . . A 42 LEU CA . 18509 1 141 . 1 1 42 42 LEU N N 15 120.137 0.40 . 1 . . . A 42 LEU N . 18509 1 142 . 1 1 43 43 HIS H H 1 8.712 0.02 . 1 . . . A 43 HIS H . 18509 1 143 . 1 1 43 43 HIS C C 13 171.504 0.40 . 1 . . . A 43 HIS C . 18509 1 144 . 1 1 43 43 HIS CA C 13 50.985 0.40 . 1 . . . A 43 HIS CA . 18509 1 145 . 1 1 43 43 HIS N N 15 114.385 0.40 . 1 . . . A 43 HIS N . 18509 1 146 . 1 1 44 44 GLY H H 1 8.875 0.02 . 1 . . . A 44 GLY H . 18509 1 147 . 1 1 44 44 GLY C C 13 168.656 0.40 . 1 . . . A 44 GLY C . 18509 1 148 . 1 1 44 44 GLY CA C 13 44.195 0.40 . 1 . . . A 44 GLY CA . 18509 1 149 . 1 1 44 44 GLY N N 15 108.872 0.40 . 1 . . . A 44 GLY N . 18509 1 150 . 1 1 45 45 PHE H H 1 8.111 0.02 . 1 . . . A 45 PHE H . 18509 1 151 . 1 1 45 45 PHE CA C 13 53.098 0.40 . 1 . . . A 45 PHE CA . 18509 1 152 . 1 1 45 45 PHE N N 15 126.439 0.40 . 1 . . . A 45 PHE N . 18509 1 153 . 1 1 46 46 HIS H H 1 8.107 0.02 . 1 . . . A 46 HIS H . 18509 1 154 . 1 1 46 46 HIS C C 13 172.415 0.40 . 1 . . . A 46 HIS C . 18509 1 155 . 1 1 46 46 HIS CA C 13 49.206 0.40 . 1 . . . A 46 HIS CA . 18509 1 156 . 1 1 46 46 HIS N N 15 115.353 0.40 . 1 . . . A 46 HIS N . 18509 1 157 . 1 1 47 47 VAL H H 1 9.366 0.02 . 1 . . . A 47 VAL H . 18509 1 158 . 1 1 47 47 VAL C C 13 173.900 0.40 . 1 . . . A 47 VAL C . 18509 1 159 . 1 1 47 47 VAL CA C 13 58.792 0.40 . 1 . . . A 47 VAL CA . 18509 1 160 . 1 1 47 47 VAL N N 15 120.548 0.40 . 1 . . . A 47 VAL N . 18509 1 161 . 1 1 48 48 HIS H H 1 10.210 0.02 . 1 . . . A 48 HIS H . 18509 1 162 . 1 1 48 48 HIS C C 13 171.084 0.40 . 1 . . . A 48 HIS C . 18509 1 163 . 1 1 48 48 HIS CA C 13 52.756 0.40 . 1 . . . A 48 HIS CA . 18509 1 164 . 1 1 48 48 HIS N N 15 129.236 0.40 . 1 . . . A 48 HIS N . 18509 1 165 . 1 1 49 49 GLU H H 1 8.492 0.02 . 1 . . . A 49 GLU H . 18509 1 166 . 1 1 49 49 GLU C C 13 171.635 0.40 . 1 . . . A 49 GLU C . 18509 1 167 . 1 1 49 49 GLU CA C 13 57.759 0.40 . 1 . . . A 49 GLU CA . 18509 1 168 . 1 1 49 49 GLU N N 15 118.119 0.40 . 1 . . . A 49 GLU N . 18509 1 169 . 1 1 50 50 PHE H H 1 8.580 0.02 . 1 . . . A 50 PHE H . 18509 1 170 . 1 1 50 50 PHE C C 13 175.252 0.40 . 1 . . . A 50 PHE C . 18509 1 171 . 1 1 50 50 PHE CA C 13 52.900 0.40 . 1 . . . A 50 PHE CA . 18509 1 172 . 1 1 50 50 PHE N N 15 110.329 0.40 . 1 . . . A 50 PHE N . 18509 1 173 . 1 1 51 51 GLY H H 1 10.208 0.02 . 1 . . . A 51 GLY H . 18509 1 174 . 1 1 51 51 GLY C C 13 168.248 0.40 . 1 . . . A 51 GLY C . 18509 1 175 . 1 1 51 51 GLY N N 15 119.251 0.40 . 1 . . . A 51 GLY N . 18509 1 176 . 1 1 52 52 ASP H H 1 5.834 0.02 . 1 . . . A 52 ASP H . 18509 1 177 . 1 1 52 52 ASP CA C 13 48.891 0.40 . 1 . . . A 52 ASP CA . 18509 1 178 . 1 1 52 52 ASP N N 15 114.958 0.40 . 1 . . . A 52 ASP N . 18509 1 179 . 1 1 53 53 ASN H H 1 9.360 0.02 . 1 . . . A 53 ASN H . 18509 1 180 . 1 1 53 53 ASN CA C 13 48.233 0.40 . 1 . . . A 53 ASN CA . 18509 1 181 . 1 1 53 53 ASN N N 15 128.224 0.40 . 1 . . . A 53 ASN N . 18509 1 182 . 1 1 54 54 THR C C 13 168.656 0.40 . 1 . . . A 54 THR C . 18509 1 183 . 1 1 55 55 ALA H H 1 8.390 0.02 . 1 . . . A 55 ALA H . 18509 1 184 . 1 1 55 55 ALA C C 13 174.185 0.40 . 1 . . . A 55 ALA C . 18509 1 185 . 1 1 55 55 ALA CA C 13 46.155 0.40 . 1 . . . A 55 ALA CA . 18509 1 186 . 1 1 55 55 ALA N N 15 126.661 0.40 . 1 . . . A 55 ALA N . 18509 1 187 . 1 1 56 56 GLY H H 1 7.282 0.02 . 1 . . . A 56 GLY H . 18509 1 188 . 1 1 56 56 GLY C C 13 171.578 0.40 . 1 . . . A 56 GLY C . 