data_18708 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18708 _Entry.Title ; Structure of Co-substituted microcrystalline SOD using PCS and PRE restraints by solid-state NMR ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-09-11 _Entry.Accession_date 2012-09-11 _Entry.Last_release_date 2013-02-12 _Entry.Original_release_date 2013-02-12 _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 . _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 M. Knight . J. . 18708 2 I. Felli . C. . 18708 3 R. Pierattelii . . . 18708 4 I. Bertini . . . 18708 5 L. Emsley . . . 18708 6 T. Herrmann . . . 18708 7 Guido Pintacuda . . . 18708 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' . 18708 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . pintacudaGroup . 18708 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID OXIDOREDUCTASE . 18708 'SOD metalloenzyme solid-state NMR PCS pseudocontact paramagnetic' . 18708 'SOD METALLOENZYME SOLID-STATE NMR PCS PSEUDO PARAMAGNETIC' . 18708 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18708 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 245 18708 '15N chemical shifts' 136 18708 '1H chemical shifts' 136 18708 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 . . 2013-02-12 2012-09-11 original author . 18708 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18708 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22916960 _Citation.Full_citation . _Citation.Title 'Rapid measurement of pseudocontact shifts in metalloproteins by proton-detected solid-state NMR spectroscopy.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Am. Chem. Soc.' _Citation.Journal_name_full 'Journal of the American Chemical Society' _Citation.Journal_volume 134 _Citation.Journal_issue 36 _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 14730 _Citation.Page_last 14733 _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. . 18708 1 2 Isabella Felli . C. . 18708 1 3 Roberta Pierattelli . . . 18708 1 4 Ivano Bertini . . . 18708 1 5 Lyndon Emsley . . . 18708 1 6 Torsten Herrmann . . . 18708 1 7 Guido Pintacuda . . . 18708 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18708 _Assembly.ID 1 _Assembly.Name 'Structure of Co-substituted microcrystalline SOD using PCS and PRE restraints by solid-state NMR' _Assembly.BMRB_code . _Assembly.Number_of_components 3 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 2 _Assembly.Non_standard_bonds yes _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass 15869.7937 _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 [CU-ZN]' 1 $SUPEROXIDE_DISMUTASE_CU-ZN A . yes native no no . . . 18708 1 2 'COBALT (II) ION' 2 $entity_CO B . no native no no . . . 18708 1 3 'COPPER (II) ION' 3 $entity_CU C . no native no no . . . 18708 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 57 57 SG . 1 . 1 CYS 146 146 SG . . . . . . . . . . 18708 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_SUPEROXIDE_DISMUTASE_CU-ZN _Entity.Sf_category entity _Entity.Sf_framecode SUPEROXIDE_DISMUTASE_CU-ZN _Entity.Entry_ID 18708 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name SUPEROXIDE_DISMUTASE_CU-ZN _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 . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation C6A,C111S _Entity.EC_number 1.15.1.1 _Entity.Calc_isoelectric_point . _Entity.Formula_weight 15747.3145 _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 yes UNP SODC_HUMAN . P00441 . . . . . . . . . . . . . . 18708 1 2 no BMRB 15711 . SOD1 . . . . . 100.00 153 98.04 98.69 2.09e-100 . . . . 18708 1 3 no BMRB 15712 . SOD1 . . . . . 100.00 153 97.39 98.04 1.37e-99 . . . . 18708 1 4 no BMRB 15713 . SOD1 . . . . . 100.00 153 97.39 98.04 2.41e-99 . . . . 18708 1 5 no BMRB 15714 . SOD1 . . . . . 100.00 153 97.39 98.04 2.49e-99 . . . . 