data_19962 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 19962 _Entry.Title ; Truncated L126Z-sod1 in DPC micelle ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2015-05-18 _Entry.Accession_date 2015-05-18 _Entry.Last_release_date 2015-05-18 _Entry.Original_release_date 2015-05-18 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.77 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 'Liang Zhong' Lim . . . 19962 2 Jianxing Song . . . 19962 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' . 19962 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'DPC micelle' . 19962 'L126Z-Sod1 mutant' . 19962 truncated . 19962 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 19962 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 230 19962 '15N chemical shifts' 117 19962 '1H chemical shifts' 252 19962 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 . . 2015-05-18 . original BMRB . 19962 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2MP3 'BMRB Entry Tracking System' 19962 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 19962 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Mechanism for transforming cytosolic SOD1 into integral membrane proteins of organelles by ALS-causing mutations ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochim. Biophys. Acta' _Citation.Journal_name_full . _Citation.Journal_volume 1848 _Citation.Journal_issue 1 _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 1 _Citation.Page_last 7 _Citation.Year 2015 _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 Liangzhong Lim . . . 19962 1 2 Xiaowen Lee . . . 19962 1 3 Jianxing Song . . . 19962 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 19962 _Assembly.ID 1 _Assembly.Name 'Truncated L126Z-sod1' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 'Truncated L126Z-sod1' 1 $L126Z-sod1 A . yes native no no . . . 19962 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_L126Z-sod1 _Entity.Sf_category entity _Entity.Sf_framecode L126Z-sod1 _Entity.Entry_ID 19962 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name L126Z-sod1 _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 ; ATKAVCVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIE DSVISLSGDHCIIGRTLVVH EKADD ; _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 125 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 13153.691 _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 18509 . Superoxide_dismutase_C6A-C111S_thermostable_mutant . . . . . 100.00 153 98.40 98.40 4.81e-81 . . . . 19962 1 2 no BMRB 18708 . SUPEROXIDE_DISMUTASE_CU-ZN . . . . . 100.00 153 98.40 98.40 4.81e-81 . . . . 19962 1 3 no BMRB 26570 . SOD1 . . . . . 100.00 153 98.40 98.40 4.81e-81 . . . . 19962 1 4 no PDB 1AZV . "Familial Als Mutant G37r Cuznsod (Human)" . . . . . 100.00 153 99.20 99.20 3.36e-82 . . . . 19962 1 5 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 98.40 98.40 4.46e-81 . . . . 19962 1 6 no PDB 1HL4 . "The Structure Of Apo Type Human Cu, Zn Superoxide Dismutase" . . . . . 100.00 154 100.00 100.00 2.64e-83 . . . . 19962 1 7 no PDB 1HL5 . "The Structure Of Holo Type Human Cu, Zn Superoxide Dismutase" . . . . . 100.00 153 100.00 100.00 2.56e-83 . . . . 19962 1 8 no PDB 1L3N . "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" . . . . . 100.00 153 98.40 98.40 4.81e-81 . . . . 19962 1 9 no PDB 1N18 . "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" . . . . . 100.00 154 98.40 98.40 4.46e-81 . . . . 19962 1 10 no PDB 1N19 . "Structure Of The Hsod A4v Mutant" . . . . . 100.00 154 97.60 97.60 2.55e-80 . . . . 19962 1 11 no PDB 1OEZ . "Zn His46arg Mutant Of Human Cu, Zn Superoxide Dismutase" . . . . . 100.00 153 99.20 99.20 1.99e-82 . . . . 19962 1 12 no PDB 1OZT . "Crystal Structure Of Apo-H46r Familial Als Mutant Human Cu, Zn Superoxide Dismutase (Cuznsod) To 2.5a Resolution" . . . . . 100.00 153 99.20 99.20 1.99e-82 . . . . 19962 1 13 no PDB 1OZU . "Crystal Structure Of Familial Als Mutant S134n Of Human Cu, Zn Superoxide Dismutase (Cuznsod) To 1.3a Resolution" . . . . . 100.00 153 99.20 99.20 8.49e-82 . . . . 19962 1 14 no PDB 1P1V . "Crystal Structure Of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125h To 1.4a" . . . . . 99.20 153 99.19 99.19 5.31e-81 . . . . 19962 1 15 no PDB 1PTZ . "Crystal Structure Of The Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43r" . . . . . 100.00 153 97.60 97.60 3.82e-80 . . . . 19962 1 16 no PDB 1PU0 . "Structure Of Human Cu,Zn Superoxide Dismutase" . . . . . 100.00 153 100.00 100.00 2.56e-83 . . . . 19962 1 17 no PDB 1SOS . "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" . . . . . 100.00 154 98.40 98.40 4.97e-81 . . . . 19962 1 18 no PDB 1SPD . "Amyotrophic Lateral Sclerosis And Structural Defects In Cu,Zn Superoxide Dismutase" . . . . . 100.00 154 100.00 100.00 2.64e-83 . . . . 19962 1 19 no PDB 1UXL . "I113t Mutant Of Human Sod1" . . . . . 100.00 153 99.20 99.20 1.23e-82 . . . . 19962 1 20 no PDB 1UXM . "A4v Mutant Of Human Sod1" . . . . . 100.00 153 99.20 99.20 1.48e-82 . . . . 19962 1 21 no PDB 2AF2 . "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" . . . . . 100.00 153 98.40 98.40 4.81e-81 . . . . 19962 1 22 no PDB 2C9S . "1.24 Angstroms Resolution Structure Of Zn-Zn Human Superoxide Dismutase" . . . . . 100.00 153 99.20 99.20 7.86e-82 . . . . 19962 1 23 no PDB 2C9U . "1.24 Angstroms Resolution Structure Of As-Isolated Cu-Zn Human Superoxide Dismutase" . . . . . 100.00 153 100.00 100.00 2.56e-83 . . . . 19962 1 24 no PDB 2C9V . "Atomic Resolution Structure Of Cu-Zn Human Superoxide Dismutase" . . . . . 100.00 153 100.00 100.00 2.56e-83 . . . . 19962 1 25 no PDB 2GBT . "C6aC111A CUZN SUPEROXIDE DISMUTASE" . . . . . 100.00 153 98.40 98.40 4.13e-81 . . . . 19962 1 26 no PDB 2GBU . "C6a/c111a/c57a/c146a Apo Cuzn Superoxide Dismutase" . . . . . 100.00 153 97.60 97.60 6.97e-81 . . . . 19962 1 27 no PDB 2GBV . "C6aC111AC57AC146A HOLO CUZN SUPEROXIDE DISMUTASE" . . . . . 100.00 153 97.60 97.60 6.97e-81 . . . . 19962 1 28 no PDB 2LU5 . "Structure And Chemical Shifts Of Cu(I),Zn(Ii) Superoxide Dismutase By Solid-State Nmr" . . . . . 100.00 153 98.40 98.40 4.81e-81 . . . . 19962 1 29 no PDB 2MP3 . "Truncated L126z-sod1 In Dpc Micelle" . . . . . 100.00 132 100.00 100.00 1.37e-82 . . . . 19962 1 30 no PDB 2NNX . "Crystal Structure Of The H46r, H48q Double Mutant Of Human [cu-Zn] Superoxide Dismutase" . . . . . 100.00 154 98.40 98.40 1.06e-81 . . . . 19962 1 31 no PDB 2V0A . "Atomic Resolution Crystal Structure Of Human Superoxide Dismutase" . . . . . 100.00 153 100.00 100.00 2.56e-83 . . . . 19962 1 32 no PDB 2VR6 . "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.3 A Resolution" . . . . . 100.00 153 99.20 99.20 3.36e-82 . . . . 19962 1 33 no PDB 2VR7 . "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.58 A Resolution" . . . . . 100.00 154 99.20 99.20 3.47e-82 . . . . 19962 1 34 no PDB 2VR8 . "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.36 A Resolution" . . . . . 100.00 154 98.40 98.40 1.10e-80 . . . . 19962 1 35 no PDB 2WKO . "Structure Of Metal Loaded Pathogenic Sod1 Mutant G93a" . . . . . 100.00 154 99.20 99.20 1.33e-82 . . . . 19962 1 36 no PDB 2WYT . "1.0 A Resolution Structure Of L38v Sod1 Mutant" . . . . . 100.00 153 99.20 100.00 8.68e-83 . . . . 19962 1 37 no PDB 2WYZ . "L38v Sod1 Mutant Complexed With Ump" . . . . . 100.00 153 98.40 99.20 2.70e-81 . . . . 19962 1 38 no PDB 2WZ0 . "L38v Sod1 Mutant Complexed With Aniline." . . . . . 100.00 153 99.20 100.00 8.68e-83 . . . . 19962 1 39 no PDB 2WZ5 . "L38v Sod1 Mutant Complexed With L-Methionine" . . . . . 100.00 153 99.20 100.00 8.68e-83 . . . . 19962 1 40 no PDB 2WZ6 . "G93a Sod1 Mutant Complexed With Quinazoline" . . . . . 100.00 153 99.20 99.20 1.29e-82 . . . . 19962 1 41 no PDB 2ZKW . "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group P21" . . . . . 100.00 159 99.20 99.20 3.87e-82 . . . . 19962 1 42 no PDB 2ZKX . "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group I212121" . . . . . 100.00 159 99.20 99.20 3.87e-82 . . . . 