18509 1 189 . 1 1 56 56 GLY CA C 13 42.580 0.40 . 1 . . . A 56 GLY CA . 18509 1 190 . 1 1 56 56 GLY N N 15 107.903 0.40 . 1 . . . A 56 GLY N . 18509 1 191 . 1 1 57 57 CYS H H 1 8.900 0.02 . 1 . . . A 57 CYS H . 18509 1 192 . 1 1 57 57 CYS C C 13 175.209 0.40 . 1 . . . A 57 CYS C . 18509 1 193 . 1 1 57 57 CYS CA C 13 49.088 0.40 . 1 . . . A 57 CYS CA . 18509 1 194 . 1 1 57 57 CYS N N 15 117.952 0.40 . 1 . . . A 57 CYS N . 18509 1 195 . 1 1 58 58 THR H H 1 8.505 0.02 . 1 . . . A 58 THR H . 18509 1 196 . 1 1 58 58 THR CA C 13 58.239 0.40 . 1 . . . A 58 THR CA . 18509 1 197 . 1 1 58 58 THR N N 15 119.852 0.40 . 1 . . . A 58 THR N . 18509 1 198 . 1 1 59 59 SER C C 13 170.763 0.40 . 1 . . . A 59 SER C . 18509 1 199 . 1 1 59 59 SER CA C 13 55.609 0.40 . 1 . . . A 59 SER CA . 18509 1 200 . 1 1 60 60 ALA H H 1 6.898 0.02 . 1 . . . A 60 ALA H . 18509 1 201 . 1 1 60 60 ALA CA C 13 49.940 0.40 . 1 . . . A 60 ALA CA . 18509 1 202 . 1 1 60 60 ALA N N 15 119.753 0.40 . 1 . . . A 60 ALA N . 18509 1 203 . 1 1 61 61 GLY H H 1 7.730 0.02 . 1 . . . A 61 GLY H . 18509 1 204 . 1 1 61 61 GLY CA C 13 42.805 0.40 . 1 . . . A 61 GLY CA . 18509 1 205 . 1 1 61 61 GLY N N 15 101.351 0.40 . 1 . . . A 61 GLY N . 18509 1 206 . 1 1 62 62 PRO C C 13 172.276 0.40 . 1 . . . A 62 PRO C . 18509 1 207 . 1 1 63 63 HIS H H 1 7.474 0.02 . 1 . . . A 63 HIS H . 18509 1 208 . 1 1 63 63 HIS CA C 13 52.119 0.40 . 1 . . . A 63 HIS CA . 18509 1 209 . 1 1 63 63 HIS N N 15 115.023 0.40 . 1 . . . A 63 HIS N . 18509 1 210 . 1 1 64 64 PHE C C 13 171.731 0.40 . 1 . . . A 64 PHE C . 18509 1 211 . 1 1 65 65 ASN H H 1 9.426 0.02 . 1 . . . A 65 ASN H . 18509 1 212 . 1 1 65 65 ASN CA C 13 47.753 0.40 . 1 . . . A 65 ASN CA . 18509 1 213 . 1 1 65 65 ASN N N 15 126.978 0.40 . 1 . . . A 65 ASN N . 18509 1 214 . 1 1 67 67 LEU H H 1 7.720 0.02 . 1 . . . A 67 LEU H . 18509 1 215 . 1 1 67 67 LEU C C 13 172.580 0.40 . 1 . . . A 67 LEU C . 18509 1 216 . 1 1 67 67 LEU CA C 13 50.911 0.40 . 1 . . . A 67 LEU CA . 18509 1 217 . 1 1 67 67 LEU N N 15 117.937 0.40 . 1 . . . A 67 LEU N . 18509 1 218 . 1 1 68 68 SER H H 1 7.428 0.02 . 1 . . . A 68 SER H . 18509 1 219 . 1 1 68 68 SER CA C 13 55.953 0.40 . 1 . . . A 68 SER CA . 18509 1 220 . 1 1 68 68 SER N N 15 110.842 0.40 . 1 . . . A 68 SER N . 18509 1 221 . 1 1 69 69 ARG H H 1 8.508 0.02 . 1 . . . A 69 ARG H . 18509 1 222 . 1 1 69 69 ARG C C 13 173.381 0.40 . 1 . . . A 69 ARG C . 18509 1 223 . 1 1 69 69 ARG CA C 13 50.543 0.40 . 1 . . . A 69 ARG CA . 18509 1 224 . 1 1 69 69 ARG N N 15 120.782 0.40 . 1 . . . A 69 ARG N . 18509 1 225 . 1 1 70 70 LYS H H 1 8.745 0.02 . 1 . . . A 70 LYS H . 18509 1 226 . 1 1 70 70 LYS C C 13 169.994 0.40 . 1 . . . A 70 LYS C . 18509 1 227 . 1 1 70 70 LYS CA C 13 52.596 0.40 . 1 . . . A 70 LYS CA . 18509 1 228 . 1 1 70 70 LYS N N 15 118.055 0.40 . 1 . . . A 70 LYS N . 18509 1 229 . 1 1 71 71 HIS H H 1 7.152 0.02 . 1 . . . A 71 HIS H . 18509 1 230 . 1 1 71 71 HIS C C 13 171.534 0.40 . 1 . . . A 71 HIS C . 18509 1 231 . 1 1 71 71 HIS CA C 13 52.549 0.40 . 1 . . . A 71 HIS CA . 18509 1 232 . 1 1 71 71 HIS N N 15 111.871 0.40 . 1 . . . A 71 HIS N . 18509 1 233 . 1 1 72 72 GLY H H 1 7.209 0.02 . 1 . . . A 72 GLY H . 18509 1 234 . 1 1 72 72 GLY C C 13 168.634 0.40 . 1 . . . A 72 GLY C . 18509 1 235 . 1 1 72 72 GLY CA C 13 41.274 0.40 . 1 . . . A 72 GLY CA . 18509 1 236 . 1 1 72 72 GLY N N 15 112.910 0.40 . 1 . . . A 72 GLY N . 