18708 1 6 no BMRB 18509 . Superoxide_dismutase_C6A-C111S_thermostable_mutant . . . . . 100.00 153 100.00 100.00 4.22e-103 . . . . 18708 1 7 no BMRB 18968 . SOD1 . . . . . 100.00 153 98.04 98.69 2.09e-100 . . . . 18708 1 8 no BMRB 19962 . L126Z-sod1 . . . . . 81.70 125 98.40 98.40 5.89e-81 . . . . 18708 1 9 no BMRB 26570 . SOD1 . . . . . 100.00 153 100.00 100.00 4.22e-103 . . . . 18708 1 10 no BMRB 4202 . "Superoxide Dismutase" . . . . . 100.00 153 98.04 98.69 2.46e-100 . . . . 18708 1 11 no PDB 1AZV . "Familial Als Mutant G37r Cuznsod (Human)" . . . . . 100.00 153 98.04 98.04 1.35e-100 . . . . 18708 1 12 no PDB 1BA9 . "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" . . . . . 99.35 153 98.03 98.68 1.14e-99 . . . . 18708 1 13 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 . . . . 18708 1 14 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 . . . . 18708 1 15 no PDB 1HL4 . "The Structure Of Apo Type Human Cu, Zn Superoxide Dismutase" . . . . . 100.00 154 98.69 98.69 1.26e-101 . . . . 18708 1 16 no PDB 1HL5 . "The Structure Of Holo Type Human Cu, Zn Superoxide Dismutase" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18708 1 17 no PDB 1KMG . "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" . . . . . 100.00 153 98.04 98.69 2.46e-100 . . . . 18708 1 18 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 . . . . 18708 1 19 no PDB 1MFM . "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" . . . . . 100.00 153 98.04 98.69 2.46e-100 . . . . 18708 1 20 no PDB 1N18 . "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" . . . . . 100.00 154 100.00 100.00 3.36e-103 . . . . 18708 1 21 no PDB 1N19 . "Structure Of The Hsod A4v Mutant" . . . . . 100.00 154 99.35 99.35 1.40e-102 . . . . 18708 1 22 no PDB 1OEZ . "Zn His46arg Mutant Of Human Cu, Zn Superoxide Dismutase" . . . . . 100.00 153 98.04 98.04 1.11e-100 . . . . 18708 1 23 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 . . . . 18708 1 24 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 . . . . 18708 1 25 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 . . . . 18708 1 26 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 . . . . 18708 1 27 no PDB 1PU0 . "Structure Of Human Cu,Zn Superoxide Dismutase" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18708 1 28 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 . . . . 18708 1 29 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 . . . . 18708 1 30 no PDB 1SPD . "Amyotrophic Lateral Sclerosis And Structural Defects In Cu,Zn Superoxide Dismutase" . . . . . 100.00 154 98.69 98.69 1.26e-101 . . . . 18708 1 31 no PDB 1UXL . "I113t Mutant Of Human Sod1" . . . . . 100.00 153 98.04 98.04 6.42e-101 . . . . 18708 1 32 no PDB 1UXM . "A4v Mutant Of Human Sod1" . . . . . 100.00 153 98.04 98.04 5.76e-101 . . . . 18708 1 33 no PDB 2AF2 . "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" . . . . . 100.00 153 100.00 100.00 4.22e-103 . . . . 18708 1 34 no PDB 2C9S . "1.24 Angstroms Resolution Structure Of Zn-Zn Human Superoxide Dismutase" . . . . . 100.00 153 98.69 98.69 1.17e-101 . . . . 18708 1 35 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 . . . . 18708 1 36 no PDB 2C9V . "Atomic Resolution Structure Of Cu-Zn Human Superoxide Dismutase" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18708 1 37 no PDB 2GBT . "C6aC111A CUZN SUPEROXIDE DISMUTASE" . . . . . 100.00 153 99.35 100.00 9.89e-103 . . . . 18708 1 38 no PDB 2GBU . "C6a/c111a/c57a/c146a Apo Cuzn Superoxide Dismutase" . . . . . 100.00 153 98.04 98.69 1.21e-100 . . . . 18708 1 39 no PDB 2GBV . "C6aC111AC57AC146A HOLO CUZN SUPEROXIDE DISMUTASE" . . . . . 100.00 153 98.04 98.69 1.21e-100 . . . . 18708 1 40 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 . . . . 18708 1 41 no PDB 2MP3 . "Truncated L126z-sod1 In Dpc Micelle" . . . . . 81.70 132 98.40 98.40 1.75e-80 . . . . 