19962 1 43 no PDB 2ZKY . "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G93a" . . . . . 100.00 159 99.20 99.20 1.40e-82 . . . . 19962 1 44 no PDB 3CQP . "Human Sod1 G85r Variant, Structure I" . . . . . 100.00 153 99.20 99.20 3.36e-82 . . . . 19962 1 45 no PDB 3CQQ . "Human Sod1 G85r Variant, Structure Ii" . . . . . 100.00 153 98.40 98.40 1.07e-80 . . . . 19962 1 46 no PDB 3ECU . "Crystal Structure Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" . . . . . 100.00 153 100.00 100.00 2.56e-83 . . . . 19962 1 47 no PDB 3ECV . "Crystal Structure Of The Als-Related Pathological Mutant I113t Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" . . . . . 100.00 153 99.20 99.20 1.23e-82 . . . . 19962 1 48 no PDB 3ECW . "Crystal Structure Of The Als-Related Pathological Mutant T54r Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" . . . . . 100.00 153 99.20 99.20 2.42e-82 . . . . 19962 1 49 no PDB 3GQF . "Structural And Biophysical Properties Of The Pathogenic Sod1 Variant H46rH48Q" . . . . . 100.00 153 98.40 98.40 1.02e-81 . . . . 19962 1 50 no PDB 3GZO . "Human Sod1 G93a Variant" . . . . . 100.00 154 99.20 99.20 1.33e-82 . . . . 19962 1 51 no PDB 3GZP . "Human Sod1 G93a Metal-Free Variant" . . . . . 100.00 153 99.20 99.20 1.29e-82 . . . . 19962 1 52 no PDB 3GZQ . "Human Sod1 A4v Metal-Free Variant" . . . . . 100.00 154 99.20 99.20 1.53e-82 . . . . 19962 1 53 no PDB 3H2P . "Human Sod1 D124v Variant" . . . . . 100.00 153 99.20 99.20 4.97e-82 . . . . 19962 1 54 no PDB 3H2Q . "Human Sod1 H80r Variant, P21 Crystal Form" . . . . . 100.00 153 99.20 99.20 1.99e-82 . . . . 19962 1 55 no PDB 3K91 . "Polysulfane Bridge In Cu-Zn Superoxide Dismutase" . . . . . 100.00 153 98.40 98.40 1.02e-81 . . . . 19962 1 56 no PDB 3KH3 . "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P212121 Crystal Form Cont" . . . . . 100.00 153 100.00 100.00 2.56e-83 . . . . 19962 1 57 no PDB 3KH4 . "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P6522 Crystal Form Contai" . . . . . 100.00 153 100.00 100.00 2.56e-83 . . . . 19962 1 58 no PDB 3QQD . "Human Sod1 H80r Variant, P212121 Crystal Form" . . . . . 100.00 154 98.40 98.40 5.73e-81 . . . . 19962 1 59 no PDB 3RE0 . "Crystal Structure Of Human Apo Cu,zn Superoxide Dismutase (sod1) Complexed With Cisplatin" . . . . . 100.00 153 100.00 100.00 2.56e-83 . . . . 19962 1 60 no PDB 3T5W . "2me Modified Human Sod1" . . . . . 100.00 153 99.20 99.20 7.86e-82 . . . . 19962 1 61 no PDB 4A7G . "Structure Of Human I113t Sod1 Mutant Complexed With 4- Methylpiperazin-1-yl)quinazoline In The P21 Space Group." . . . . . 100.00 153 99.20 99.20 1.23e-82 . . . . 19962 1 62 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 99.20 99.20 1.23e-82 . . . . 19962 1 63 no PDB 4A7S . "Structure Of Human I113t Sod1 Mutant Complexed With 5- Fluorouridine In The P21 Space Group" . . . . . 100.00 153 99.20 99.20 1.23e-82 . . . . 19962 1 64 no PDB 4A7T . "Structure Of Human I113t Sod1 Mutant Complexed With Isoproteranol In The P21 Space Group" . . . . . 100.00 153 99.20 99.20 1.23e-82 . . . . 19962 1 65 no PDB 4A7U . "Structure Of Human I113t Sod1 Complexed With Adrenaline In The P21 Space Group." . . . . . 100.00 153 99.20 99.20 1.23e-82 . . . . 19962 1 66 no PDB 4A7V . "Structure Of Human I113t Sod1 Mutant Complexed With Dopamine In The P21 Space Group" . . . . . 100.00 153 99.20 99.20 1.23e-82 . . . . 19962 1 67 no PDB 4B3E . "Structure Of Copper-Zinc Superoxide Dismutase Complexed With Bicarbonate." . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 68 no PDB 4FF9 . "Crystal Structure Of Cysteinylated Wt Sod1" . . . . . 100.00 153 100.00 100.00 2.56e-83 . . . . 19962 1 69 no PDB 4MCM . "Human Sod1 C57s Mutant, As-isolated" . . . . . 100.00 153 99.20 99.20 4.92e-82 . . . . 19962 1 70 no PDB 4MCN . "Human Sod1 C57s Mutant, Metal-free" . . . . . 100.00 153 99.20 99.20 4.92e-82 . . . . 19962 1 71 no PDB 4OH2 . "Crystal Structure Of Cu/zn Superoxide Dismutase I149t" . . . . . 100.00 153 98.40 98.40 4.00e-81 . . . . 19962 1 72 no DBJ BAA14373 . "unnamed protein product [Schizosaccharomyces pombe]" . . . . . 100.00 179 100.00 100.00 4.10e-83 . . . . 19962 1 73 no DBJ BAC20345 . "Cu,Zn-superoxide dismutase [Pan troglodytes]" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 74 no DBJ BAG35052 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 75 no DBJ BAG73767 . "superoxide dismutase 1, soluble [synthetic construct]" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 76 no EMBL CAA26182 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 77 no EMBL CAG29351 . "SOD1 [Homo sapiens]" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 78 no EMBL CAG46542 . "SOD1 [Homo sapiens]" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 79 no GB AAA72747 . "CuZn superoxide dismutase [synthetic construct]" . . . . . 100.00 154 98.40 98.40 4.46e-81 . . . . 19962 1 80 no GB AAA80237 . "HSOD-GlyProGly-A+, partial [synthetic construct]" . . . . . 100.00 171 98.40 98.40 1.70e-80 . . . . 19962 1 81 no GB AAB05661 . "Cu/Zn-superoxide dismutase [Homo sapiens]" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 82 no GB AAB05662 . "Cu/Zn-superoxide dismutase [Homo sapiens]" . . . . . 100.00 154 99.20 99.20 2.37e-82 . . . . 19962 1 83 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 99.20 99.20 1.48e-82 . . . . 19962 1 84 no REF NP_000445 . "superoxide dismutase [Cu-Zn] [Homo sapiens]" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 85 no REF NP_001009025 . "superoxide dismutase [Cu-Zn] [Pan troglodytes]" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 86 no REF XP_003813274 . "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 87 no REF XP_004062735 . "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" . . . . . 100.00 154 99.20 99.20 2.82e-82 . . . . 19962 1 88 no REF XP_004062736 . "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" . . . . . 100.00 154 99.20 99.20 2.82e-82 . . . . 19962 1 89 no SP P00441 . "RecName: Full=Superoxide dismutase [Cu-Zn]; AltName: Full=Superoxide dismutase 1; Short=hSod1" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 1 90 no SP P60052 . "RecName: Full=Superoxide dismutase [Cu-Zn]" . . . . . 100.00 154 100.00 100.00 2.08e-83 . . . . 19962 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 ALA . 19962 1 2 2 THR . 19962 1 3 3 LYS . 19962 1 4 4 ALA . 19962 1 5 5 VAL . 19962 1 6 6 CYS . 19962 1 7 7 VAL . 19962 1 8 8 LEU . 19962 1 9 9 LYS . 19962 1 10 10 GLY . 19962 1 11 11 ASP . 19962 1 12 12 GLY . 19962 1 13 13 PRO . 19962 1 14 14 VAL . 19962 1 15 15 GLN . 19962 1 16 16 GLY . 19962 1 17 17 ILE . 19962 1 18 18 ILE . 19962 1 19 19 ASN . 19962 1 20 20 PHE . 19962 1 21 21 GLU . 19962 1 22 22 GLN . 19962 1 23 23 LYS . 19962 1 24 24 GLU . 19962 1 25 25 SER . 19962 1 26 26 ASN . 19962 1 27 27 GLY . 19962 1 28 28 PRO . 19962 1 29 29 VAL . 19962 1 30 30 LYS . 19962 1 31 31 VAL . 19962 1 32 32 TRP . 19962 1 33 33 GLY . 19962 1 34 34 SER . 19962 1 35 35 ILE . 19962 1 36 36 LYS . 19962 1 37 37 GLY . 19962 1 38 38 LEU . 19962 1 39 39 THR . 19962 1 40 40 GLU . 19962 1 41 41 GLY . 19962 1 42 42 LEU . 19962 1 43 43 HIS . 19962 1 44 44 GLY . 19962 1 45 45 PHE . 19962 1 46 46 HIS . 19962 1 47 47 VAL . 19962 1 48 48 HIS . 19962 1 49 49 GLU . 19962 1 50 50 PHE . 19962 1 51 51 GLY . 19962 1 52 52 ASP . 19962 1 53 53 ASN . 19962 1 54 54 THR . 19962 1 55 55 ALA . 19962 1 56 56 GLY . 19962 1 57 57 CYS . 19962 1 58 58 THR . 19962 1 59 59 SER . 19962 1 60 60 ALA . 19962 1 61 61 GLY . 19962 1 62 62 PRO . 19962 1 63 63 HIS . 19962 1 64 64 PHE . 19962 1 65 65 ASN . 19962 1 66 66 PRO . 19962 1 67 67 LEU . 19962 1 68 68 SER . 19962 1 69 69 ARG . 19962 1 70 70 LYS . 19962 1 71 71 HIS . 19962 1 72 72 GLY . 19962 1 73 73 GLY . 19962 1 74 74 PRO . 19962 1 75 75 LYS . 19962 1 76 76 ASP . 19962 1 77 77 GLU . 19962 1 78 78 GLU . 19962 1 79 79 ARG . 19962 1 80 80 HIS . 19962 1 81 81 VAL . 19962 1 82 82 GLY . 19962 1 83 83 ASP . 19962 1 84 84 LEU . 19962 1 85 85 GLY . 19962 1 86 86 ASN . 19962 1 87 87 VAL . 19962 1 88 88 THR . 19962 1 89 89 ALA . 19962 1 90 90 ASP . 