18509 1 237 . 1 1 73 73 GLY H H 1 8.789 0.02 . 1 . . . A 73 GLY H . 18509 1 238 . 1 1 73 73 GLY CA C 13 41.221 0.40 . 1 . . . A 73 GLY CA . 18509 1 239 . 1 1 73 73 GLY N N 15 105.207 0.40 . 1 . . . A 73 GLY N . 18509 1 240 . 1 1 74 74 PRO C C 13 175.753 0.40 . 1 . . . A 74 PRO C . 18509 1 241 . 1 1 75 75 LYS H H 1 8.651 0.02 . 1 . . . A 75 LYS H . 18509 1 242 . 1 1 75 75 LYS C C 13 173.640 0.40 . 1 . . . A 75 LYS C . 18509 1 243 . 1 1 75 75 LYS CA C 13 51.103 0.40 . 1 . . . A 75 LYS CA . 18509 1 244 . 1 1 75 75 LYS N N 15 114.868 0.40 . 1 . . . A 75 LYS N . 18509 1 245 . 1 1 76 76 ASP H H 1 7.461 0.02 . 1 . . . A 76 ASP H . 18509 1 246 . 1 1 76 76 ASP C C 13 172.557 0.40 . 1 . . . A 76 ASP C . 18509 1 247 . 1 1 76 76 ASP CA C 13 51.309 0.40 . 1 . . . A 76 ASP CA . 18509 1 248 . 1 1 76 76 ASP N N 15 120.414 0.40 . 1 . . . A 76 ASP N . 18509 1 249 . 1 1 77 77 GLU H H 1 8.315 0.02 . 1 . . . A 77 GLU H . 18509 1 250 . 1 1 77 77 GLU C C 13 174.101 0.40 . 1 . . . A 77 GLU C . 18509 1 251 . 1 1 77 77 GLU CA C 13 55.513 0.40 . 1 . . . A 77 GLU CA . 18509 1 252 . 1 1 77 77 GLU N N 15 120.820 0.40 . 1 . . . A 77 GLU N . 18509 1 253 . 1 1 78 78 GLU H H 1 8.109 0.02 . 1 . . . A 78 GLU H . 18509 1 254 . 1 1 78 78 GLU C C 13 168.285 0.40 . 1 . . . A 78 GLU C . 18509 1 255 . 1 1 78 78 GLU CA C 13 52.078 0.40 . 1 . . . A 78 GLU CA . 18509 1 256 . 1 1 78 78 GLU N N 15 119.251 0.40 . 1 . . . A 78 GLU N . 18509 1 257 . 1 1 79 79 ARG H H 1 6.999 0.02 . 1 . . . A 79 ARG H . 18509 1 258 . 1 1 79 79 ARG C C 13 172.123 0.40 . 1 . . . A 79 ARG C . 18509 1 259 . 1 1 79 79 ARG CA C 13 51.074 0.40 . 1 . . . A 79 ARG CA . 18509 1 260 . 1 1 79 79 ARG N N 15 118.991 0.40 . 1 . . . A 79 ARG N . 18509 1 261 . 1 1 80 80 HIS H H 1 8.355 0.02 . 1 . . . A 80 HIS H . 18509 1 262 . 1 1 80 80 HIS CA C 13 49.953 0.40 . 1 . . . A 80 HIS CA . 18509 1 263 . 1 1 80 80 HIS N N 15 118.000 0.40 . 1 . . . A 80 HIS N . 18509 1 264 . 1 1 81 81 VAL C C 13 173.460 0.40 . 1 . . . A 81 VAL C . 18509 1 265 . 1 1 82 82 GLY H H 1 8.487 0.02 . 1 . . . A 82 GLY H . 18509 1 266 . 1 1 82 82 GLY C C 13 170.370 0.40 . 1 . . . A 82 GLY C . 18509 1 267 . 1 1 82 82 GLY CA C 13 42.688 0.40 . 1 . . . A 82 GLY CA . 18509 1 268 . 1 1 82 82 GLY N N 15 97.322 0.40 . 1 . . . A 82 GLY N . 18509 1 269 . 1 1 83 83 ASP H H 1 7.127 0.02 . 1 . . . A 83 ASP H . 18509 1 270 . 1 1 83 83 ASP C C 13 168.737 0.40 . 1 . . . A 83 ASP C . 18509 1 271 . 1 1 83 83 ASP CA C 13 52.918 0.40 . 1 . . . A 83 ASP CA . 18509 1 272 . 1 1 83 83 ASP N N 15 120.890 0.40 . 1 . . . A 83 ASP N . 18509 1 273 . 1 1 84 84 LEU H H 1 7.128 0.02 . 1 . . . A 84 LEU H . 18509 1 274 . 1 1 84 84 LEU C C 13 173.212 0.40 . 1 . . . A 84 LEU C . 18509 1 275 . 1 1 84 84 LEU CA C 13 50.433 0.40 . 1 . . . A 84 LEU CA . 18509 1 276 . 1 1 84 84 LEU N N 15 120.154 0.40 . 1 . . . A 84 LEU N . 18509 1 277 . 1 1 85 85 GLY H H 1 8.260 0.02 . 1 . . . A 85 GLY H . 18509 1 278 . 1 1 85 85 GLY C C 13 167.654 0.40 . 1 . . . A 85 GLY C . 18509 1 279 . 1 1 85 85 GLY CA C 13 43.011 0.40 . 1 . . . A 85 GLY CA . 18509 1 280 . 1 1 85 85 GLY N N 15 106.867 0.40 . 1 . . . A 85 GLY N . 18509 1 281 . 1 1 86 86 ASN H H 1 8.041 0.02 . 1 . . . A 86 ASN H . 18509 1 282 . 1 1 86 86 ASN C C 13 173.942 0.40 . 1 . . . A 86 ASN C . 18509 1 283 . 1 1 86 86 ASN CA C 13 49.266 0.40 . 1 . . . A 86 ASN CA . 18509 1 284 . 1 1 86 86 ASN N N 15 117.454 0.40 . 1 . . . A 86 ASN N . 18509 1 285 . 