18708 1 42 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 . . . . 18708 1 43 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 . . . . 18708 1 44 no PDB 2V0A . "Atomic Resolution Crystal Structure Of Human Superoxide Dismutase" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18708 1 45 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 . . . . 18708 1 46 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 . . . . 18708 1 47 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 . . . . 18708 1 48 no PDB 2WKO . "Structure Of Metal Loaded Pathogenic Sod1 Mutant G93a" . . . . . 100.00 154 98.04 98.04 4.89e-101 . . . . 18708 1 49 no PDB 2WYT . "1.0 A Resolution Structure Of L38v Sod1 Mutant" . . . . . 100.00 153 98.04 98.69 4.01e-101 . . . . 18708 1 50 no PDB 2WYZ . "L38v Sod1 Mutant Complexed With Ump" . . . . . 100.00 153 98.04 98.69 4.29e-101 . . . . 18708 1 51 no PDB 2WZ0 . "L38v Sod1 Mutant Complexed With Aniline." . . . . . 100.00 153 98.04 98.69 4.01e-101 . . . . 18708 1 52 no PDB 2WZ5 . "L38v Sod1 Mutant Complexed With L-Methionine" . . . . . 100.00 153 98.04 98.69 4.01e-101 . . . . 18708 1 53 no PDB 2WZ6 . "G93a Sod1 Mutant Complexed With Quinazoline" . . . . . 100.00 153 98.04 98.04 4.73e-101 . . . . 18708 1 54 no PDB 2XJK . "Monomeric Human Cu,Zn Superoxide Dismutase" . . . . . 100.00 153 98.04 98.69 2.09e-100 . . . . 18708 1 55 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 . . . . 18708 1 56 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 . . . . 18708 1 57 no PDB 2ZKY . "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G93a" . . . . . 100.00 159 98.04 98.04 4.50e-101 . . . . 18708 1 58 no PDB 3CQP . "Human Sod1 G85r Variant, Structure I" . . . . . 100.00 153 98.04 98.04 1.35e-100 . . . . 18708 1 59 no PDB 3CQQ . "Human Sod1 G85r Variant, Structure Ii" . . . . . 100.00 153 98.04 98.04 1.31e-100 . . . . 18708 1 60 no PDB 3ECU . "Crystal Structure Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18708 1 61 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 . . . . 18708 1 62 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 . . . . 18708 1 63 no PDB 3GQF . "Structural And Biophysical Properties Of The Pathogenic Sod1 Variant H46rH48Q" . . . . . 100.00 153 97.39 97.39 6.72e-100 . . . . 18708 1 64 no PDB 3GZO . "Human Sod1 G93a Variant" . . . . . 100.00 154 98.04 98.04 4.89e-101 . . . . 18708 1 65 no PDB 3GZP . "Human Sod1 G93a Metal-Free Variant" . . . . . 100.00 153 98.04 98.04 4.73e-101 . . . . 18708 1 66 no PDB 3GZQ . "Human Sod1 A4v Metal-Free Variant" . . . . . 100.00 154 98.04 98.04 5.95e-101 . . . . 18708 1 67 no PDB 3H2P . "Human Sod1 D124v Variant" . . . . . 100.00 153 98.04 98.04 1.83e-100 . . . . 18708 1 68 no PDB 3H2Q . "Human Sod1 H80r Variant, P21 Crystal Form" . . . . . 100.00 153 98.04 98.04 1.11e-100 . . . . 18708 1 69 no PDB 3K91 . "Polysulfane Bridge In Cu-Zn Superoxide Dismutase" . . . . . 100.00 153 97.39 97.39 6.72e-100 . . . . 18708 1 70 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 . . . . 18708 1 71 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 . . . . 18708 1 72 no PDB 3QQD . "Human Sod1 H80r Variant, P212121 Crystal Form" . . . . . 100.00 154 98.04 98.04 1.24e-100 . . . . 18708 1 73 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 . . . . 18708 1 74 no PDB 3T5W . "2me Modified Human Sod1" . . . . . 100.00 153 98.69 98.69 1.17e-101 . . . . 18708 1 75 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 . . . . 18708 1 76 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 . . . . 18708 1 77 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 . . . . 18708 1 78 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 . . . . 18708 1 79 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 . . . . 18708 1 80 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 . . . . 