19962 1 91 91 LYS . 19962 1 92 92 ASP . 19962 1 93 93 GLY . 19962 1 94 94 VAL . 19962 1 95 95 ALA . 19962 1 96 96 ASP . 19962 1 97 97 VAL . 19962 1 98 98 SER . 19962 1 99 99 ILE . 19962 1 100 100 GLU . 19962 1 101 101 ASP . 19962 1 102 102 SER . 19962 1 103 103 VAL . 19962 1 104 104 ILE . 19962 1 105 105 SER . 19962 1 106 106 LEU . 19962 1 107 107 SER . 19962 1 108 108 GLY . 19962 1 109 109 ASP . 19962 1 110 110 HIS . 19962 1 111 111 CYS . 19962 1 112 112 ILE . 19962 1 113 113 ILE . 19962 1 114 114 GLY . 19962 1 115 115 ARG . 19962 1 116 116 THR . 19962 1 117 117 LEU . 19962 1 118 118 VAL . 19962 1 119 119 VAL . 19962 1 120 120 HIS . 19962 1 121 121 GLU . 19962 1 122 122 LYS . 19962 1 123 123 ALA . 19962 1 124 124 ASP . 19962 1 125 125 ASP . 19962 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 19962 1 . THR 2 2 19962 1 . LYS 3 3 19962 1 . ALA 4 4 19962 1 . VAL 5 5 19962 1 . CYS 6 6 19962 1 . VAL 7 7 19962 1 . LEU 8 8 19962 1 . LYS 9 9 19962 1 . GLY 10 10 19962 1 . ASP 11 11 19962 1 . GLY 12 12 19962 1 . PRO 13 13 19962 1 . VAL 14 14 19962 1 . GLN 15 15 19962 1 . GLY 16 16 19962 1 . ILE 17 17 19962 1 . ILE 18 18 19962 1 . ASN 19 19 19962 1 . PHE 20 20 19962 1 . GLU 21 21 19962 1 . GLN 22 22 19962 1 . LYS 23 23 19962 1 . GLU 24 24 19962 1 . SER 25 25 19962 1 . ASN 26 26 19962 1 . GLY 27 27 19962 1 . PRO 28 28 19962 1 . VAL 29 29 19962 1 . LYS 30 30 19962 1 . VAL 31 31 19962 1 . TRP 32 32 19962 1 . GLY 33 33 19962 1 . SER 34 34 19962 1 . ILE 35 35 19962 1 . LYS 36 36 19962 1 . GLY 37 37 19962 1 . LEU 38 38 19962 1 . THR 39 39 19962 1 . GLU 40 40 19962 1 . GLY 41 41 19962 1 . LEU 42 42 19962 1 . HIS 43 43 19962 1 . GLY 44 44 19962 1 . PHE 45 45 19962 1 . HIS 46 46 19962 1 . VAL 47 47 19962 1 . HIS 48 48 19962 1 . GLU 49 49 19962 1 . PHE 50 50 19962 1 . GLY 51 51 19962 1 . ASP 52 52 19962 1 . ASN 53 53 19962 1 . THR 54 54 19962 1 . ALA 55 55 19962 1 . GLY 56 56 19962 1 . CYS 57 57 19962 1 . THR 58 58 19962 1 . SER 59 59 19962 1 . ALA 60 60 19962 1 . GLY 61 61 19962 1 . PRO 62 62 19962 1 . HIS 63 63 19962 1 . PHE 64 64 19962 1 . ASN 65 65 19962 1 . PRO 66 66 19962 1 . LEU 67 67 19962 1 . SER 68 68 19962 1 . ARG 69 69 19962 1 . LYS 70 70 19962 1 . HIS 71 71 19962 1 . GLY 72 72 19962 1 . GLY 73 73 19962 1 . PRO 74 74 19962 1 . LYS 75 75 19962 1 . ASP 76 76 19962 1 . GLU 77 77 19962 1 . GLU 78 78 19962 1 . ARG 79 79 19962 1 . HIS 80 80 19962 1 . VAL 81 81 19962 1 . GLY 82 82 19962 1 . ASP 83 83 19962 1 . LEU 84 84 19962 1 . GLY 85 85 19962 1 . ASN 86 86 19962 1 . VAL 87 87 19962 1 . THR 88 88 19962 1 . ALA 89 89 19962 1 . ASP 90 90 19962 1 . LYS 91 91 19962 1 . ASP 92 92 19962 1 . GLY 93 93 19962 1 . VAL 94 94 19962 1 . ALA 95 95 19962 1 . ASP 96 96 19962 1 . VAL 97 97 19962 1 . SER 98 98 19962 1 . ILE 99 99 19962 1 . GLU 100 100 19962 1 . ASP 101 101 19962 1 . SER 102 102 19962 1 . VAL 103 103 19962 1 . ILE 104 104 19962 1 . SER 105 105 19962 1 . LEU 106 106 19962 1 . SER 107 107 19962 1 . GLY 108 108 19962 1 . ASP 109 109 19962 1 . HIS 110 110 19962 1 . CYS 111 111 19962 1 . ILE 112 112 19962 1 . ILE 113 113 19962 1 . GLY 114 114 19962 1 . ARG 115 115 19962 1 . THR 116 116 19962 1 . LEU 117 117 19962 1 . VAL 118 118 19962 1 . VAL 119 119 19962 1 . HIS 120 120 19962 1 . GLU 121 121 19962 1 . LYS 122 122 19962 1 . ALA 123 123 19962 1 . ASP 124 124 19962 1 . ASP 125 125 19962 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 19962 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $L126Z-sod1 . 562 plasmid . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli . . . . . . . . . . . . . 19962 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 19962 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $L126Z-sod1 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21 (DE3)' . . . . . pET28a . . . 19962 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 19962 _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 L126Z-sod1 '[U-100% 13C; U-100% 15N]' . . 1 $L126Z-sod1 . . 400 . . uM . . . . 19962 1 2 'dodecylphosphocholine (DPC)' 'natural abundance' . . . . . . 20 . . mM . . . . 19962 1 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 19962 1 4 D2O '[U-100% 2H]' . . . . . . 10 . . % . . . . 19962 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 19962 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 4 . pH 19962 1 pressure 1 . atm 19962 1 temperature 313 . K 19962 1 stop_ save_ ############################ # Computer software used # ############################ save_Cyana _Software.Sf_category software _Software.Sf_framecode Cyana _Software.Entry_ID 19962 _Software.ID 1 _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' . . 19962 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 19962 1 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 19962 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 19962 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 800 . . . 19962 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 19962 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19962 1 2 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19962 1 3 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19962 1 4 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19962 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 19962 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 19962 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 19962 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 19962 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 19962 _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 '3D CBCA(CO)NH' . . . 19962 1 2 '3D HNCACB' . . . 19962 1 3 '3D 1H-15N NOESY' . . . 19962 1 4 '3D 1H-15N TOCSY' . . . 19962 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 ALA HA H 1 4.361 0.00 . 1 . . . A 1 ALA HA . 19962 1 2 . 1 1 1 1 ALA H H 1 8.510 0.00 . 1 . . . A 1 ALA H1 . 19962 1 3 . 1 1 1 1 ALA CA C 13 52.648 0.00 . 1 . . . A 1 ALA CA . 19962 1 4 . 1 1 1 1 ALA CB C 13 19.448 0.00 . 1 . . . A 1 ALA CB . 19962 1 5 . 1 1 1 1 ALA N N 15 126.197 0.00 . 1 . . . A 1 ALA N . 19962 1 6 . 1 1 2 2 THR H H 1 8.114 0.00 . 1 . . . A 2 THR H . 19962 1 7 . 1 1 2 2 THR HA H 1 4.279 0.00 . 1 . . . A 2 THR HA . 19962 1 8 . 1 1 2 2 THR CA C 13 62.284 0.00 . 1 . . . A 2 THR CA . 19962 1 9 . 1 1 2 2 THR CB C 13 69.857 0.00 . 1 . . . A 2 THR CB . 19962 1 10 . 1 1 2 2 THR N N 15 114.102 0.00 . 1 . . . A 2 THR N . 19962 1 11 . 1 1 3 3 LYS H H 1 8.244 0.00 . 1 . . . A 3 LYS H . 19962 1 12 . 1 1 3 3 LYS HA H 1 4.281 0.00 . 1 . . . A 3 LYS HA . 19962 1 13 . 1 1 3 3 LYS CA C 13 56.818 0.00 . 1 . . . A 3 LYS CA . 19962 1 14 . 1 1 3 3 LYS CB C 13 33.007 0.00 . 1 . . . A 3 LYS CB . 19962 1 15 . 1 1 3 3 LYS N N 15 123.285 0.00 . 1 . . . A 3 LYS N . 19962 1 16 . 1 1 4 4 ALA H H 1 8.043 0.00 . 1 . . . A 4 ALA H . 19962 1 17 . 1 1 4 4 ALA HA H 1 4.282 0.00 . 1 . . . A 4 ALA HA . 19962 1 18 . 1 1 4 4 ALA CA C 13 52.906 0.00 . 1 . . . A 4 ALA CA . 19962 1 19 . 1 1 4 4 ALA CB C 13 19.274 0.00 . 1 . . . A 4 ALA CB . 19962 1 20 . 1 1 4 4 ALA N N 15 123.571 0.00 . 1 . . . A 4 ALA N . 19962 1 21 . 1 1 5 5 VAL H H 1 7.954 0.00 . 1 . . . A 5 VAL H . 19962 1 22 . 1 1 5 5 VAL HA H 1 4.005 0.00 . 1 . . . A 5 VAL HA . 19962 1 23 . 1 1 5 5 VAL CA C 13 63.247 0.00 . 1 . . . A 5 VAL CA . 19962 1 24 . 1 1 5 5 VAL CB C 13 32.563 0.00 . 1 . . . A 5 VAL CB . 19962 1 25 . 1 1 5 5 VAL N N 15 117.713 0.00 . 1 . . . A 5 VAL N . 19962 1 26 . 1 1 6 6 CYS H H 1 8.159 0.00 . 1 . . . A 6 CYS H . 19962 1 27 . 1 1 6 6 CYS HA H 1 4.607 0.00 . 1 . . . A 6 CYS HA . 19962 1 28 . 1 1 6 6 CYS CA C 13 59.415 0.00 . 1 . . . A 6 CYS CA . 19962 1 29 . 1 1 6 6 CYS CB C 13 27.718 0.00 . 1 . . . A 6 CYS CB . 19962 1 30 . 1 1 6 6 CYS N N 15 121.534 0.00 . 1 . . . A 6 CYS N . 19962 1 31 . 1 1 7 7 VAL H H 1 8.051 0.00 . 1 . . . A 7 VAL H . 19962 1 32 . 1 1 7 7 VAL HA H 1 4.264 0.00 . 1 . . . A 7 VAL HA . 19962 1 33 . 1 1 7 7 VAL CA C 13 63.142 0.00 . 1 . . . A 7 VAL CA . 19962 1 34 . 1 1 7 7 VAL CB C 13 32.454 0.00 . 1 . . . A 7 VAL CB . 19962 1 35 . 1 1 7 7 VAL N N 15 121.442 0.00 . 1 . . . A 7 VAL N . 