1 1 87 87 VAL H H 1 8.960 0.02 . 1 . . . A 87 VAL H . 18509 1 286 . 1 1 87 87 VAL C C 13 171.526 0.40 . 1 . . . A 87 VAL C . 18509 1 287 . 1 1 87 87 VAL CA C 13 55.708 0.40 . 1 . . . A 87 VAL CA . 18509 1 288 . 1 1 87 87 VAL N N 15 113.370 0.40 . 1 . . . A 87 VAL N . 18509 1 289 . 1 1 88 88 THR H H 1 8.681 0.02 . 1 . . . A 88 THR H . 18509 1 290 . 1 1 88 88 THR C C 13 170.367 0.40 . 1 . . . A 88 THR C . 18509 1 291 . 1 1 88 88 THR CA C 13 58.694 0.40 . 1 . . . A 88 THR CA . 18509 1 292 . 1 1 88 88 THR N N 15 117.939 0.40 . 1 . . . A 88 THR N . 18509 1 293 . 1 1 89 89 ALA H H 1 9.377 0.02 . 1 . . . A 89 ALA H . 18509 1 294 . 1 1 89 89 ALA C C 13 174.480 0.40 . 1 . . . A 89 ALA C . 18509 1 295 . 1 1 89 89 ALA CA C 13 46.369 0.40 . 1 . . . A 89 ALA CA . 18509 1 296 . 1 1 89 89 ALA N N 15 128.674 0.40 . 1 . . . A 89 ALA N . 18509 1 297 . 1 1 90 90 ASP H H 1 8.455 0.02 . 1 . . . A 90 ASP H . 18509 1 298 . 1 1 90 90 ASP C C 13 173.825 0.40 . 1 . . . A 90 ASP C . 18509 1 299 . 1 1 90 90 ASP CA C 13 49.347 0.40 . 1 . . . A 90 ASP CA . 18509 1 300 . 1 1 90 90 ASP N N 15 124.235 0.40 . 1 . . . A 90 ASP N . 18509 1 301 . 1 1 91 91 LYS H H 1 8.231 0.02 . 1 . . . A 91 LYS H . 18509 1 302 . 1 1 91 91 LYS C C 13 174.101 0.40 . 1 . . . A 91 LYS C . 18509 1 303 . 1 1 91 91 LYS CA C 13 55.279 0.40 . 1 . . . A 91 LYS CA . 18509 1 304 . 1 1 91 91 LYS N N 15 114.942 0.40 . 1 . . . A 91 LYS N . 18509 1 305 . 1 1 92 92 ASP H H 1 8.109 0.02 . 1 . . . A 92 ASP H . 18509 1 306 . 1 1 92 92 ASP C C 13 173.020 0.40 . 1 . . . A 92 ASP C . 18509 1 307 . 1 1 92 92 ASP CA C 13 51.127 0.40 . 1 . . . A 92 ASP CA . 18509 1 308 . 1 1 92 92 ASP N N 15 119.251 0.40 . 1 . . . A 92 ASP N . 18509 1 309 . 1 1 93 93 GLY H H 1 8.405 0.02 . 1 . . . A 93 GLY H . 18509 1 310 . 1 1 93 93 GLY C C 13 169.706 0.40 . 1 . . . A 93 GLY C . 18509 1 311 . 1 1 93 93 GLY CA C 13 43.763 0.40 . 1 . . . A 93 GLY CA . 18509 1 312 . 1 1 93 93 GLY N N 15 110.868 0.40 . 1 . . . A 93 GLY N . 18509 1 313 . 1 1 94 94 VAL H H 1 7.814 0.02 . 1 . . . A 94 VAL H . 18509 1 314 . 1 1 94 94 VAL C C 13 173.510 0.40 . 1 . . . A 94 VAL C . 18509 1 315 . 1 1 94 94 VAL CA C 13 58.185 0.40 . 1 . . . A 94 VAL CA . 18509 1 316 . 1 1 94 94 VAL N N 15 118.755 0.40 . 1 . . . A 94 VAL N . 18509 1 317 . 1 1 95 95 ALA H H 1 9.763 0.02 . 1 . . . A 95 ALA H . 18509 1 318 . 1 1 95 95 ALA C C 13 171.635 0.40 . 1 . . . A 95 ALA C . 18509 1 319 . 1 1 95 95 ALA CA C 13 46.914 0.40 . 1 . . . A 95 ALA CA . 18509 1 320 . 1 1 95 95 ALA N N 15 131.313 0.40 . 1 . . . A 95 ALA N . 18509 1 321 . 1 1 96 96 ASP H H 1 8.515 0.02 . 1 . . . A 96 ASP H . 18509 1 322 . 1 1 96 96 ASP C C 13 172.336 0.40 . 1 . . . A 96 ASP C . 18509 1 323 . 1 1 96 96 ASP N N 15 125.170 0.40 . 1 . . . A 96 ASP N . 18509 1 324 . 1 1 97 97 VAL H H 1 8.703 0.02 . 1 . . . A 97 VAL H . 18509 1 325 . 1 1 97 97 VAL C C 13 173.488 0.40 . 1 . . . A 97 VAL C . 18509 1 326 . 1 1 97 97 VAL CA C 13 58.243 0.40 . 1 . . . A 97 VAL CA . 18509 1 327 . 1 1 97 97 VAL N N 15 125.879 0.40 . 1 . . . A 97 VAL N . 18509 1 328 . 1 1 98 98 SER H H 1 8.784 0.02 . 1 . . . A 98 SER H . 18509 1 329 . 1 1 98 98 SER C C 13 169.715 0.40 . 1 . . . A 98 SER C . 18509 1 330 . 1 1 98 98 SER CA C 13 55.068 0.40 . 1 . . . A 98 SER CA . 18509 1 331 . 1 1 98 98 SER N N 15 123.017 0.40 . 1 . . . A 98 SER N . 18509 1 332 . 1 1 99 99 ILE H H 1 9.411 0.02 . 1 . . . A 99 ILE H . 18509 1 333 . 