18708 1 81 no PDB 4B3E . "Structure Of Copper-Zinc Superoxide Dismutase Complexed With Bicarbonate." . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 82 no PDB 4BCY . "Monomeric Human Cu,zn Superoxide Dismutase, Mutation H43f" . . . . . 100.00 153 97.39 98.04 3.99e-99 . . . . 18708 1 83 no PDB 4FF9 . "Crystal Structure Of Cysteinylated Wt Sod1" . . . . . 100.00 153 98.69 98.69 1.22e-101 . . . . 18708 1 84 no PDB 4MCM . "Human Sod1 C57s Mutant, As-isolated" . . . . . 100.00 153 98.04 98.04 3.16e-100 . . . . 18708 1 85 no PDB 4MCN . "Human Sod1 C57s Mutant, Metal-free" . . . . . 100.00 153 98.04 98.04 3.16e-100 . . . . 18708 1 86 no PDB 4OH2 . "Crystal Structure Of Cu/zn Superoxide Dismutase I149t" . . . . . 100.00 153 99.35 99.35 1.67e-102 . . . . 18708 1 87 no DBJ BAA14373 . "unnamed protein product [Schizosaccharomyces pombe]" . . . . . 98.69 179 98.68 98.68 4.70e-100 . . . . 18708 1 88 no DBJ BAC20345 . "Cu,Zn-superoxide dismutase [Pan troglodytes]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 89 no DBJ BAG35052 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 90 no DBJ BAG73767 . "superoxide dismutase 1, soluble [synthetic construct]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 91 no EMBL CAA26182 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 92 no EMBL CAG29351 . "SOD1 [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 93 no EMBL CAG46542 . "SOD1 [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 94 no GB AAA72747 . "CuZn superoxide dismutase [synthetic construct]" . . . . . 100.00 154 100.00 100.00 3.36e-103 . . . . 18708 1 95 no GB AAA80237 . "HSOD-GlyProGly-A+, partial [synthetic construct]" . . . . . 100.00 171 100.00 100.00 1.23e-102 . . . . 18708 1 96 no GB AAB05661 . "Cu/Zn-superoxide dismutase [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 97 no GB AAB05662 . "Cu/Zn-superoxide dismutase [Homo sapiens]" . . . . . 100.00 154 98.04 98.04 1.46e-100 . . . . 18708 1 98 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 . . . . 18708 1 99 no REF NP_000445 . "superoxide dismutase [Cu-Zn] [Homo sapiens]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 100 no REF NP_001009025 . "superoxide dismutase [Cu-Zn] [Pan troglodytes]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 101 no REF XP_003813274 . "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 102 no REF XP_004062735 . "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" . . . . . 100.00 154 98.04 98.04 9.02e-101 . . . . 18708 1 103 no REF XP_004062736 . "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" . . . . . 100.00 154 98.04 98.04 9.02e-101 . . . . 18708 1 104 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 . . . . 18708 1 105 no SP P60052 . "RecName: Full=Superoxide dismutase [Cu-Zn]" . . . . . 100.00 154 98.69 98.69 9.40e-102 . . . . 18708 1 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID 1.15.1.1 EC 18708 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 . 18708 1 2 . THR . 18708 1 3 . LYS . 18708 1 4 . ALA . 18708 1 5 . VAL . 18708 1 6 . ALA . 18708 1 7 . VAL . 18708 1 8 . LEU . 18708 1 9 . LYS . 18708 1 10 . GLY . 18708 1 11 . ASP . 18708 1 12 . GLY . 18708 1 13 . PRO . 18708 1 14 . VAL . 18708 1 15 . GLN . 18708 1 16 . GLY . 18708 1 17 . ILE . 18708 1 18 . ILE . 18708 1 19 . ASN . 18708 1 20 . PHE . 18708 1 21 . GLU . 18708 1 22 . GLN . 18708 1 23 . LYS . 18708 1 24 . GLU . 18708 1 25 . SER . 18708 1 26 . ASN . 18708 1 27 . GLY . 18708 1 28 . PRO . 18708 1 29 . VAL . 18708 1 30 . LYS . 18708 1 31 . VAL . 18708 1 32 . TRP . 18708 1 33 . GLY . 18708 1 34 . SER . 18708 1 35 . ILE . 18708 1 36 . LYS . 18708 1 37 . GLY . 18708 1 38 . LEU . 18708 1 39 . THR . 18708 1 40 . GLU . 18708 1 41 . GLY . 18708 1 42 . LEU . 18708 1 43 . HIS . 18708 1 44 . GLY . 18708 1 45 . PHE . 18708 1 46 . HIS . 18708 1 47 . VAL . 