19962 1 36 . 1 1 8 8 LEU H H 1 8.028 0.00 . 1 . . . A 8 LEU H . 19962 1 37 . 1 1 8 8 LEU CA C 13 55.503 0.00 . 1 . . . A 8 LEU CA . 19962 1 38 . 1 1 8 8 LEU CB C 13 42.320 0.00 . 1 . . . A 8 LEU CB . 19962 1 39 . 1 1 8 8 LEU N N 15 122.905 0.00 . 1 . . . A 8 LEU N . 19962 1 40 . 1 1 9 9 LYS H H 1 8.005 0.00 . 1 . . . A 9 LYS H . 19962 1 41 . 1 1 9 9 LYS HA H 1 4.239 0.00 . 1 . . . A 9 LYS HA . 19962 1 42 . 1 1 9 9 LYS CA C 13 56.817 0.00 . 1 . . . A 9 LYS CA . 19962 1 43 . 1 1 9 9 LYS CB C 13 33.156 0.00 . 1 . . . A 9 LYS CB . 19962 1 44 . 1 1 9 9 LYS N N 15 120.185 0.00 . 1 . . . A 9 LYS N . 19962 1 45 . 1 1 10 10 GLY H H 1 8.492 0.00 . 1 . . . A 10 GLY H . 19962 1 46 . 1 1 10 10 GLY HA2 H 1 3.829 0.00 . 1 . . . A 10 GLY HA2 . 19962 1 47 . 1 1 10 10 GLY HA3 H 1 3.829 0.00 . 1 . . . A 10 GLY HA3 . 19962 1 48 . 1 1 10 10 GLY CA C 13 45.474 0.00 . 1 . . . A 10 GLY CA . 19962 1 49 . 1 1 10 10 GLY N N 15 108.482 0.00 . 1 . . . A 10 GLY N . 19962 1 50 . 1 1 11 11 ASP H H 1 8.177 0.00 . 1 . . . A 11 ASP H . 19962 1 51 . 1 1 11 11 ASP HA H 1 4.759 0.00 . 1 . . . A 11 ASP HA . 19962 1 52 . 1 1 11 11 ASP CA C 13 53.202 0.00 . 1 . . . A 11 ASP CA . 19962 1 53 . 1 1 11 11 ASP CB C 13 38.839 0.00 . 1 . . . A 11 ASP CB . 19962 1 54 . 1 1 11 11 ASP N N 15 118.480 0.00 . 1 . . . A 11 ASP N . 19962 1 55 . 1 1 12 12 GLY H H 1 8.397 0.00 . 1 . . . A 12 GLY H . 19962 1 56 . 1 1 12 12 GLY HA2 H 1 4.125 0.00 . 1 . . . A 12 GLY HA2 . 19962 1 57 . 1 1 12 12 GLY HA3 H 1 4.125 0.00 . 1 . . . A 12 GLY HA3 . 19962 1 58 . 1 1 12 12 GLY CA C 13 46.143 0.00 . 1 . . . A 12 GLY CA . 19962 1 59 . 1 1 12 12 GLY N N 15 109.077 0.00 . 1 . . . A 12 GLY N . 19962 1 60 . 1 1 13 13 PRO HA H 1 4.423 0.00 . 1 . . . A 13 PRO HA . 19962 1 61 . 1 1 13 13 PRO CA C 13 64.749 0.00 . 1 . . . A 13 PRO CA . 19962 1 62 . 1 1 13 13 PRO CB C 13 32.213 0.00 . 1 . . . A 13 PRO CB . 19962 1 63 . 1 1 14 14 VAL H H 1 7.931 0.00 . 1 . . . A 14 VAL H . 19962 1 64 . 1 1 14 14 VAL HA H 1 3.763 0.00 . 1 . . . A 14 VAL HA . 19962 1 65 . 1 1 14 14 VAL CA C 13 65.607 0.00 . 1 . . . A 14 VAL CA . 19962 1 66 . 1 1 14 14 VAL CB C 13 31.548 0.00 . 1 . . . A 14 VAL CB . 19962 1 67 . 1 1 14 14 VAL N N 15 116.976 0.00 . 1 . . . A 14 VAL N . 19962 1 68 . 1 1 15 15 GLN H H 1 8.184 0.00 . 1 . . . A 15 GLN H . 19962 1 69 . 1 1 15 15 GLN HA H 1 4.002 0.00 . 1 . . . A 15 GLN HA . 19962 1 70 . 1 1 15 15 GLN CA C 13 58.533 0.00 . 1 . . . A 15 GLN CA . 19962 1 71 . 1 1 15 15 GLN CB C 13 28.387 0.00 . 1 . . . A 15 GLN CB . 19962 1 72 . 1 1 15 15 GLN N N 15 120.074 0.00 . 1 . . . A 15 GLN N . 19962 1 73 . 1 1 16 16 GLY H H 1 8.270 0.00 . 1 . . . A 16 GLY H . 19962 1 74 . 1 1 16 16 GLY HA2 H 1 3.903 0.00 . 1 . . . A 16 GLY HA2 . 19962 1 75 . 1 1 16 16 GLY HA3 H 1 3.903 0.00 . 1 . . . A 16 GLY HA3 . 19962 1 76 . 1 1 16 16 GLY CA C 13 46.945 0.00 . 1 . . . A 16 GLY CA . 19962 1 77 . 1 1 16 16 GLY N N 15 127.937 0.00 . 1 . . . A 16 GLY N . 19962 1 78 . 1 1 17 17 ILE H H 1 7.934 0.00 . 1 . . . A 17 ILE H . 19962 1 79 . 1 1 17 17 ILE HA H 1 3.890 0.00 . 1 . . . A 17 ILE HA . 19962 1 80 . 1 1 17 17 ILE CA C 13 64.622 0.00 . 1 . . . A 17 ILE CA . 19962 1 81 . 1 1 17 17 ILE CB C 13 38.072 0.00 . 1 . . . A 17 ILE CB . 19962 1 82 . 1 1 17 17 ILE N N 15 121.982 0.00 . 1 . . . A 17 ILE N . 19962 1 83 . 1 1 18 18 ILE H H 1 8.007 0.00 . 1 . . . A 18 ILE H . 19962 1 84 . 1 1 18 18 ILE HA H 1 3.763 0.00 . 1 . . . A 18 ILE HA . 19962 1 85 . 1 1 18 18 ILE CA C 13 64.717 0.00 . 1 . . . A 18 ILE CA . 19962 1 86 . 1 1 18 18 ILE CB C 13 37.833 0.00 . 1 . . . A 18 ILE CB . 19962 1 87 . 1 1 18 18 ILE N N 15 120.869 0.00 . 1 . . . A 18 ILE N . 19962 1 88 . 1 1 19 19 ASN H H 1 8.388 0.00 . 1 . . . A 19 ASN H . 19962 1 89 . 1 1 19 19 ASN HA H 1 4.485 0.00 . 1 . . . A 19 ASN HA . 19962 1 90 . 1 1 19 19 ASN CA C 13 55.719 0.00 . 1 . . . A 19 ASN CA . 19962 1 91 . 1 1 19 19 ASN CB C 13 38.405 0.00 . 1 . . . A 19 ASN CB . 19962 1 92 . 1 1 19 19 ASN N N 15 118.523 0.00 . 1 . . . A 19 ASN N . 19962 1 93 . 1 1 20 20 PHE H H 1 8.049 0.00 . 1 . . . A 20 PHE H . 19962 1 94 . 1 1 20 20 PHE HA H 1 4.306 0.00 . 1 . . . A 20 PHE HA . 19962 1 95 . 1 1 20 20 PHE CA C 13 61.018 0.00 . 1 . . . A 20 PHE CA . 19962 1 96 . 1 1 20 20 PHE CB C 13 39.469 0.00 . 1 . . . A 20 PHE CB . 19962 1 97 . 1 1 20 20 PHE N N 15 120.599 0.00 . 1 . . . A 20 PHE N . 19962 1 98 . 1 1 21 21 GLU H H 1 8.415 0.00 . 1 . . . A 21 GLU H . 19962 1 99 . 1 1 21 21 GLU HA H 1 3.865 0.00 . 1 . . . A 21 GLU HA . 19962 1 100 . 1 1 21 21 GLU CA C 13 58.894 0.00 . 1 . . . A 21 GLU CA . 19962 1 101 . 1 1 21 21 GLU CB C 13 27.778 0.00 . 1 . . . A 21 GLU CB . 19962 1 102 . 1 1 21 21 GLU N N 15 118.658 0.00 . 1 . . . A 21 GLU N . 19962 1 103 . 1 1 22 22 GLN H H 1 8.174 0.00 . 1 . . . A 22 GLN H . 19962 1 104 . 1 1 22 22 GLN HA H 1 4.018 0.00 . 1 . . . A 22 GLN HA . 19962 1 105 . 1 1 22 22 GLN CA C 13 58.017 0.00 . 1 . . . A 22 GLN CA . 19962 1 106 . 1 1 22 22 GLN CB C 13 29.013 0.00 . 1 . . . A 22 GLN CB . 19962 1 107 . 1 1 22 22 GLN N N 15 117.512 0.00 . 1 . . . A 22 GLN N . 19962 1 108 . 1 1 23 23 LYS H H 1 7.752 0.00 . 1 . . . A 23 LYS H . 19962 1 109 . 1 1 23 23 LYS HA H 1 4.189 0.00 . 1 . . . A 23 LYS HA . 19962 1 110 . 1 1 23 23 LYS CA C 13 57.620 0.00 . 1 . . . A 23 LYS CA . 19962 1 111 . 1 1 23 23 LYS CB C 13 32.803 0.00 . 1 . . . A 23 LYS CB . 19962 1 112 . 1 1 23 23 LYS N N 15 118.902 0.00 . 1 . . . A 23 LYS N . 19962 1 113 . 1 1 24 24 GLU H H 1 7.816 0.00 . 1 . . . A 24 GLU H . 19962 1 114 . 1 1 24 24 GLU HA H 1 4.263 0.00 . 1 . . . A 24 GLU HA . 19962 1 115 . 1 1 24 24 GLU CA C 13 56.058 0.00 . 1 . . . A 24 GLU CA . 19962 1 116 . 1 1 24 24 GLU CB C 13 28.542 0.00 . 1 . . . A 24 GLU CB . 19962 1 117 . 1 1 24 24 GLU N N 15 117.945 0.00 . 1 . . . A 24 GLU N . 19962 1 118 . 1 1 25 25 SER H H 1 7.923 0.00 . 1 . . . A 25 SER H . 19962 1 119 . 1 1 25 25 SER HA H 1 4.291 0.00 . 1 . . . A 25 SER HA . 19962 1 120 . 1 1 25 25 SER CA C 13 59.316 0.00 . 1 . . . A 25 SER CA . 19962 1 121 . 1 1 25 25 SER CB C 13 63.793 0.00 . 1 . . . A 25 SER CB . 19962 1 122 . 1 1 25 25 SER N N 15 114.711 0.00 . 1 . . . A 25 SER N . 19962 1 123 . 1 1 26 26 ASN H H 1 8.122 0.00 . 1 . . . A 26 ASN H . 19962 1 124 . 1 1 26 26 ASN HA H 1 4.776 0.00 . 1 . . . A 26 ASN HA . 19962 1 125 . 1 1 26 26 ASN CA C 13 53.446 0.00 . 1 . . . A 26 ASN CA . 19962 1 126 . 1 1 26 26 ASN CB C 13 39.173 0.00 . 1 . . . A 26 ASN CB . 19962 1 127 . 1 1 26 26 ASN N N 15 119.305 0.00 . 1 . . . A 26 ASN N . 19962 1 128 . 1 1 27 27 GLY H H 1 8.073 0.00 . 1 . . . A 27 GLY H . 19962 1 129 . 1 1 27 27 GLY HA2 H 1 4.072 0.00 . 1 . . . A 27 GLY HA2 . 19962 1 130 . 1 1 27 27 GLY HA3 H 1 4.072 0.00 . 1 . . . A 27 GLY HA3 . 19962 1 131 . 1 1 27 27 GLY CA C 13 45.810 0.00 . 1 . . . A 27 GLY CA . 19962 1 132 . 1 1 27 27 GLY N N 15 108.196 0.00 . 1 . . . A 27 GLY N . 19962 1 133 . 1 1 28 28 PRO HA H 1 4.260 0.00 . 1 . . . A 28 PRO HA . 19962 1 134 . 1 1 28 28 PRO CA C 13 63.997 0.00 . 1 . . . A 28 PRO CA . 19962 1 135 . 1 1 28 28 PRO CB C 13 32.294 0.00 . 1 . . . A 28 PRO CB . 19962 1 136 . 1 1 29 29 VAL H H 1 7.891 0.00 . 1 . . . A 29 VAL H . 19962 1 137 . 1 1 29 29 VAL HA H 1 3.956 0.00 . 1 . . . A 29 VAL HA . 19962 1 138 . 1 1 29 29 VAL CA C 13 63.818 0.00 . 1 . . . A 29 VAL CA . 19962 1 139 . 1 1 29 29 VAL CB C 13 32.351 0.00 . 1 . . . A 29 VAL CB . 19962 1 140 . 1 1 29 29 VAL N N 15 120.509 0.00 . 1 . . . A 29 VAL N . 19962 1 141 . 1 1 30 30 LYS H H 1 8.276 0.00 . 1 . . . A 30 LYS H . 19962 1 142 . 1 1 30 30 LYS HA H 1 4.317 0.00 . 1 . . . A 30 LYS HA . 19962 1 143 . 1 1 30 30 LYS CA C 13 57.432 0.00 . 1 . . . A 30 LYS CA . 19962 1 144 . 1 1 30 30 LYS CB C 13 32.414 0.00 . 1 . . . A 30 LYS CB . 19962 1 145 . 1 1 30 30 LYS N N 15 123.745 0.00 . 1 . . . A 30 LYS N . 19962 1 146 . 1 1 31 31 VAL H H 1 8.090 0.00 . 1 . . . A 31 VAL H . 19962 1 147 . 1 1 31 31 VAL HA H 1 3.877 0.00 . 1 . . . A 31 VAL HA . 19962 1 148 . 1 1 31 31 VAL CA C 13 64.946 0.00 . 1 . . . A 31 VAL CA . 19962 1 149 . 1 1 31 31 VAL CB C 13 32.163 0.00 . 1 . . . A 31 VAL CB . 19962 1 150 . 1 1 31 31 VAL N N 15 119.301 0.00 . 