1 1 99 99 ILE C C 13 171.321 0.40 . 1 . . . A 99 ILE C . 18509 1 334 . 1 1 99 99 ILE CA C 13 57.155 0.40 . 1 . . . A 99 ILE CA . 18509 1 335 . 1 1 99 99 ILE N N 15 125.807 0.40 . 1 . . . A 99 ILE N . 18509 1 336 . 1 1 100 100 GLU H H 1 8.652 0.02 . 1 . . . A 100 GLU H . 18509 1 337 . 1 1 100 100 GLU C C 13 172.098 0.40 . 1 . . . A 100 GLU C . 18509 1 338 . 1 1 100 100 GLU CA C 13 52.290 0.40 . 1 . . . A 100 GLU CA . 18509 1 339 . 1 1 100 100 GLU N N 15 124.068 0.40 . 1 . . . A 100 GLU N . 18509 1 340 . 1 1 101 101 ASP H H 1 9.317 0.02 . 1 . . . A 101 ASP H . 18509 1 341 . 1 1 101 101 ASP C C 13 171.144 0.40 . 1 . . . A 101 ASP C . 18509 1 342 . 1 1 101 101 ASP CA C 13 51.419 0.40 . 1 . . . A 101 ASP CA . 18509 1 343 . 1 1 101 101 ASP N N 15 126.109 0.40 . 1 . . . A 101 ASP N . 18509 1 344 . 1 1 102 102 SER H H 1 8.933 0.02 . 1 . . . A 102 SER H . 18509 1 345 . 1 1 102 102 SER C C 13 171.596 0.40 . 1 . . . A 102 SER C . 18509 1 346 . 1 1 102 102 SER CA C 13 55.245 0.40 . 1 . . . A 102 SER CA . 18509 1 347 . 1 1 102 102 SER N N 15 118.470 0.40 . 1 . . . A 102 SER N . 18509 1 348 . 1 1 103 103 VAL H H 1 8.148 0.02 . 1 . . . A 103 VAL H . 18509 1 349 . 1 1 103 103 VAL CA C 13 61.450 0.40 . 1 . . . A 103 VAL CA . 18509 1 350 . 1 1 103 103 VAL N N 15 123.179 0.40 . 1 . . . A 103 VAL N . 18509 1 351 . 1 1 104 104 ILE C C 13 169.576 0.40 . 1 . . . A 104 ILE C . 18509 1 352 . 1 1 104 104 ILE CA C 13 60.194 0.40 . 1 . . . A 104 ILE CA . 18509 1 353 . 1 1 105 105 SER H H 1 6.988 0.02 . 1 . . . A 105 SER H . 18509 1 354 . 1 1 105 105 SER C C 13 170.046 0.40 . 1 . . . A 105 SER C . 18509 1 355 . 1 1 105 105 SER CA C 13 52.550 0.40 . 1 . . . A 105 SER CA . 18509 1 356 . 1 1 105 105 SER N N 15 107.618 0.40 . 1 . . . A 105 SER N . 18509 1 357 . 1 1 106 106 LEU H H 1 8.313 0.02 . 1 . . . A 106 LEU H . 18509 1 358 . 1 1 106 106 LEU N N 15 120.137 0.40 . 1 . . . A 106 LEU N . 18509 1 359 . 1 1 107 107 SER C C 13 170.701 0.40 . 1 . . . A 107 SER C . 18509 1 360 . 1 1 107 107 SER CA C 13 54.540 0.40 . 1 . . . A 107 SER CA . 18509 1 361 . 1 1 108 108 GLY H H 1 8.717 0.02 . 1 . . . A 108 GLY H . 18509 1 362 . 1 1 108 108 GLY C C 13 173.128 0.40 . 1 . . . A 108 GLY C . 18509 1 363 . 1 1 108 108 GLY CA C 13 41.287 0.40 . 1 . . . A 108 GLY CA . 18509 1 364 . 1 1 108 108 GLY N N 15 107.603 0.40 . 1 . . . A 108 GLY N . 18509 1 365 . 1 1 109 109 ASP H H 1 9.019 0.02 . 1 . . . A 109 ASP H . 18509 1 366 . 1 1 109 109 ASP C C 13 171.904 0.40 . 1 . . . A 109 ASP C . 18509 1 367 . 1 1 109 109 ASP N N 15 120.664 0.40 . 1 . . . A 109 ASP N . 18509 1 368 . 1 1 110 110 HIS H H 1 9.283 0.02 . 1 . . . A 110 HIS H . 18509 1 369 . 1 1 110 110 HIS N N 15 116.324 0.40 . 1 . . . A 110 HIS N . 18509 1 370 . 1 1 111 111 SER H H 1 7.156 0.02 . 1 . . . A 111 SER H . 18509 1 371 . 1 1 111 111 SER CA C 13 54.681 0.40 . 1 . . . A 111 SER CA . 18509 1 372 . 1 1 111 111 SER N N 15 110.225 0.40 . 1 . . . A 111 SER N . 18509 1 373 . 1 1 112 112 ILE H H 1 7.837 0.02 . 1 . . . A 112 ILE H . 18509 1 374 . 1 1 112 112 ILE C C 13 171.419 0.40 . 1 . . . A 112 ILE C . 18509 1 375 . 1 1 112 112 ILE CA C 13 57.239 0.40 . 1 . . . A 112 ILE CA . 18509 1 376 . 1 1 112 112 ILE N N 15 117.053 0.40 . 1 . . . A 112 ILE N . 18509 1 377 . 1 1 113 113 ILE H H 1 7.592 0.02 . 1 . . . A 113 ILE H . 18509 1 378 . 1 1 113 113 ILE C C 13 173.604 0.40 . 1 . . . A 113 ILE C . 18509 1 379 . 1 1 113 113 ILE CA C 13 58.318 0.40 . 