18708 1 48 . HIS . 18708 1 49 . GLU . 18708 1 50 . PHE . 18708 1 51 . GLY . 18708 1 52 . ASP . 18708 1 53 . ASN . 18708 1 54 . THR . 18708 1 55 . ALA . 18708 1 56 . GLY . 18708 1 57 . CYS . 18708 1 58 . THR . 18708 1 59 . SER . 18708 1 60 . ALA . 18708 1 61 . GLY . 18708 1 62 . PRO . 18708 1 63 . HIS . 18708 1 64 . PHE . 18708 1 65 . ASN . 18708 1 66 . PRO . 18708 1 67 . LEU . 18708 1 68 . SER . 18708 1 69 . ARG . 18708 1 70 . LYS . 18708 1 71 . HIS . 18708 1 72 . GLY . 18708 1 73 . GLY . 18708 1 74 . PRO . 18708 1 75 . LYS . 18708 1 76 . ASP . 18708 1 77 . GLU . 18708 1 78 . GLU . 18708 1 79 . ARG . 18708 1 80 . HIS . 18708 1 81 . VAL . 18708 1 82 . GLY . 18708 1 83 . ASP . 18708 1 84 . LEU . 18708 1 85 . GLY . 18708 1 86 . ASN . 18708 1 87 . VAL . 18708 1 88 . THR . 18708 1 89 . ALA . 18708 1 90 . ASP . 18708 1 91 . LYS . 18708 1 92 . ASP . 18708 1 93 . GLY . 18708 1 94 . VAL . 18708 1 95 . ALA . 18708 1 96 . ASP . 18708 1 97 . VAL . 18708 1 98 . SER . 18708 1 99 . ILE . 18708 1 100 . GLU . 18708 1 101 . ASP . 18708 1 102 . SER . 18708 1 103 . VAL . 18708 1 104 . ILE . 18708 1 105 . SER . 18708 1 106 . LEU . 18708 1 107 . SER . 18708 1 108 . GLY . 18708 1 109 . ASP . 18708 1 110 . HIS . 18708 1 111 . SER . 18708 1 112 . ILE . 18708 1 113 . ILE . 18708 1 114 . GLY . 18708 1 115 . ARG . 18708 1 116 . THR . 18708 1 117 . LEU . 18708 1 118 . VAL . 18708 1 119 . VAL . 18708 1 120 . HIS . 18708 1 121 . GLU . 18708 1 122 . LYS . 18708 1 123 . ALA . 18708 1 124 . ASP . 18708 1 125 . ASP . 18708 1 126 . LEU . 18708 1 127 . GLY . 18708 1 128 . LYS . 18708 1 129 . GLY . 18708 1 130 . GLY . 18708 1 131 . ASN . 18708 1 132 . GLU . 18708 1 133 . GLU . 18708 1 134 . SER . 18708 1 135 . THR . 18708 1 136 . LYS . 18708 1 137 . THR . 18708 1 138 . GLY . 18708 1 139 . ASN . 18708 1 140 . ALA . 18708 1 141 . GLY . 18708 1 142 . SER . 18708 1 143 . ARG . 18708 1 144 . LEU . 18708 1 145 . ALA . 18708 1 146 . CYS . 18708 1 147 . GLY . 18708 1 148 . VAL . 18708 1 149 . ILE . 18708 1 150 . GLY . 18708 1 151 . ILE . 18708 1 152 . ALA . 18708 1 153 . GLN . 18708 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 18708 1 . THR 2 2 18708 1 . LYS 3 3 18708 1 . ALA 4 4 18708 1 . VAL 5 5 18708 1 . ALA 6 6 18708 1 . VAL 7 7 18708 1 . LEU 8 8 18708 1 . LYS 9 9 18708 1 . GLY 10 10 18708 1 . ASP 11 11 18708 1 . GLY 12 12 18708 1 . PRO 13 13 18708 1 . VAL 14 14 18708 1 . GLN 15 15 18708 1 . GLY 16 16 18708 1 . ILE 17 17 18708 1 . ILE 18 18 18708 1 . ASN 19 19 18708 1 . PHE 20 20 18708 1 . GLU 21 21 18708 1 . GLN 22 22 18708 1 . LYS 23 23 18708 1 . GLU 24 24 18708 1 . SER 25 25 18708 1 . ASN 26 26 18708 1 . GLY 27 27 18708 1 . PRO 28 28 18708 1 . VAL 29 29 18708 1 . LYS 30 30 18708 1 . VAL 31 31 18708 1 . TRP 32 32 18708 1 . GLY 33 33 18708 1 . SER 34 34 18708 1 . ILE 35 35 18708 1 . LYS 36 36 18708 1 . GLY 37 37 18708 1 . LEU 38 38 18708 1 . THR 39 39 18708 1 . GLU 40 40 18708 1 . GLY 41 41 18708 1 . LEU 42 42 18708 1 . HIS 43 43 18708 1 . GLY 44 44 18708 1 . PHE 45 45 18708 1 . HIS 46 46 18708 1 . VAL 47 47 18708 1 . HIS 48 48 18708 1 . GLU 49 49 18708 1 . PHE 50 50 18708 1 . GLY 51 51 18708 1 . ASP 52 52 18708 1 . ASN 53 53 18708 1 . THR 54 54 18708 1 . ALA 55 55 18708 1 . GLY 56 56 18708 1 . CYS 57 57 18708 1 . THR 58 58 18708 1 . SER 59 59 18708 1 . ALA 60 60 18708 1 . GLY 61 61 18708 1 . PRO 62 62 18708 1 . HIS 63 63 18708 1 . PHE 64 64 18708 1 . ASN 65 65 18708 1 . PRO 66 66 18708 1 . LEU 67 67 18708 1 . SER 68 68 18708 1 . ARG 69 69 18708 1 . LYS 70 70 18708 1 . HIS 71 71 18708 1 . GLY 72 72 18708 1 . GLY 73 73 18708 1 . PRO 74 74 18708 1 . LYS 75 75 18708 1 . ASP 76 76 18708 1 . GLU 77 77 18708 1 . GLU 78 78 18708 1 . ARG 79 79 18708 1 . HIS 80 80 18708 1 . VAL 81 81 18708 1 . GLY 82 82 18708 1 . ASP 83 83 18708 1 . LEU 84 84 18708 1 . GLY 85 85 18708 1 . ASN 86 86 18708 1 . VAL 87 87 18708 1 . THR 88 88 18708 1 . ALA 89 89 18708 1 . ASP 90 90 18708 1 . LYS 91 91 18708 1 . ASP 92 92 18708 1 . GLY 93 93 18708 1 . VAL 94 94 18708 1 . ALA 95 95 18708 1 . ASP 96 96 18708 1 . VAL 97 97 18708 1 . SER 98 98 18708 1 . ILE 99 99 18708 1 . GLU 100 100 18708 1 . ASP 101 101 18708 1 . SER 102 102 18708 1 . VAL 103 103 18708 1 . ILE 104 104 18708 1 . SER 105 105 18708 1 . LEU 106 106 18708 1 . SER 107 107 18708 1 . GLY 108 108 18708 1 . ASP 109 109 18708 1 . HIS 110 110 18708 1 . SER 111 111 18708 1 . ILE 112 112 18708 1 . ILE 113 113 18708 1 . GLY 114 114 18708 1 . ARG 115 115 18708 1 . THR 116 116 18708 1 . LEU 117 117 18708 1 . VAL 118 118 18708 1 . VAL 119 119 18708 1 . HIS 120 120 18708 1 . GLU 121 121 18708 1 . LYS 122 122 18708 1 . ALA 123 123 18708 1 . ASP 124 124 18708 1 . ASP 125 125 18708 1 . LEU 126 126 18708 1 . GLY 127 127 18708 1 . LYS 128 128 18708 1 . GLY 129 129 18708 1 . GLY 130 130 18708 1 . ASN 131 131 18708 1 . GLU 132 132 18708 1 . GLU 133 133 18708 1 . SER 134 134 18708 1 . THR 135 135 18708 1 . LYS 136 136 18708 1 . THR 137 137 18708 1 . GLY 138 138 18708 1 . ASN 139 139 18708 1 . ALA 140 140 18708 1 . GLY 141 141 18708 1 . SER 142 142 18708 1 . ARG 143 143 18708 1 . LEU 144 144 18708 1 . ALA 145 145 18708 1 . CYS 146 146 18708 1 . GLY 147 147 18708 1 . VAL 148 148 18708 1 . ILE 149 149 18708 1 . GLY 150 150 18708 1 . ILE 151 151 18708 1 . ALA 152 152 18708 1 . GLN 153 153 18708 1 stop_ save_ save_entity_CO _Entity.Sf_category entity _Entity.Sf_framecode entity_CO _Entity.Entry_ID 18708 _Entity.ID 2 _Entity.BMRB_code CO _Entity.Name entity_CO _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 CO _Entity.Nonpolymer_comp_label $chem_comp_CO _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 58.933 _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 'COBALT (II) ION' BMRB 18708 2 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID 'COBALT (II) ION' BMRB 18708 2 CO 'Three letter code' 18708 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 CO $chem_comp_CO 18708 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 CO CO 18708 2 stop_ save_ save_entity_CU _Entity.Sf_category entity _Entity.Sf_framecode entity_CU _Entity.Entry_ID 18708 _Entity.ID 3 _Entity.BMRB_code CU _Entity.Name entity_CU _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 3 _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 18708 3 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 18708 3 CU 'Three letter code' 18708 3 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 18708 3 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 18708 3 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 18708 _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_CU-ZN . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18708 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 18708 _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_CU-ZN . 'recombinant technology' 'Escherichia coli' 'Escherichia coli' . . Escherichia coli Topp1 . . . . . . . . . . . . . . . . . . . . . . 18708 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_CO _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CO _Chem_comp.Entry_ID 18708 _Chem_comp.ID CO _Chem_comp.Provenance PDB _Chem_comp.Name 'COBALT (II) ION' _Chem_comp.Type NON-POLYMER _Chem_comp.BMRB_code CO _Chem_comp.PDB_code CO _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 CO _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/Co/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 Co _Chem_comp.Formula_weight 58.933 _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 [Co++] SMILES CACTVS 3.341 18708 CO [Co++] SMILES_CANONICAL CACTVS 3.341 18708 CO [Co+2] SMILES ACDLabs 10.04 18708 CO [Co+2] SMILES 'OpenEye OEToolkits' 1.5.0 18708 CO [Co+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 18708 CO InChI=1S/Co/q+2 InChI InChI 1.03 18708 CO XLJKHNWPARRRJB-UHFFFAOYSA-N InChIKey InChI 1.03 18708 CO 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 cobalt(2+) 'SYSTEMATIC NAME' ACDLabs 10.04 18708 CO 'cobalt(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 18708 CO 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 CO CO CO CO . CO . . N 2 . . . 