1 . . . A 31 VAL N . 19962 1 151 . 1 1 32 32 TRP H H 1 8.123 0.00 . 1 . . . A 32 TRP H . 19962 1 152 . 1 1 32 32 TRP HA H 1 4.557 0.00 . 1 . . . A 32 TRP HA . 19962 1 153 . 1 1 32 32 TRP CA C 13 59.291 0.00 . 1 . . . A 32 TRP CA . 19962 1 154 . 1 1 32 32 TRP CB C 13 29.861 0.00 . 1 . . . A 32 TRP CB . 19962 1 155 . 1 1 32 32 TRP N N 15 121.167 0.00 . 1 . . . A 32 TRP N . 19962 1 156 . 1 1 33 33 GLY H H 1 8.230 0.00 . 1 . . . A 33 GLY H . 19962 1 157 . 1 1 33 33 GLY HA2 H 1 3.840 0.00 . 1 . . . A 33 GLY HA2 . 19962 1 158 . 1 1 33 33 GLY HA3 H 1 3.840 0.00 . 1 . . . A 33 GLY HA3 . 19962 1 159 . 1 1 33 33 GLY CA C 13 46.948 0.00 . 1 . . . A 33 GLY CA . 19962 1 160 . 1 1 33 33 GLY N N 15 126.289 0.00 . 1 . . . A 33 GLY N . 19962 1 161 . 1 1 34 34 SER H H 1 7.842 0.00 . 1 . . . A 34 SER H . 19962 1 162 . 1 1 34 34 SER HA H 1 4.420 0.00 . 1 . . . A 34 SER HA . 19962 1 163 . 1 1 34 34 SER CA C 13 60.973 0.00 . 1 . . . A 34 SER CA . 19962 1 164 . 1 1 34 34 SER CB C 13 63.594 0.00 . 1 . . . A 34 SER CB . 19962 1 165 . 1 1 34 34 SER N N 15 116.831 0.00 . 1 . . . A 34 SER N . 19962 1 166 . 1 1 35 35 ILE H H 1 7.962 0.00 . 1 . . . A 35 ILE H . 19962 1 167 . 1 1 35 35 ILE HA H 1 3.848 0.00 . 1 . . . A 35 ILE HA . 19962 1 168 . 1 1 35 35 ILE CA C 13 63.911 0.00 . 1 . . . A 35 ILE CA . 19962 1 169 . 1 1 35 35 ILE CB C 13 37.785 0.00 . 1 . . . A 35 ILE CB . 19962 1 170 . 1 1 35 35 ILE N N 15 120.855 0.00 . 1 . . . A 35 ILE N . 19962 1 171 . 1 1 36 36 LYS CA C 13 59.341 0.00 . 1 . . . A 36 LYS CA . 19962 1 172 . 1 1 36 36 LYS CB C 13 31.799 0.00 . 1 . . . A 36 LYS CB . 19962 1 173 . 1 1 37 37 GLY H H 1 8.067 0.00 . 1 . . . A 37 GLY H . 19962 1 174 . 1 1 37 37 GLY HA2 H 1 3.858 0.00 . 1 . . . A 37 GLY HA2 . 19962 1 175 . 1 1 37 37 GLY HA3 H 1 3.858 0.00 . 1 . . . A 37 GLY HA3 . 19962 1 176 . 1 1 37 37 GLY CA C 13 46.624 0.00 . 1 . . . A 37 GLY CA . 19962 1 177 . 1 1 37 37 GLY N N 15 127.648 0.00 . 1 . . . A 37 GLY N . 19962 1 178 . 1 1 38 38 LEU H H 1 7.838 0.00 . 1 . . . A 38 LEU H . 19962 1 179 . 1 1 38 38 LEU HA H 1 4.192 0.00 . 1 . . . A 38 LEU HA . 19962 1 180 . 1 1 38 38 LEU CA C 13 57.365 0.00 . 1 . . . A 38 LEU CA . 19962 1 181 . 1 1 38 38 LEU CB C 13 42.553 0.00 . 1 . . . A 38 LEU CB . 19962 1 182 . 1 1 38 38 LEU N N 15 121.080 0.00 . 1 . . . A 38 LEU N . 19962 1 183 . 1 1 39 39 THR H H 1 7.887 0.00 . 1 . . . A 39 THR H . 19962 1 184 . 1 1 39 39 THR HA H 1 4.286 0.00 . 1 . . . A 39 THR HA . 19962 1 185 . 1 1 39 39 THR CA C 13 64.464 0.00 . 1 . . . A 39 THR CA . 19962 1 186 . 1 1 39 39 THR CB C 13 69.053 0.00 . 1 . . . A 39 THR CB . 19962 1 187 . 1 1 39 39 THR N N 15 108.219 0.00 . 1 . . . A 39 THR N . 19962 1 188 . 1 1 40 40 GLU H H 1 7.793 0.00 . 1 . . . A 40 GLU H . 19962 1 189 . 1 1 40 40 GLU HA H 1 4.187 0.00 . 1 . . . A 40 GLU HA . 19962 1 190 . 1 1 40 40 GLU CA C 13 57.782 0.00 . 1 . . . A 40 GLU CA . 19962 1 191 . 1 1 40 40 GLU CB C 13 28.112 0.00 . 1 . . . A 40 GLU CB . 19962 1 192 . 1 1 40 40 GLU N N 15 120.404 0.00 . 1 . . . A 40 GLU N . 19962 1 193 . 1 1 41 41 GLY H H 1 8.117 0.00 . 1 . . . A 41 GLY H . 19962 1 194 . 1 1 41 41 GLY HA2 H 1 3.913 0.00 . 1 . . . A 41 GLY HA2 . 19962 1 195 . 1 1 41 41 GLY HA3 H 1 3.913 0.00 . 1 . . . A 41 GLY HA3 . 19962 1 196 . 1 1 41 41 GLY CA C 13 45.809 0.00 . 1 . . . A 41 GLY CA . 19962 1 197 . 1 1 41 41 GLY N N 15 107.101 0.00 . 1 . . . A 41 GLY N . 19962 1 198 . 1 1 42 42 LEU H H 1 7.718 0.00 . 1 . . . A 42 LEU H . 19962 1 199 . 1 1 42 42 LEU HA H 1 4.262 0.00 . 1 . . . A 42 LEU HA . 19962 1 200 . 1 1 42 42 LEU CA C 13 55.684 0.00 . 1 . . . A 42 LEU CA . 19962 1 201 . 1 1 42 42 LEU CB C 13 42.060 0.00 . 1 . . . A 42 LEU CB . 19962 1 202 . 1 1 42 42 LEU N N 15 119.986 0.00 . 1 . . . A 42 LEU N . 19962 1 203 . 1 1 43 43 HIS H H 1 8.142 0.00 . 1 . . . A 43 HIS H . 19962 1 204 . 1 1 43 43 HIS HA H 1 4.574 0.00 . 1 . . . A 43 HIS HA . 19962 1 205 . 1 1 43 43 HIS CA C 13 56.492 0.00 . 1 . . . A 43 HIS CA . 19962 1 206 . 1 1 43 43 HIS CB C 13 28.656 0.00 . 1 . . . A 43 HIS CB . 19962 1 207 . 1 1 43 43 HIS N N 15 116.877 0.00 . 1 . . . A 43 HIS N . 19962 1 208 . 1 1 44 44 GLY H H 1 8.381 0.00 . 1 . . . A 44 GLY H . 19962 1 209 . 1 1 44 44 GLY HA2 H 1 3.850 0.00 . 1 . . . A 44 GLY HA2 . 19962 1 210 . 1 1 44 44 GLY HA3 H 1 3.850 0.00 . 1 . . . A 44 GLY HA3 . 19962 1 211 . 1 1 44 44 GLY CA C 13 45.566 0.00 . 1 . . . A 44 GLY CA . 19962 1 212 . 1 1 44 44 GLY N N 15 108.027 0.00 . 1 . . . A 44 GLY N . 19962 1 213 . 1 1 45 45 PHE H H 1 7.799 0.00 . 1 . . . A 45 PHE H . 19962 1 214 . 1 1 45 45 PHE HA H 1 4.495 0.00 . 1 . . . A 45 PHE HA . 19962 1 215 . 1 1 45 45 PHE CA C 13 58.237 0.00 . 1 . . . A 45 PHE CA . 19962 1 216 . 1 1 45 45 PHE CB C 13 39.916 0.00 . 1 . . . A 45 PHE CB . 19962 1 217 . 1 1 45 45 PHE N N 15 119.781 0.00 . 1 . . . A 45 PHE N . 19962 1 218 . 1 1 46 46 HIS H H 1 8.203 0.00 . 1 . . . A 46 HIS H . 19962 1 219 . 1 1 46 46 HIS HA H 1 4.611 0.00 . 1 . . . A 46 HIS HA . 19962 1 220 . 1 1 46 46 HIS CA C 13 55.147 0.00 . 1 . . . A 46 HIS CA . 19962 1 221 . 1 1 46 46 HIS CB C 13 29.233 0.00 . 1 . . . A 46 HIS CB . 19962 1 222 . 1 1 46 46 HIS N N 15 119.576 0.00 . 1 . . . A 46 HIS N . 19962 1 223 . 1 1 47 47 VAL H H 1 8.178 0.00 . 1 . . . A 47 VAL H . 19962 1 224 . 1 1 47 47 VAL CA C 13 62.976 0.00 . 1 . . . A 47 VAL CA . 19962 1 225 . 1 1 47 47 VAL CB C 13 32.303 0.00 . 1 . . . A 47 VAL CB . 19962 1 226 . 1 1 47 47 VAL N N 15 120.726 0.00 . 1 . . . A 47 VAL N . 19962 1 227 . 1 1 48 48 HIS H H 1 8.439 0.00 . 1 . . . A 48 HIS H . 19962 1 228 . 1 1 48 48 HIS HA H 1 4.652 0.00 . 1 . . . A 48 HIS HA . 19962 1 229 . 1 1 48 48 HIS CA C 13 55.094 0.00 . 1 . . . A 48 HIS CA . 19962 1 230 . 1 1 48 48 HIS CB C 13 29.017 0.00 . 1 . . . A 48 HIS CB . 19962 1 231 . 1 1 48 48 HIS N N 15 118.055 0.00 . 1 . . . A 48 HIS N . 19962 1 232 . 1 1 49 49 GLU H H 1 8.173 0.00 . 1 . . . A 49 GLU H . 19962 1 233 . 1 1 49 49 GLU HA H 1 4.358 0.00 . 1 . . . A 49 GLU HA . 19962 1 234 . 1 1 49 49 GLU CA C 13 56.408 0.00 . 1 . . . A 49 GLU CA . 19962 1 235 . 1 1 49 49 GLU CB C 13 28.978 0.00 . 1 . . . A 49 GLU CB . 19962 1 236 . 1 1 49 49 GLU N N 15 119.231 0.00 . 1 . . . A 49 GLU N . 19962 1 237 . 1 1 50 50 PHE H H 1 8.045 0.00 . 1 . . . A 50 PHE H . 19962 1 238 . 1 1 50 50 PHE HA H 1 4.616 0.00 . 1 . . . A 50 PHE HA . 19962 1 239 . 1 1 50 50 PHE CA C 13 57.761 0.00 . 1 . . . A 50 PHE CA . 19962 1 240 . 1 1 50 50 PHE CB C 13 39.663 0.00 . 1 . . . A 50 PHE CB . 19962 1 241 . 1 1 50 50 PHE N N 15 119.140 0.00 . 1 . . . A 50 PHE N . 19962 1 242 . 1 1 51 51 GLY H H 1 8.242 0.00 . 1 . . . A 51 GLY H . 19962 1 243 . 1 1 51 51 GLY HA2 H 1 3.929 0.00 . 1 . . . A 51 GLY HA2 . 19962 1 244 . 1 1 51 51 GLY HA3 H 1 3.929 0.00 . 1 . . . A 51 GLY HA3 . 19962 1 245 . 1 1 51 51 GLY CA C 13 45.456 0.00 . 1 . . . A 51 GLY CA . 19962 1 246 . 1 1 51 51 GLY N N 15 108.952 0.00 . 1 . . . A 51 GLY N . 19962 1 247 . 1 1 52 52 ASP H H 1 8.251 0.00 . 1 . . . A 52 ASP H . 19962 1 248 . 1 1 52 52 ASP HA H 1 4.682 0.00 . 1 . . . A 52 ASP HA . 19962 1 249 . 1 1 52 52 ASP CA C 13 53.572 0.00 . 1 . . . A 52 ASP CA . 19962 1 250 . 1 1 52 52 ASP CB C 13 38.813 0.00 . 1 . . . A 52 ASP CB . 19962 1 251 . 1 1 52 52 ASP N N 15 119.033 0.00 . 1 . . . A 52 ASP N . 19962 1 252 . 1 1 53 53 ASN H H 1 7.918 0.00 . 1 . . . A 53 ASN H . 19962 1 253 . 1 1 53 53 ASN HA H 1 4.618 0.00 . 1 . . . A 53 ASN HA . 19962 1 254 . 1 1 53 53 ASN CA C 13 52.912 0.00 . 1 . . . A 53 ASN CA . 19962 1 255 . 1 1 53 53 ASN CB C 13 38.973 0.00 . 1 . . . A 53 ASN CB . 19962 1 256 . 1 1 53 53 ASN N N 15 120.466 0.00 . 1 . . . A 53 ASN N . 19962 1 257 . 1 1 54 54 THR H H 1 8.026 0.00 . 1 . . . A 54 THR H . 19962 1 258 . 1 1 54 54 THR HA H 1 4.274 0.00 . 1 . . . A 54 THR HA . 19962 1 259 . 1 1 54 54 THR CA C 13 62.121 0.00 . 1 . . . A 54 THR CA . 19962 1 260 . 1 1 54 54 THR CB C 13 69.696 0.00 . 1 . . . A 54 THR CB . 19962 1 261 . 1 1 54 54 THR N N 15 113.893 0.00 . 1 . . . A 54 THR N . 19962 1 262 . 1 1 55 55 ALA H H 1 8.176 0.00 . 1 . . . A 55 ALA H . 19962 1 263 . 1 1 55 55 ALA HA H 1 4.384 0.00 . 1 . . . A 55 ALA HA . 19962 1 264 . 