1 . . . A 113 ILE CA . 18509 1 380 . 1 1 113 113 ILE N N 15 121.032 0.40 . 1 . . . A 113 ILE N . 18509 1 381 . 1 1 114 114 GLY H H 1 9.575 0.02 . 1 . . . A 114 GLY H . 18509 1 382 . 1 1 114 114 GLY C C 13 169.739 0.40 . 1 . . . A 114 GLY C . 18509 1 383 . 1 1 114 114 GLY CA C 13 41.910 0.40 . 1 . . . A 114 GLY CA . 18509 1 384 . 1 1 114 114 GLY N N 15 112.661 0.40 . 1 . . . A 114 GLY N . 18509 1 385 . 1 1 115 115 ARG H H 1 7.464 0.02 . 1 . . . A 115 ARG H . 18509 1 386 . 1 1 115 115 ARG C C 13 171.079 0.40 . 1 . . . A 115 ARG C . 18509 1 387 . 1 1 115 115 ARG CA C 13 51.663 0.40 . 1 . . . A 115 ARG CA . 18509 1 388 . 1 1 115 115 ARG N N 15 118.398 0.40 . 1 . . . A 115 ARG N . 18509 1 389 . 1 1 116 116 THR H H 1 6.677 0.02 . 1 . . . A 116 THR H . 18509 1 390 . 1 1 116 116 THR C C 13 169.821 0.40 . 1 . . . A 116 THR C . 18509 1 391 . 1 1 116 116 THR CA C 13 59.633 0.40 . 1 . . . A 116 THR CA . 18509 1 392 . 1 1 116 116 THR N N 15 112.218 0.40 . 1 . . . A 116 THR N . 18509 1 393 . 1 1 117 117 LEU H H 1 8.799 0.02 . 1 . . . A 117 LEU H . 18509 1 394 . 1 1 117 117 LEU C C 13 171.126 0.40 . 1 . . . A 117 LEU C . 18509 1 395 . 1 1 117 117 LEU CA C 13 50.415 0.40 . 1 . . . A 117 LEU CA . 18509 1 396 . 1 1 117 117 LEU N N 15 129.477 0.40 . 1 . . . A 117 LEU N . 18509 1 397 . 1 1 118 118 VAL H H 1 8.906 0.02 . 1 . . . A 118 VAL H . 18509 1 398 . 1 1 118 118 VAL C C 13 170.267 0.40 . 1 . . . A 118 VAL C . 18509 1 399 . 1 1 118 118 VAL CA C 13 58.139 0.40 . 1 . . . A 118 VAL CA . 18509 1 400 . 1 1 118 118 VAL N N 15 125.091 0.40 . 1 . . . A 118 VAL N . 18509 1 401 . 1 1 119 119 VAL H H 1 7.982 0.02 . 1 . . . A 119 VAL H . 18509 1 402 . 1 1 119 119 VAL C C 13 171.175 0.40 . 1 . . . A 119 VAL C . 18509 1 403 . 1 1 119 119 VAL CA C 13 55.271 0.40 . 1 . . . A 119 VAL CA . 18509 1 404 . 1 1 119 119 VAL N N 15 120.716 0.40 . 1 . . . A 119 VAL N . 18509 1 405 . 1 1 120 120 HIS H H 1 8.935 0.02 . 1 . . . A 120 HIS H . 18509 1 406 . 1 1 120 120 HIS C C 13 172.599 0.40 . 1 . . . A 120 HIS C . 18509 1 407 . 1 1 120 120 HIS CA C 13 53.394 0.40 . 1 . . . A 120 HIS CA . 18509 1 408 . 1 1 120 120 HIS N N 15 125.052 0.40 . 1 . . . A 120 HIS N . 18509 1 409 . 1 1 121 121 GLU H H 1 9.178 0.02 . 1 . . . A 121 GLU H . 18509 1 410 . 1 1 121 121 GLU C C 13 172.304 0.40 . 1 . . . A 121 GLU C . 18509 1 411 . 1 1 121 121 GLU CA C 13 56.090 0.40 . 1 . . . A 121 GLU CA . 18509 1 412 . 1 1 121 121 GLU N N 15 121.453 0.40 . 1 . . . A 121 GLU N . 18509 1 413 . 1 1 122 122 LYS H H 1 8.478 0.02 . 1 . . . A 122 LYS H . 18509 1 414 . 1 1 122 122 LYS C C 13 171.523 0.40 . 1 . . . A 122 LYS C . 18509 1 415 . 1 1 122 122 LYS CA C 13 50.619 0.40 . 1 . . . A 122 LYS CA . 18509 1 416 . 1 1 122 122 LYS N N 15 115.248 0.40 . 1 . . . A 122 LYS N . 18509 1 417 . 1 1 123 123 ALA H H 1 7.796 0.02 . 1 . . . A 123 ALA H . 18509 1 418 . 1 1 123 123 ALA C C 13 173.219 0.40 . 1 . . . A 123 ALA C . 18509 1 419 . 1 1 123 123 ALA CA C 13 48.850 0.40 . 1 . . . A 123 ALA CA . 18509 1 420 . 1 1 123 123 ALA N N 15 120.866 0.40 . 1 . . . A 123 ALA N . 18509 1 421 . 1 1 124 124 ASP H H 1 10.165 0.02 . 1 . . . A 124 ASP H . 18509 1 422 . 1 1 124 124 ASP C C 13 174.458 0.40 . 1 . . . A 124 ASP C . 18509 1 423 . 1 1 124 124 ASP CA C 13 49.408 0.40 . 1 . . . A 124 ASP CA . 18509 1 424 . 1 1 124 124 ASP N N 15 121.799 0.40 . 1 . . . A 124 ASP N . 18509 1 425 . 1 1 125 125 ASP H H 1 10.055 0.02 . 