0 no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 18708 CO stop_ save_ save_chem_comp_CU _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CU _Chem_comp.Entry_ID 18708 _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 18708 CU [Cu++] SMILES_CANONICAL CACTVS 3.341 18708 CU [Cu+2] SMILES ACDLabs 10.04 18708 CU [Cu+2] SMILES 'OpenEye OEToolkits' 1.5.0 18708 CU [Cu+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 18708 CU InChI=1S/Cu/q+2 InChI InChI 1.03 18708 CU JPVYNHNXODAKFH-UHFFFAOYSA-N InChIKey InChI 1.03 18708 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 18708 CU 'copper(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 18708 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 . 18708 CU stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18708 _Sample.ID 1 _Sample.Type solid _Sample.Sub_type . _Sample.Details 'SOD,20% PEG' _Sample.Aggregate_sample_number . _Sample.Solvent_system solid _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 [CU-ZN]' '[U-13C; U-15N]' . . 1 $SUPEROXIDE_DISMUTASE_CU-ZN . . . . . mM . . . . 18708 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 18708 _Sample_condition_list.ID 1 _Sample_condition_list.Details 'pH [0.0], temp [298], pressure [0.0], ionStrength [0.0]' 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' . . mM 18708 1 pH . . pH 18708 1 pressure . . atm 18708 1 temperature 298.000 . K 18708 1 stop_ save_ ############################ # Computer software used # ############################ save_AutoDep _Software.Sf_category software _Software.Sf_framecode AutoDep _Software.Entry_ID 18708 _Software.ID 1 _Software.Name AutoDep _Software.Version 4.3 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID PDBe . . 18708 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18708 1 stop_ save_ save_cyana _Software.Sf_category software _Software.Sf_framecode cyana _Software.Entry_ID 18708 _Software.ID 2 _Software.Name CYANA _Software.Version any _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 18708 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18708 2 'data analysis' 18708 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Bruker_Avance-1000 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode Bruker_Avance-1000 _NMR_spectrometer.Entry_ID 18708 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 1000 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 18708 _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 Bruker_Avance-1000 Bruker Avance . 1000 . . . 18708 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 18708 _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 NMR_expt no 1 $NMR_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $Bruker_Avance-1000 . . . . . . . . . . . . . . . . 18708 1 stop_ save_ save_NMR_expt _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_expt _NMR_spec_expt.Entry_ID 18708 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name . _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $Bruker_Avance-1000 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . 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 18708 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.0 external indirect 0.251449519 'separate MAS rotor' cylindrical Parallel . . . . . . 18708 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 external indirect 1 'separate MAS rotor' cylindrical Parallel . . . . . . 