1 1 55 55 ALA CA C 13 52.655 0.00 . 1 . . . A 55 ALA CA . 19962 1 265 . 1 1 55 55 ALA CB C 13 19.478 0.00 . 1 . . . A 55 ALA CB . 19962 1 266 . 1 1 55 55 ALA N N 15 125.777 0.00 . 1 . . . A 55 ALA N . 19962 1 267 . 1 1 56 56 GLY H H 1 8.048 0.00 . 1 . . . A 56 GLY H . 19962 1 268 . 1 1 56 56 GLY HA2 H 1 4.049 0.00 . 1 . . . A 56 GLY HA2 . 19962 1 269 . 1 1 56 56 GLY HA3 H 1 4.049 0.00 . 1 . . . A 56 GLY HA3 . 19962 1 270 . 1 1 56 56 GLY CA C 13 44.634 0.00 . 1 . . . A 56 GLY CA . 19962 1 271 . 1 1 56 56 GLY N N 15 107.810 0.00 . 1 . . . A 56 GLY N . 19962 1 272 . 1 1 57 57 CYS H H 1 8.122 0.00 . 1 . . . A 57 CYS H . 19962 1 273 . 1 1 57 57 CYS HA H 1 4.574 0.00 . 1 . . . A 57 CYS HA . 19962 1 274 . 1 1 57 57 CYS CA C 13 58.627 0.00 . 1 . . . A 57 CYS CA . 19962 1 275 . 1 1 57 57 CYS CB C 13 28.122 0.00 . 1 . . . A 57 CYS CB . 19962 1 276 . 1 1 57 57 CYS N N 15 118.586 0.00 . 1 . . . A 57 CYS N . 19962 1 277 . 1 1 58 58 THR H H 1 8.201 0.00 . 1 . . . A 58 THR H . 19962 1 278 . 1 1 58 58 THR HA H 1 4.382 0.00 . 1 . . . A 58 THR HA . 19962 1 279 . 1 1 58 58 THR CA C 13 62.006 0.00 . 1 . . . A 58 THR CA . 19962 1 280 . 1 1 58 58 THR CB C 13 69.822 0.00 . 1 . . . A 58 THR CB . 19962 1 281 . 1 1 58 58 THR N N 15 116.035 0.00 . 1 . . . A 58 THR N . 19962 1 282 . 1 1 59 59 SER H H 1 8.173 0.00 . 1 . . . A 59 SER H . 19962 1 283 . 1 1 59 59 SER HA H 1 4.425 0.00 . 1 . . . A 59 SER HA . 19962 1 284 . 1 1 59 59 SER CA C 13 58.376 0.00 . 1 . . . A 59 SER CA . 19962 1 285 . 1 1 59 59 SER CB C 13 63.969 0.00 . 1 . . . A 59 SER CB . 19962 1 286 . 1 1 59 59 SER N N 15 117.834 0.00 . 1 . . . A 59 SER N . 19962 1 287 . 1 1 60 60 ALA H H 1 8.201 0.00 . 1 . . . A 60 ALA H . 19962 1 288 . 1 1 60 60 ALA HA H 1 4.360 0.00 . 1 . . . A 60 ALA HA . 19962 1 289 . 1 1 60 60 ALA CA C 13 52.534 0.00 . 1 . . . A 60 ALA CA . 19962 1 290 . 1 1 60 60 ALA CB C 13 19.583 0.00 . 1 . . . A 60 ALA CB . 19962 1 291 . 1 1 60 60 ALA N N 15 125.777 0.00 . 1 . . . A 60 ALA N . 19962 1 292 . 1 1 61 61 GLY H H 1 7.958 0.00 . 1 . . . A 61 GLY H . 19962 1 293 . 1 1 61 61 GLY HA2 H 1 3.825 0.00 . 1 . . . A 61 GLY HA2 . 19962 1 294 . 1 1 61 61 GLY HA3 H 1 3.825 0.00 . 1 . . . A 61 GLY HA3 . 19962 1 295 . 1 1 61 61 GLY CA C 13 43.747 0.00 . 1 . . . A 61 GLY CA . 19962 1 296 . 1 1 61 61 GLY N N 15 107.119 0.00 . 1 . . . A 61 GLY N . 19962 1 297 . 1 1 62 62 PRO HA H 1 4.452 0.00 . 1 . . . A 62 PRO HA . 19962 1 298 . 1 1 62 62 PRO CA C 13 62.358 0.00 . 1 . . . A 62 PRO CA . 19962 1 299 . 1 1 62 62 PRO CB C 13 32.638 0.00 . 1 . . . A 62 PRO CB . 19962 1 300 . 1 1 63 63 HIS H H 1 8.642 0.00 . 1 . . . A 63 HIS H . 19962 1 301 . 1 1 63 63 HIS HA H 1 4.756 0.00 . 1 . . . A 63 HIS HA . 19962 1 302 . 1 1 63 63 HIS CA C 13 54.997 0.00 . 1 . . . A 63 HIS CA . 19962 1 303 . 1 1 63 63 HIS CB C 13 29.147 0.00 . 1 . . . A 63 HIS CB . 19962 1 304 . 1 1 63 63 HIS N N 15 118.969 0.00 . 1 . . . A 63 HIS N . 19962 1 305 . 1 1 64 64 PHE H H 1 8.318 0.00 . 1 . . . A 64 PHE H . 19962 1 306 . 1 1 64 64 PHE HA H 1 4.597 0.00 . 1 . . . A 64 PHE HA . 19962 1 307 . 1 1 64 64 PHE CA C 13 57.508 0.00 . 1 . . . A 64 PHE CA . 19962 1 308 . 1 1 64 64 PHE CB C 13 40.011 0.00 . 1 . . . A 64 PHE CB . 19962 1 309 . 1 1 64 64 PHE N N 15 121.743 0.00 . 1 . . . A 64 PHE N . 19962 1 310 . 1 1 65 65 ASN H H 1 8.314 0.00 . 1 . . . A 65 ASN H . 19962 1 311 . 1 1 65 65 ASN HA H 1 4.894 0.00 . 1 . . . A 65 ASN HA . 19962 1 312 . 1 1 65 65 ASN CA C 13 50.669 0.00 . 1 . . . A 65 ASN CA . 19962 1 313 . 1 1 65 65 ASN CB C 13 39.177 0.00 . 1 . . . A 65 ASN CB . 19962 1 314 . 1 1 65 65 ASN N N 15 122.466 0.00 . 1 . . . A 65 ASN N . 19962 1 315 . 1 1 66 66 PRO CA C 13 63.748 0.00 . 1 . . . A 66 PRO CA . 19962 1 316 . 1 1 66 66 PRO CB C 13 32.145 0.00 . 1 . . . A 66 PRO CB . 19962 1 317 . 1 1 67 67 LEU H H 1 7.997 0.00 . 1 . . . A 67 LEU H . 19962 1 318 . 1 1 67 67 LEU HA H 1 4.273 0.00 . 1 . . . A 67 LEU HA . 19962 1 319 . 1 1 67 67 LEU CA C 13 55.411 0.00 . 1 . . . A 67 LEU CA . 19962 1 320 . 1 1 67 67 LEU CB C 13 41.729 0.00 . 1 . . . A 67 LEU CB . 19962 1 321 . 1 1 67 67 LEU N N 15 119.364 0.00 . 1 . . . A 67 LEU N . 19962 1 322 . 1 1 68 68 SER H H 1 7.814 0.00 . 1 . . . A 68 SER H . 19962 1 323 . 1 1 68 68 SER HA H 1 4.337 0.00 . 1 . . . A 68 SER HA . 19962 1 324 . 1 1 68 68 SER CA C 13 58.658 0.00 . 1 . . . A 68 SER CA . 19962 1 325 . 1 1 68 68 SER CB C 13 63.815 0.00 . 1 . . . A 68 SER CB . 19962 1 326 . 1 1 68 68 SER N N 15 115.077 0.00 . 1 . . . A 68 SER N . 19962 1 327 . 1 1 69 69 ARG H H 1 8.043 0.00 . 1 . . . A 69 ARG H . 19962 1 328 . 1 1 69 69 ARG HA H 1 4.328 0.00 . 1 . . . A 69 ARG HA . 19962 1 329 . 1 1 69 69 ARG CA C 13 56.056 0.00 . 1 . . . A 69 ARG CA . 19962 1 330 . 1 1 69 69 ARG CB C 13 30.750 0.00 . 1 . . . A 69 ARG CB . 19962 1 331 . 1 1 69 69 ARG N N 15 122.421 0.00 . 1 . . . A 69 ARG N . 19962 1 332 . 1 1 70 70 LYS H H 1 8.086 0.00 . 1 . . . A 70 LYS H . 19962 1 333 . 1 1 70 70 LYS HA H 1 4.238 0.00 . 1 . . . A 70 LYS HA . 19962 1 334 . 1 1 70 70 LYS CA C 13 56.513 0.00 . 1 . . . A 70 LYS CA . 19962 1 335 . 1 1 70 70 LYS CB C 13 33.011 0.00 . 1 . . . A 70 LYS CB . 19962 1 336 . 1 1 70 70 LYS N N 15 121.683 0.00 . 1 . . . A 70 LYS N . 19962 1 337 . 1 1 71 71 HIS H H 1 8.410 0.00 . 1 . . . A 71 HIS H . 19962 1 338 . 1 1 71 71 HIS HA H 1 4.734 0.00 . 1 . . . A 71 HIS HA . 19962 1 339 . 1 1 71 71 HIS CA C 13 55.212 0.00 . 1 . . . A 71 HIS CA . 19962 1 340 . 1 1 71 71 HIS CB C 13 29.332 0.00 . 1 . . . A 71 HIS CB . 19962 1 341 . 1 1 71 71 HIS N N 15 119.321 0.00 . 1 . . . A 71 HIS N . 19962 1 342 . 1 1 72 72 GLY H H 1 8.368 0.00 . 1 . . . A 72 GLY H . 19962 1 343 . 1 1 72 72 GLY HA2 H 1 4.014 0.00 . 1 . . . A 72 GLY HA2 . 19962 1 344 . 1 1 72 72 GLY HA3 H 1 4.014 0.00 . 1 . . . A 72 GLY HA3 . 19962 1 345 . 1 1 72 72 GLY CA C 13 45.117 0.00 . 1 . . . A 72 GLY CA . 19962 1 346 . 1 1 72 72 GLY N N 15 110.453 0.00 . 1 . . . A 72 GLY N . 19962 1 347 . 1 1 73 73 GLY H H 1 8.149 0.00 . 1 . . . A 73 GLY H . 19962 1 348 . 1 1 73 73 GLY HA2 H 1 4.102 0.00 . 1 . . . A 73 GLY HA2 . 19962 1 349 . 1 1 73 73 GLY HA3 H 1 4.102 0.00 . 1 . . . A 73 GLY HA3 . 19962 1 350 . 1 1 73 73 GLY CA C 13 44.617 0.00 . 1 . . . A 73 GLY CA . 19962 1 351 . 1 1 73 73 GLY N N 15 108.744 0.00 . 1 . . . A 73 GLY N . 19962 1 352 . 1 1 74 74 PRO HA H 1 4.404 0.00 . 1 . . . A 74 PRO HA . 19962 1 353 . 1 1 74 74 PRO CA C 13 63.408 0.00 . 1 . . . A 74 PRO CA . 19962 1 354 . 1 1 74 74 PRO CB C 13 32.193 0.00 . 1 . . . A 74 PRO CB . 19962 1 355 . 1 1 75 75 LYS H H 1 8.351 0.00 . 1 . . . A 75 LYS H . 19962 1 356 . 1 1 75 75 LYS HA H 1 4.237 0.00 . 1 . . . A 75 LYS HA . 19962 1 357 . 1 1 75 75 LYS CA C 13 56.722 0.00 . 1 . . . A 75 LYS CA . 19962 1 358 . 1 1 75 75 LYS CB C 13 32.833 0.00 . 1 . . . A 75 LYS CB . 19962 1 359 . 1 1 75 75 LYS N N 15 120.609 0.00 . 1 . . . A 75 LYS N . 19962 1 360 . 1 1 76 76 ASP H H 1 8.223 0.00 . 1 . . . A 76 ASP H . 19962 1 361 . 1 1 76 76 ASP HA H 1 4.624 0.00 . 1 . . . A 76 ASP HA . 19962 1 362 . 1 1 76 76 ASP CA C 13 53.584 0.00 . 1 . . . A 76 ASP CA . 19962 1 363 . 1 1 76 76 ASP CB C 13 39.083 0.00 . 1 . . . A 76 ASP CB . 19962 1 364 . 1 1 76 76 ASP N N 15 119.583 0.00 . 1 . . . A 76 ASP N . 19962 1 365 . 1 1 77 77 GLU H H 1 8.279 0.00 . 1 . . . A 77 GLU H . 19962 1 366 . 1 1 77 77 GLU HA H 1 4.332 0.00 . 1 . . . A 77 GLU HA . 19962 1 367 . 1 1 77 77 GLU CA C 13 56.224 0.00 . 1 . . . A 77 GLU CA . 19962 1 368 . 1 1 77 77 GLU CB C 13 28.978 0.00 . 1 . . . A 77 GLU CB . 19962 1 369 . 1 1 77 77 GLU N N 15 120.900 0.00 . 1 . . . A 77 GLU N . 19962 1 370 . 1 1 78 78 GLU H H 1 8.244 0.00 . 1 . . . A 78 GLU H . 19962 1 371 . 1 1 78 78 GLU HA H 1 4.268 0.00 . 1 . . . A 78 GLU HA . 19962 1 372 . 1 1 78 78 GLU CA C 13 56.613 0.00 . 1 . . . A 78 GLU CA . 19962 1 373 . 1 1 78 78 GLU CB C 13 28.913 0.00 . 1 . . . A 78 GLU CB . 19962 1 374 . 1 1 78 78 GLU N N 15 120.207 0.00 . 1 . . . A 78 GLU N . 19962 1 375 . 1 1 79 79 ARG H H 1 8.129 0.00 . 1 . . . A 79 ARG H . 19962 1 376 . 1 1 79 79 ARG HA H 1 4.260 0.00 . 1 . . . A 79 ARG HA . 19962 1 377 . 1 1 79 79 ARG CA C 13 56.185 0.00 . 1 . . . A 79 ARG CA . 