1 . . . A 125 ASP H . 18509 1 426 . 1 1 125 125 ASP C C 13 175.231 0.40 . 1 . . . A 125 ASP C . 18509 1 427 . 1 1 125 125 ASP CA C 13 50.939 0.40 . 1 . . . A 125 ASP CA . 18509 1 428 . 1 1 125 125 ASP N N 15 129.369 0.40 . 1 . . . A 125 ASP N . 18509 1 429 . 1 1 126 126 LEU H H 1 10.483 0.02 . 1 . . . A 126 LEU H . 18509 1 430 . 1 1 126 126 LEU C C 13 173.964 0.40 . 1 . . . A 126 LEU C . 18509 1 431 . 1 1 126 126 LEU N N 15 117.190 0.40 . 1 . . . A 126 LEU N . 18509 1 432 . 1 1 127 127 GLY H H 1 8.637 0.02 . 1 . . . A 127 GLY H . 18509 1 433 . 1 1 127 127 GLY CA C 13 42.878 0.40 . 1 . . . A 127 GLY CA . 18509 1 434 . 1 1 127 127 GLY N N 15 103.809 0.40 . 1 . . . A 127 GLY N . 18509 1 435 . 1 1 128 128 LYS H H 1 7.158 0.02 . 1 . . . A 128 LYS H . 18509 1 436 . 1 1 128 128 LYS CA C 13 51.740 0.40 . 1 . . . A 128 LYS CA . 18509 1 437 . 1 1 128 128 LYS N N 15 118.290 0.40 . 1 . . . A 128 LYS N . 18509 1 438 . 1 1 129 129 GLY H H 1 8.913 0.02 . 1 . . . A 129 GLY H . 18509 1 439 . 1 1 129 129 GLY C C 13 171.524 0.40 . 1 . . . A 129 GLY C . 18509 1 440 . 1 1 129 129 GLY CA C 13 42.113 0.40 . 1 . . . A 129 GLY CA . 18509 1 441 . 1 1 129 129 GLY N N 15 108.507 0.40 . 1 . . . A 129 GLY N . 18509 1 442 . 1 1 130 130 GLY H H 1 8.723 0.02 . 1 . . . A 130 GLY H . 18509 1 443 . 1 1 130 130 GLY C C 13 169.994 0.40 . 1 . . . A 130 GLY C . 18509 1 444 . 1 1 130 130 GLY CA C 13 42.419 0.40 . 1 . . . A 130 GLY CA . 18509 1 445 . 1 1 130 130 GLY N N 15 108.537 0.40 . 1 . . . A 130 GLY N . 18509 1 446 . 1 1 131 131 ASN H H 1 7.152 0.02 . 1 . . . A 131 ASN H . 18509 1 447 . 1 1 131 131 ASN C C 13 172.236 0.40 . 1 . . . A 131 ASN C . 18509 1 448 . 1 1 131 131 ASN N N 15 111.951 0.40 . 1 . . . A 131 ASN N . 18509 1 449 . 1 1 132 132 GLU H H 1 8.935 0.02 . 1 . . . A 132 GLU H . 18509 1 450 . 1 1 132 132 GLU C C 13 171.084 0.40 . 1 . . . A 132 GLU C . 18509 1 451 . 1 1 132 132 GLU N N 15 120.461 0.40 . 1 . . . A 132 GLU N . 18509 1 452 . 1 1 133 133 GLU H H 1 8.775 0.02 . 1 . . . A 133 GLU H . 18509 1 453 . 1 1 133 133 GLU C C 13 176.239 0.40 . 1 . . . A 133 GLU C . 18509 1 454 . 1 1 133 133 GLU N N 15 120.137 0.40 . 1 . . . A 133 GLU N . 18509 1 455 . 1 1 134 134 SER H H 1 8.117 0.02 . 1 . . . A 134 SER H . 18509 1 456 . 1 1 134 134 SER CA C 13 59.046 0.40 . 1 . . . A 134 SER CA . 18509 1 457 . 1 1 134 134 SER N N 15 114.981 0.40 . 1 . . . A 134 SER N . 18509 1 458 . 1 1 135 135 THR H H 1 7.206 0.02 . 1 . . . A 135 THR H . 18509 1 459 . 1 1 135 135 THR C C 13 172.804 0.40 . 1 . . . A 135 THR C . 18509 1 460 . 1 1 135 135 THR CA C 13 60.029 0.40 . 1 . . . A 135 THR CA . 18509 1 461 . 1 1 135 135 THR N N 15 102.263 0.40 . 1 . . . A 135 THR N . 18509 1 462 . 1 1 136 136 LYS H H 1 7.884 0.02 . 1 . . . A 136 LYS H . 18509 1 463 . 1 1 136 136 LYS N N 15 122.108 0.40 . 1 . . . A 136 LYS N . 18509 1 464 . 1 1 137 137 THR H H 1 8.630 0.02 . 1 . . . A 137 THR H . 18509 1 465 . 1 1 137 137 THR N N 15 105.718 0.40 . 1 . . . A 137 THR N . 18509 1 466 . 1 1 138 138 GLY H H 1 7.426 0.02 . 1 . . . A 138 GLY H . 18509 1 467 . 1 1 138 138 GLY CA C 13 42.483 0.40 . 1 . . . A 138 GLY CA . 18509 1 468 . 1 1 138 138 GLY N N 15 111.372 0.40 . 1 . . . A 138 GLY N . 18509 1 469 . 1 1 139 139 ASN H H 1 7.545 0.02 . 1 . . . A 139 ASN H . 18509 1 470 . 1 1 139 139 ASN N N 15 107.496 0.40 . 1 . . . A 139 ASN N . 18509 1 471 . 1 1 140 140 ALA H H 1 6.368 0.02 . 1 . . . A 140 ALA H . 