19962 1 378 . 1 1 79 79 ARG CB C 13 30.924 0.00 . 1 . . . A 79 ARG CB . 19962 1 379 . 1 1 79 79 ARG N N 15 121.243 0.00 . 1 . . . A 79 ARG N . 19962 1 380 . 1 1 80 80 HIS H H 1 8.449 0.00 . 1 . . . A 80 HIS H . 19962 1 381 . 1 1 80 80 HIS HA H 1 4.739 0.00 . 1 . . . A 80 HIS HA . 19962 1 382 . 1 1 80 80 HIS CA C 13 55.407 0.00 . 1 . . . A 80 HIS CA . 19962 1 383 . 1 1 80 80 HIS CB C 13 29.241 0.00 . 1 . . . A 80 HIS CB . 19962 1 384 . 1 1 80 80 HIS N N 15 119.446 0.00 . 1 . . . A 80 HIS N . 19962 1 385 . 1 1 81 81 VAL H H 1 8.170 0.00 . 1 . . . A 81 VAL H . 19962 1 386 . 1 1 81 81 VAL HA H 1 3.953 0.00 . 1 . . . A 81 VAL HA . 19962 1 387 . 1 1 81 81 VAL CA C 13 62.886 0.00 . 1 . . . A 81 VAL CA . 19962 1 388 . 1 1 81 81 VAL CB C 13 32.615 0.00 . 1 . . . A 81 VAL CB . 19962 1 389 . 1 1 81 81 VAL N N 15 119.297 0.00 . 1 . . . A 81 VAL N . 19962 1 390 . 1 1 82 82 GLY H H 1 8.372 0.00 . 1 . . . A 82 GLY H . 19962 1 391 . 1 1 82 82 GLY HA2 H 1 4.012 0.00 . 1 . . . A 82 GLY HA2 . 19962 1 392 . 1 1 82 82 GLY HA3 H 1 4.012 0.00 . 1 . . . A 82 GLY HA3 . 19962 1 393 . 1 1 82 82 GLY CA C 13 45.465 0.00 . 1 . . . A 82 GLY CA . 19962 1 394 . 1 1 82 82 GLY N N 15 111.075 0.00 . 1 . . . A 82 GLY N . 19962 1 395 . 1 1 83 83 ASP H H 1 8.230 0.00 . 1 . . . A 83 ASP H . 19962 1 396 . 1 1 83 83 ASP HA H 1 4.679 0.00 . 1 . . . A 83 ASP HA . 19962 1 397 . 1 1 83 83 ASP CA C 13 53.309 0.00 . 1 . . . A 83 ASP CA . 19962 1 398 . 1 1 83 83 ASP CB C 13 38.782 0.00 . 1 . . . A 83 ASP CB . 19962 1 399 . 1 1 83 83 ASP N N 15 118.677 0.00 . 1 . . . A 83 ASP N . 19962 1 400 . 1 1 84 84 LEU H H 1 8.231 0.00 . 1 . . . A 84 LEU H . 19962 1 401 . 1 1 84 84 LEU HA H 1 4.268 0.00 . 1 . . . A 84 LEU HA . 19962 1 402 . 1 1 84 84 LEU CA C 13 55.890 0.00 . 1 . . . A 84 LEU CA . 19962 1 403 . 1 1 84 84 LEU CB C 13 42.175 0.00 . 1 . . . A 84 LEU CB . 19962 1 404 . 1 1 84 84 LEU N N 15 121.711 0.00 . 1 . . . A 84 LEU N . 19962 1 405 . 1 1 85 85 GLY H H 1 8.215 0.00 . 1 . . . A 85 GLY H . 19962 1 406 . 1 1 85 85 GLY HA2 H 1 3.917 0.00 . 1 . . . A 85 GLY HA2 . 19962 1 407 . 1 1 85 85 GLY HA3 H 1 3.917 0.00 . 1 . . . A 85 GLY HA3 . 19962 1 408 . 1 1 85 85 GLY CA C 13 45.796 0.00 . 1 . . . A 85 GLY CA . 19962 1 409 . 1 1 85 85 GLY N N 15 107.521 0.00 . 1 . . . A 85 GLY N . 19962 1 410 . 1 1 86 86 ASN H H 1 8.140 0.00 . 1 . . . A 86 ASN H . 19962 1 411 . 1 1 86 86 ASN HA H 1 4.727 0.00 . 1 . . . A 86 ASN HA . 19962 1 412 . 1 1 86 86 ASN CA C 13 53.368 0.00 . 1 . . . A 86 ASN CA . 19962 1 413 . 1 1 86 86 ASN CB C 13 38.795 0.00 . 1 . . . A 86 ASN CB . 19962 1 414 . 1 1 86 86 ASN N N 15 118.522 0.00 . 1 . . . A 86 ASN N . 19962 1 415 . 1 1 87 87 VAL H H 1 7.977 0.00 . 1 . . . A 87 VAL H . 19962 1 416 . 1 1 87 87 VAL HA H 1 4.110 0.00 . 1 . . . A 87 VAL HA . 19962 1 417 . 1 1 87 87 VAL CA C 13 63.404 0.00 . 1 . . . A 87 VAL CA . 19962 1 418 . 1 1 87 87 VAL CB C 13 32.401 0.00 . 1 . . . A 87 VAL CB . 19962 1 419 . 1 1 87 87 VAL N N 15 119.653 0.00 . 1 . . . A 87 VAL N . 19962 1 420 . 1 1 88 88 THR H H 1 7.996 0.00 . 1 . . . A 88 THR H . 19962 1 421 . 1 1 88 88 THR HA H 1 4.302 0.00 . 1 . . . A 88 THR HA . 19962 1 422 . 1 1 88 88 THR CA C 13 62.737 0.00 . 1 . . . A 88 THR CA . 19962 1 423 . 1 1 88 88 THR CB C 13 69.424 0.00 . 1 . . . A 88 THR CB . 19962 1 424 . 1 1 88 88 THR N N 15 115.427 0.00 . 1 . . . A 88 THR N . 19962 1 425 . 1 1 89 89 ALA H H 1 8.005 0.00 . 1 . . . A 89 ALA H . 19962 1 426 . 1 1 89 89 ALA HA H 1 4.281 0.00 . 1 . . . A 89 ALA HA . 19962 1 427 . 1 1 89 89 ALA CA C 13 52.992 0.00 . 1 . . . A 89 ALA CA . 19962 1 428 . 1 1 89 89 ALA CB C 13 19.151 0.00 . 1 . . . A 89 ALA CB . 19962 1 429 . 1 1 89 89 ALA N N 15 125.054 0.00 . 1 . . . A 89 ALA N . 19962 1 430 . 1 1 90 90 ASP H H 1 8.173 0.00 . 1 . . . A 90 ASP H . 19962 1 431 . 1 1 90 90 ASP HA H 1 4.625 0.00 . 1 . . . A 90 ASP HA . 19962 1 432 . 1 1 90 90 ASP CA C 13 53.478 0.00 . 1 . . . A 90 ASP CA . 19962 1 433 . 1 1 90 90 ASP CB C 13 38.348 0.00 . 1 . . . A 90 ASP CB . 19962 1 434 . 1 1 90 90 ASP N N 15 117.513 0.00 . 1 . . . A 90 ASP N . 19962 1 435 . 1 1 91 91 LYS H H 1 8.147 0.00 . 1 . . . A 91 LYS H . 19962 1 436 . 1 1 91 91 LYS HA H 1 4.226 0.00 . 1 . . . A 91 LYS HA . 19962 1 437 . 1 1 91 91 LYS CA C 13 57.168 0.00 . 1 . . . A 91 LYS CA . 19962 1 438 . 1 1 91 91 LYS CB C 13 32.670 0.00 . 1 . . . A 91 LYS CB . 19962 1 439 . 1 1 91 91 LYS N N 15 120.988 0.00 . 1 . . . A 91 LYS N . 19962 1 440 . 1 1 92 92 ASP H H 1 8.279 0.00 . 1 . . . A 92 ASP H . 19962 1 441 . 1 1 92 92 ASP HA H 1 4.646 0.00 . 1 . . . A 92 ASP HA . 19962 1 442 . 1 1 92 92 ASP CA C 13 53.659 0.00 . 1 . . . A 92 ASP CA . 19962 1 443 . 1 1 92 92 ASP CB C 13 38.425 0.00 . 1 . . . A 92 ASP CB . 19962 1 444 . 1 1 92 92 ASP N N 15 118.400 0.00 . 1 . . . A 92 ASP N . 19962 1 445 . 1 1 93 93 GLY H H 1 8.133 0.00 . 1 . . . A 93 GLY H . 19962 1 446 . 1 1 93 93 GLY HA2 H 1 3.946 0.00 . 1 . . . A 93 GLY HA2 . 19962 1 447 . 1 1 93 93 GLY HA3 H 1 3.946 0.00 . 1 . . . A 93 GLY HA3 . 19962 1 448 . 1 1 93 93 GLY CA C 13 45.880 0.00 . 1 . . . A 93 GLY CA . 19962 1 449 . 1 1 93 93 GLY N N 15 107.991 0.00 . 1 . . . A 93 GLY N . 19962 1 450 . 1 1 94 94 VAL H H 1 7.840 0.00 . 1 . . . A 94 VAL H . 19962 1 451 . 1 1 94 94 VAL HA H 1 4.061 0.00 . 1 . . . A 94 VAL HA . 19962 1 452 . 1 1 94 94 VAL CA C 13 62.865 0.00 . 1 . . . A 94 VAL CA . 19962 1 453 . 1 1 94 94 VAL CB C 13 32.529 0.00 . 1 . . . A 94 VAL CB . 19962 1 454 . 1 1 94 94 VAL N N 15 118.556 0.00 . 1 . . . A 94 VAL N . 19962 1 455 . 1 1 95 95 ALA H H 1 8.190 0.00 . 1 . . . A 95 ALA H . 19962 1 456 . 1 1 95 95 ALA HA H 1 4.308 0.00 . 1 . . . A 95 ALA HA . 19962 1 457 . 1 1 95 95 ALA CA C 13 52.890 0.00 . 1 . . . A 95 ALA CA . 19962 1 458 . 1 1 95 95 ALA CB C 13 19.276 0.00 . 1 . . . A 95 ALA CB . 19962 1 459 . 1 1 95 95 ALA N N 15 125.410 0.00 . 1 . . . A 95 ALA N . 19962 1 460 . 1 1 96 96 ASP H H 1 8.253 0.00 . 1 . . . A 96 ASP H . 19962 1 461 . 1 1 96 96 ASP HA H 1 4.614 0.00 . 1 . . . A 96 ASP HA . 19962 1 462 . 1 1 96 96 ASP CA C 13 54.145 0.00 . 1 . . . A 96 ASP CA . 19962 1 463 . 1 1 96 96 ASP CB C 13 38.193 0.00 . 1 . . . A 96 ASP CB . 19962 1 464 . 1 1 96 96 ASP N N 15 117.528 0.00 . 1 . . . A 96 ASP N . 19962 1 465 . 1 1 97 97 VAL H H 1 7.935 0.00 . 1 . . . A 97 VAL H . 19962 1 466 . 1 1 97 97 VAL HA H 1 4.048 0.00 . 1 . . . A 97 VAL HA . 19962 1 467 . 1 1 97 97 VAL CA C 13 63.455 0.00 . 1 . . . A 97 VAL CA . 19962 1 468 . 1 1 97 97 VAL CB C 13 32.564 0.00 . 1 . . . A 97 VAL CB . 19962 1 469 . 1 1 97 97 VAL N N 15 119.362 0.00 . 1 . . . A 97 VAL N . 19962 1 470 . 1 1 98 98 SER H H 1 8.103 0.00 . 1 . . . A 98 SER H . 19962 1 471 . 1 1 98 98 SER HA H 1 4.530 0.00 . 1 . . . A 98 SER HA . 19962 1 472 . 1 1 98 98 SER CA C 13 59.185 0.00 . 1 . . . A 98 SER CA . 19962 1 473 . 1 1 98 98 SER CB C 13 63.579 0.00 . 1 . . . A 98 SER CB . 19962 1 474 . 1 1 98 98 SER N N 15 117.866 0.00 . 1 . . . A 98 SER N . 19962 1 475 . 1 1 99 99 ILE H H 1 8.395 0.00 . 1 . . . A 99 ILE H . 19962 1 476 . 1 1 99 99 ILE HA H 1 3.917 0.00 . 1 . . . A 99 ILE HA . 19962 1 477 . 1 1 99 99 ILE CA C 13 64.000 0.00 . 1 . . . A 99 ILE CA . 19962 1 478 . 1 1 99 99 ILE CB C 13 38.001 0.00 . 1 . . . A 99 ILE CB . 19962 1 479 . 1 1 99 99 ILE N N 15 123.797 0.00 . 1 . . . A 99 ILE N . 19962 1 480 . 1 1 100 100 GLU H H 1 8.433 0.00 . 1 . . . A 100 GLU H . 19962 1 481 . 1 1 100 100 GLU HA H 1 4.251 0.00 . 1 . . . A 100 GLU HA . 19962 1 482 . 1 1 100 100 GLU CA C 13 59.247 0.00 . 1 . . . A 100 GLU CA . 19962 1 483 . 1 1 100 100 GLU CB C 13 28.160 0.00 . 1 . . . A 100 GLU CB . 19962 1 484 . 1 1 100 100 GLU N N 15 120.053 0.00 . 1 . . . A 100 GLU N . 19962 1 485 . 1 1 101 101 ASP H H 1 8.339 0.00 . 1 . . . A 101 ASP H . 19962 1 486 . 1 1 101 101 ASP HA H 1 4.497 0.00 . 1 . . . A 101 ASP HA . 19962 1 487 . 1 1 101 101 ASP CA C 13 55.395 0.00 . 1 . . . A 101 ASP CA . 19962 1 488 . 1 1 101 101 ASP CB C 13 37.691 0.00 . 1 . . . A 101 ASP CB . 19962 1 489 . 1 1 101 101 ASP N N 15 116.680 0.00 . 1 . . . A 101 ASP N . 19962 1 490 . 1 1 102 102 SER H H 1 7.999 0.00 . 1 . . . A 102 SER H . 19962 1 491 . 