18509 1 472 . 1 1 140 140 ALA C C 13 173.571 0.40 . 1 . . . A 140 ALA C . 18509 1 473 . 1 1 140 140 ALA N N 15 114.542 0.40 . 1 . . . A 140 ALA N . 18509 1 474 . 1 1 141 141 GLY H H 1 8.271 0.02 . 1 . . . A 141 GLY H . 18509 1 475 . 1 1 141 141 GLY C C 13 173.542 0.40 . 1 . . . A 141 GLY C . 18509 1 476 . 1 1 141 141 GLY N N 15 105.287 0.40 . 1 . . . A 141 GLY N . 18509 1 477 . 1 1 142 142 SER H H 1 9.196 0.02 . 1 . . . A 142 SER H . 18509 1 478 . 1 1 142 142 SER C C 13 170.188 0.40 . 1 . . . A 142 SER C . 18509 1 479 . 1 1 142 142 SER N N 15 118.771 0.40 . 1 . . . A 142 SER N . 18509 1 480 . 1 1 143 143 ARG H H 1 8.943 0.02 . 1 . . . A 143 ARG H . 18509 1 481 . 1 1 143 143 ARG C C 13 171.596 0.40 . 1 . . . A 143 ARG C . 18509 1 482 . 1 1 143 143 ARG N N 15 120.189 0.40 . 1 . . . A 143 ARG N . 18509 1 483 . 1 1 144 144 LEU H H 1 8.395 0.02 . 1 . . . A 144 LEU H . 18509 1 484 . 1 1 144 144 LEU C C 13 174.393 0.40 . 1 . . . A 144 LEU C . 18509 1 485 . 1 1 144 144 LEU CA C 13 53.375 0.40 . 1 . . . A 144 LEU CA . 18509 1 486 . 1 1 144 144 LEU N N 15 122.907 0.40 . 1 . . . A 144 LEU N . 18509 1 487 . 1 1 145 145 ALA H H 1 7.356 0.02 . 1 . . . A 145 ALA H . 18509 1 488 . 1 1 145 145 ALA C C 13 171.752 0.40 . 1 . . . A 145 ALA C . 18509 1 489 . 1 1 145 145 ALA CA C 13 48.129 0.40 . 1 . . . A 145 ALA CA . 18509 1 490 . 1 1 145 145 ALA N N 15 114.159 0.40 . 1 . . . A 145 ALA N . 18509 1 491 . 1 1 146 146 CYS H H 1 9.008 0.02 . 1 . . . A 146 CYS H . 18509 1 492 . 1 1 146 146 CYS C C 13 170.087 0.40 . 1 . . . A 146 CYS C . 18509 1 493 . 1 1 146 146 CYS CA C 13 51.077 0.40 . 1 . . . A 146 CYS CA . 18509 1 494 . 1 1 146 146 CYS N N 15 110.738 0.40 . 1 . . . A 146 CYS N . 18509 1 495 . 1 1 147 147 GLY H H 1 8.018 0.02 . 1 . . . A 147 GLY H . 18509 1 496 . 1 1 147 147 GLY C C 13 167.909 0.40 . 1 . . . A 147 GLY C . 18509 1 497 . 1 1 147 147 GLY CA C 13 42.674 0.40 . 1 . . . A 147 GLY CA . 18509 1 498 . 1 1 147 147 GLY N N 15 106.461 0.40 . 1 . . . A 147 GLY N . 18509 1 499 . 1 1 148 148 VAL H H 1 8.434 0.02 . 1 . . . A 148 VAL H . 18509 1 500 . 1 1 148 148 VAL C C 13 172.084 0.40 . 1 . . . A 148 VAL C . 18509 1 501 . 1 1 148 148 VAL CA C 13 59.635 0.40 . 1 . . . A 148 VAL CA . 18509 1 502 . 1 1 148 148 VAL N N 15 124.054 0.40 . 1 . . . A 148 VAL N . 18509 1 503 . 1 1 149 149 ILE H H 1 8.613 0.02 . 1 . . . A 149 ILE H . 18509 1 504 . 1 1 149 149 ILE C C 13 171.804 0.40 . 1 . . . A 149 ILE C . 18509 1 505 . 1 1 149 149 ILE CA C 13 59.184 0.40 . 1 . . . A 149 ILE CA . 18509 1 506 . 1 1 149 149 ILE N N 15 126.918 0.40 . 1 . . . A 149 ILE N . 18509 1 507 . 1 1 150 150 GLY H H 1 9.283 0.02 . 1 . . . A 150 GLY H . 18509 1 508 . 1 1 150 150 GLY C C 13 170.188 0.40 . 1 . . . A 150 GLY C . 18509 1 509 . 1 1 150 150 GLY CA C 13 40.120 0.40 . 1 . . . A 150 GLY CA . 18509 1 510 . 1 1 150 150 GLY N N 15 116.493 0.40 . 1 . . . A 150 GLY N . 18509 1 511 . 1 1 151 151 ILE H H 1 8.943 0.02 . 1 . . . A 151 ILE H . 18509 1 512 . 1 1 151 151 ILE C C 13 172.231 0.40 . 1 . . . A 151 ILE C . 18509 1 513 . 1 1 151 151 ILE CA C 13 60.372 0.40 . 1 . . . A 151 ILE CA . 18509 1 514 . 1 1 151 151 ILE N N 15 120.189 0.40 . 1 . . . A 151 ILE N . 18509 1 515 . 1 1 152 152 ALA H H 1 8.170 0.02 . 1 . . . A 152 ALA H . 18509 1 516 . 1 1 152 152 ALA CA C 13 46.772 0.40 . 1 . . . A 152 ALA CA . 18509 1 517 . 1 1 152 152 ALA N N 15 129.719 0.40 . 1 . . . A 152 ALA N . 18509 1 stop_ save_