1 1 102 102 SER HA H 1 4.335 0.00 . 1 . . . A 102 SER HA . 19962 1 492 . 1 1 102 102 SER CA C 13 61.843 0.00 . 1 . . . A 102 SER CA . 19962 1 493 . 1 1 102 102 SER CB C 13 63.396 0.00 . 1 . . . A 102 SER CB . 19962 1 494 . 1 1 102 102 SER N N 15 116.686 0.00 . 1 . . . A 102 SER N . 19962 1 495 . 1 1 103 103 VAL H H 1 8.004 0.00 . 1 . . . A 103 VAL H . 19962 1 496 . 1 1 103 103 VAL HA H 1 3.816 0.00 . 1 . . . A 103 VAL HA . 19962 1 497 . 1 1 103 103 VAL CA C 13 65.719 0.00 . 1 . . . A 103 VAL CA . 19962 1 498 . 1 1 103 103 VAL CB C 13 31.920 0.00 . 1 . . . A 103 VAL CB . 19962 1 499 . 1 1 103 103 VAL N N 15 120.346 0.00 . 1 . . . A 103 VAL N . 19962 1 500 . 1 1 104 104 ILE H H 1 8.009 0.00 . 1 . . . A 104 ILE H . 19962 1 501 . 1 1 104 104 ILE HA H 1 3.890 0.00 . 1 . . . A 104 ILE HA . 19962 1 502 . 1 1 104 104 ILE CA C 13 63.862 0.00 . 1 . . . A 104 ILE CA . 19962 1 503 . 1 1 104 104 ILE CB C 13 38.048 0.00 . 1 . . . A 104 ILE CB . 19962 1 504 . 1 1 104 104 ILE N N 15 119.732 0.00 . 1 . . . A 104 ILE N . 19962 1 505 . 1 1 105 105 SER H H 1 7.995 0.00 . 1 . . . A 105 SER H . 19962 1 506 . 1 1 105 105 SER HA H 1 4.501 0.00 . 1 . . . A 105 SER HA . 19962 1 507 . 1 1 105 105 SER CA C 13 60.533 0.00 . 1 . . . A 105 SER CA . 19962 1 508 . 1 1 105 105 SER CB C 13 63.459 0.00 . 1 . . . A 105 SER CB . 19962 1 509 . 1 1 105 105 SER N N 15 116.660 0.00 . 1 . . . A 105 SER N . 19962 1 510 . 1 1 106 106 LEU H H 1 8.053 0.00 . 1 . . . A 106 LEU H . 19962 1 511 . 1 1 106 106 LEU CA C 13 56.562 0.00 . 1 . . . A 106 LEU CA . 19962 1 512 . 1 1 106 106 LEU CB C 13 42.454 0.00 . 1 . . . A 106 LEU CB . 19962 1 513 . 1 1 106 106 LEU N N 15 122.130 0.00 . 1 . . . A 106 LEU N . 19962 1 514 . 1 1 107 107 SER H H 1 7.996 0.00 . 1 . . . A 107 SER H . 19962 1 515 . 1 1 107 107 SER HA H 1 4.269 0.00 . 1 . . . A 107 SER HA . 19962 1 516 . 1 1 107 107 SER CA C 13 60.287 0.00 . 1 . . . A 107 SER CA . 19962 1 517 . 1 1 107 107 SER CB C 13 63.893 0.00 . 1 . . . A 107 SER CB . 19962 1 518 . 1 1 107 107 SER N N 15 113.088 0.00 . 1 . . . A 107 SER N . 19962 1 519 . 1 1 108 108 GLY H H 1 8.066 0.00 . 1 . . . A 108 GLY H . 19962 1 520 . 1 1 108 108 GLY HA2 H 1 3.970 0.00 . 1 . . . A 108 GLY HA2 . 19962 1 521 . 1 1 108 108 GLY HA3 H 1 3.970 0.00 . 1 . . . A 108 GLY HA3 . 19962 1 522 . 1 1 108 108 GLY CA C 13 45.944 0.00 . 1 . . . A 108 GLY CA . 19962 1 523 . 1 1 108 108 GLY N N 15 109.156 0.00 . 1 . . . A 108 GLY N . 19962 1 524 . 1 1 109 109 ASP H H 1 8.119 0.00 . 1 . . . A 109 ASP H . 19962 1 525 . 1 1 109 109 ASP CA C 13 53.269 0.00 . 1 . . . A 109 ASP CA . 19962 1 526 . 1 1 109 109 ASP CB C 13 38.170 0.00 . 1 . . . A 109 ASP CB . 19962 1 527 . 1 1 109 109 ASP N N 15 118.500 0.00 . 1 . . . A 109 ASP N . 19962 1 528 . 1 1 110 110 HIS H H 1 8.302 0.00 . 1 . . . A 110 HIS H . 19962 1 529 . 1 1 110 110 HIS HA H 1 4.654 0.00 . 1 . . . A 110 HIS HA . 19962 1 530 . 1 1 110 110 HIS CA C 13 56.094 0.00 . 1 . . . A 110 HIS CA . 19962 1 531 . 1 1 110 110 HIS CB C 13 28.660 0.00 . 1 . . . A 110 HIS CB . 19962 1 532 . 1 1 110 110 HIS N N 15 117.415 0.00 . 1 . . . A 110 HIS N . 19962 1 533 . 1 1 111 111 CYS H H 1 8.293 0.00 . 1 . . . A 111 CYS H . 19962 1 534 . 1 1 111 111 CYS HA H 1 4.502 0.00 . 1 . . . A 111 CYS HA . 19962 1 535 . 1 1 111 111 CYS CA C 13 59.399 0.00 . 1 . . . A 111 CYS CA . 19962 1 536 . 1 1 111 111 CYS CB C 13 27.674 0.00 . 1 . . . A 111 CYS CB . 19962 1 537 . 1 1 111 111 CYS N N 15 118.550 0.00 . 1 . . . A 111 CYS N . 19962 1 538 . 1 1 112 112 ILE H H 1 8.265 0.00 . 1 . . . A 112 ILE H . 19962 1 539 . 1 1 112 112 ILE HA H 1 4.115 0.00 . 1 . . . A 112 ILE HA . 19962 1 540 . 1 1 112 112 ILE CA C 13 62.697 0.00 . 1 . . . A 112 ILE CA . 19962 1 541 . 1 1 112 112 ILE CB C 13 38.458 0.00 . 1 . . . A 112 ILE CB . 19962 1 542 . 1 1 112 112 ILE N N 15 121.950 0.00 . 1 . . . A 112 ILE N . 19962 1 543 . 1 1 113 113 ILE H H 1 8.031 0.00 . 1 . . . A 113 ILE H . 19962 1 544 . 1 1 113 113 ILE HA H 1 4.027 0.00 . 1 . . . A 113 ILE HA . 19962 1 545 . 1 1 113 113 ILE CA C 13 62.669 0.00 . 1 . . . A 113 ILE CA . 19962 1 546 . 1 1 113 113 ILE CB C 13 38.270 0.00 . 1 . . . A 113 ILE CB . 19962 1 547 . 1 1 113 113 ILE N N 15 121.561 0.00 . 1 . . . A 113 ILE N . 19962 1 548 . 1 1 114 114 GLY H H 1 8.265 0.00 . 1 . . . A 114 GLY H . 19962 1 549 . 1 1 114 114 GLY HA2 H 1 3.897 0.00 . 1 . . . A 114 GLY HA2 . 19962 1 550 . 1 1 114 114 GLY HA3 H 1 3.897 0.00 . 1 . . . A 114 GLY HA3 . 19962 1 551 . 1 1 114 114 GLY CA C 13 46.498 0.00 . 1 . . . A 114 GLY CA . 19962 1 552 . 1 1 114 114 GLY N N 15 109.652 0.00 . 1 . . . A 114 GLY N . 19962 1 553 . 1 1 115 115 ARG H H 1 8.073 0.00 . 1 . . . A 115 ARG H . 19962 1 554 . 1 1 115 115 ARG HA H 1 4.215 0.00 . 1 . . . A 115 ARG HA . 19962 1 555 . 1 1 115 115 ARG CA C 13 57.749 0.00 . 1 . . . A 115 ARG CA . 19962 1 556 . 1 1 115 115 ARG CB C 13 30.641 0.00 . 1 . . . A 115 ARG CB . 19962 1 557 . 1 1 115 115 ARG N N 15 119.514 0.00 . 1 . . . A 115 ARG N . 19962 1 558 . 1 1 116 116 THR H H 1 7.965 0.00 . 1 . . . A 116 THR H . 19962 1 559 . 1 1 116 116 THR HA H 1 4.182 0.00 . 1 . . . A 116 THR HA . 19962 1 560 . 1 1 116 116 THR CA C 13 64.288 0.00 . 1 . . . A 116 THR CA . 19962 1 561 . 1 1 116 116 THR CB C 13 69.277 0.00 . 1 . . . A 116 THR CB . 19962 1 562 . 1 1 116 116 THR N N 15 113.665 0.00 . 1 . . . A 116 THR N . 19962 1 563 . 1 1 117 117 LEU H H 1 8.009 0.00 . 1 . . . A 117 LEU H . 19962 1 564 . 1 1 117 117 LEU HA H 1 4.256 0.00 . 1 . . . A 117 LEU HA . 19962 1 565 . 1 1 117 117 LEU CA C 13 56.750 0.00 . 1 . . . A 117 LEU CA . 19962 1 566 . 1 1 117 117 LEU CB C 13 42.374 0.00 . 1 . . . A 117 LEU CB . 19962 1 567 . 1 1 117 117 LEU N N 15 122.716 0.00 . 1 . . . A 117 LEU N . 19962 1 568 . 1 1 118 118 VAL H H 1 7.805 0.00 . 1 . . . A 118 VAL H . 19962 1 569 . 1 1 118 118 VAL HA H 1 3.923 0.00 . 1 . . . A 118 VAL HA . 19962 1 570 . 1 1 118 118 VAL CA C 13 64.159 0.00 . 1 . . . A 118 VAL CA . 19962 1 571 . 1 1 118 118 VAL CB C 13 32.290 0.00 . 1 . . . A 118 VAL CB . 19962 1 572 . 1 1 118 118 VAL N N 15 118.610 0.00 . 1 . . . A 118 VAL N . 19962 1 573 . 1 1 119 119 VAL H H 1 7.971 0.00 . 1 . . . A 119 VAL H . 19962 1 574 . 1 1 119 119 VAL HA H 1 3.952 0.00 . 1 . . . A 119 VAL HA . 19962 1 575 . 1 1 119 119 VAL CA C 13 64.233 0.00 . 1 . . . A 119 VAL CA . 19962 1 576 . 1 1 119 119 VAL CB C 13 32.197 0.00 . 1 . . . A 119 VAL CB . 19962 1 577 . 1 1 119 119 VAL N N 15 118.576 0.00 . 1 . . . A 119 VAL N . 19962 1 578 . 1 1 120 120 HIS H H 1 8.444 0.00 . 1 . . . A 120 HIS H . 19962 1 579 . 1 1 120 120 HIS HA H 1 4.618 0.00 . 1 . . . A 120 HIS HA . 19962 1 580 . 1 1 120 120 HIS CA C 13 55.955 0.00 . 1 . . . A 120 HIS CA . 19962 1 581 . 1 1 120 120 HIS CB C 13 28.903 0.00 . 1 . . . A 120 HIS CB . 19962 1 582 . 1 1 120 120 HIS N N 15 119.988 0.00 . 1 . . . A 120 HIS N . 19962 1 583 . 1 1 121 121 GLU H H 1 8.188 0.00 . 1 . . . A 121 GLU H . 19962 1 584 . 1 1 121 121 GLU HA H 1 4.336 0.00 . 1 . . . A 121 GLU HA . 19962 1 585 . 1 1 121 121 GLU CA C 13 56.096 0.00 . 1 . . . A 121 GLU CA . 19962 1 586 . 1 1 121 121 GLU CB C 13 28.975 0.00 . 1 . . . A 121 GLU CB . 19962 1 587 . 1 1 121 121 GLU N N 15 120.536 0.00 . 1 . . . A 121 GLU N . 19962 1 588 . 1 1 122 122 LYS CA C 13 56.787 0.00 . 1 . . . A 122 LYS CA . 19962 1 589 . 1 1 122 122 LYS CB C 13 33.068 0.00 . 1 . . . A 122 LYS CB . 19962 1 590 . 1 1 123 123 ALA H H 1 8.228 0.00 . 1 . . . A 123 ALA H . 19962 1 591 . 1 1 123 123 ALA HA H 1 4.265 0.00 . 1 . . . A 123 ALA HA . 19962 1 592 . 1 1 123 123 ALA CA C 13 53.030 0.00 . 1 . . . A 123 ALA CA . 19962 1 593 . 1 1 123 123 ALA CB C 13 19.238 0.00 . 1 . . . A 123 ALA CB . 19962 1 594 . 1 1 123 123 ALA N N 15 124.596 0.00 . 1 . . . A 123 ALA N . 19962 1 595 . 1 1 124 124 ASP H H 1 8.169 0.00 . 1 . . . A 124 ASP H . 19962 1 596 . 1 1 124 124 ASP HA H 1 4.702 0.00 . 1 . . . A 124 ASP HA . 19962 1 597 . 1 1 124 124 ASP CA C 13 53.276 0.00 . 1 . . . A 124 ASP CA . 19962 1 598 . 1 1 124 124 ASP CB C 13 38.415 0.00 . 1 . . . A 124 ASP CB . 19962 1 599 . 1 1 124 124 ASP N N 15 117.288 0.00 . 1 . . . A 124 ASP N . 19962 1 stop_ save_