18708 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 external indirect 0.1014 'separate MAS rotor' cylindrical Parallel . . . . . . 18708 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 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list _Assigned_chem_shift_list.Entry_ID 18708 _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 'Origin nmrStar file /ebi/msd/pdb_root/Processing/prepare/4b8k/ebi/shifts_3.bmrb.csh' _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 NMR_expt 1 $sample_1 solid 18708 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 0.1 . 1 . 1 . . 2 THR C . 18708 1 2 . 1 1 3 3 LYS H H 1 8.666 0.05 . 1 . 3 . . 3 LYS H . 18708 1 3 . 1 1 3 3 LYS C C 13 171.607 0.1 . 1 . 5 . . 3 LYS C . 18708 1 4 . 1 1 3 3 LYS CA C 13 51.178 0.1 . 1 . 4 . . 3 LYS CA . 18708 1 5 . 1 1 3 3 LYS N N 15 123.998 0.1 . 1 . 2 . . 3 LYS N . 18708 1 6 . 1 1 4 4 ALA H H 1 9.116 0.05 . 1 . 7 . . 4 ALA H . 18708 1 7 . 1 1 4 4 ALA C C 13 172.145 0.1 . 1 . 9 . . 4 ALA C . 18708 1 8 . 1 1 4 4 ALA CA C 13 47.504 0.1 . 1 . 8 . . 4 ALA CA . 18708 1 9 . 1 1 4 4 ALA N N 15 123.295 0.1 . 1 . 6 . . 4 ALA N . 18708 1 10 . 1 1 5 5 VAL H H 1 9.545 0.05 . 1 . 11 . . 5 VAL H . 18708 1 11 . 1 1 5 5 VAL C C 13 167.836 0.1 . 1 . 13 . . 5 VAL C . 18708 1 12 . 1 1 5 5 VAL CA C 13 56.875 0.1 . 1 . 12 . . 5 VAL CA . 18708 1 13 . 1 1 5 5 VAL N N 15 121.466 0.1 . 1 . 10 . . 5 VAL N . 18708 1 14 . 1 1 6 6 ALA H H 1 9.177 0.05 . 1 . 15 . . 6 ALA H . 18708 1 15 . 1 1 6 6 ALA C C 13 171.607 0.1 . 1 . 17 . . 6 ALA C . 18708 1 16 . 1 1 6 6 ALA CA C 13 47.471 0.1 . 1 . 16 . . 6 ALA CA . 18708 1 17 . 1 1 6 6 ALA N N 15 125.984 0.1 . 1 . 14 . . 6 ALA N . 18708 1 18 . 1 1 7 7 VAL H H 1 9.116 0.05 . 1 . 19 . . 7 VAL H . 18708 1 19 . 1 1 7 7 VAL C C 13 172.244 0.1 . 1 . 21 . . 7 VAL C . 18708 1 20 . 1 1 7 7 VAL CA C 13 58.476 0.1 . 1 . 20 . . 7 VAL CA . 18708 1 21 . 1 1 7 7 VAL N N 15 123.600 0.1 . 1 . 18 . . 7 VAL N . 18708 1 22 . 1 1 8 8 LEU H H 1 8.916 0.05 . 1 . 23 . . 8 LEU H . 18708 1 23 . 1 1 8 8 LEU C C 13 172.557 0.1 . 1 . 25 . . 8 LEU C . 18708 1 24 . 1 1 8 8 LEU CA C 13 51.052 0.1 . 1 . 24 . . 8 LEU CA . 18708 1 25 . 1 1 8 8 LEU N N 15 126.455 0.1 . 1 . 22 . . 8 LEU N . 18708 1 26 . 1 1 9 9 LYS H H 1 8.315 0.05 . 1 . 27 . . 9 LYS H . 18708 1 27 . 1 1 9 9 LYS C C 13 172.509 0.1 . 1 . 29 . . 9 LYS C . 18708 1 28 . 1 1 9 9 LYS CA C 13 51.897 0.1 . 1 . 28 . . 9 LYS CA . 18708 1 29 . 1 1 9 9 LYS N N 15 120.820 0.1 . 1 . 26 . . 9 LYS N . 18708 1 30 . 1 1 10 10 GLY H H 1 8.968 0.05 . 1 . 31 . . 10 GLY H . 18708 1 31 . 1 1 10 10 GLY C C 13 169.847 0.1 . 1 . 33 . . 10 GLY C . 18708 1 32 . 1 1 10 10 GLY CA C 13 42.275 0.1 . 1 . 32 . . 10 GLY CA . 18708 1 33 . 1 1 10 10 GLY N N 15 111.249 0.1 . 1 . 30 . . 10 GLY N . 18708 1 34 . 1 1 11 11 ASP H H 1 8.745 0.05 . 1 . 35 . . 11 ASP H . 18708 1 35 . 1 1 11 11 ASP C C 13 173.132 0.1 . 1 . 37 . . 11 ASP C . 18708 1 36 . 1 1 11 11 ASP CA C 13 51.317 0.1 . 1 . 36 . . 11 ASP CA . 18708 1 37 . 1 1 11 11 ASP N N 15 120.904 0.1 . 1 . 34 . . 11 ASP N . 18708 1 38 . 1 1 12 12 GLY H H 1 7.985 0.05 . 1 . 39 . . 12 GLY H . 18708 1 39 . 1 1 12 12 GLY CA C 13 41.200 0.1 . 1 . 40 . . 12 GLY CA . 18708 1 40 . 1 1 12 12 GLY N N 15 109.862 0.1 . 1 . 38 . . 12 GLY N . 18708 1 41 . 1 1 13 13 PRO C C 13 173.640 0.1 . 1 . 41 . . 13 PRO C . 18708 1 42 . 1 1 14 14 VAL H H 1 7.476 0.05 . 1 . 43 . . 14 VAL H . 18708 1 43 . 1 1 14 14 VAL C C 13 172.804 0.1 . 1 . 45 . . 14 VAL C . 18708 1 44 . 1 1 14 14 VAL CA C 13 59.884 0.1 . 1 . 44 . . 14 VAL CA . 18708 1 45 . 1 1 14 14 VAL N N 15 120.414 0.1 . 1 . 42 . . 14 VAL N . 18708 1 46 . 1 1 15 15 GLN H H 1 7.938 0.05 . 1 . 47 . . 15 GLN H . 18708 1 47 . 1 1 15 15 GLN C C 13 171.168 0.1 . 1 . 49 . . 15 GLN C . 18708 1 48 . 1 1 15 15 GLN CA C 13 50.679 0.1 . 1 . 48 . . 15 GLN CA . 18708 1 49 . 1 1 15 15 GLN N N 15 122.664 0.1 . 1 . 46 . . 15 GLN N . 18708 1 50 . 1 1 16 16 GLY H H 1 8.288 0.05 . 1 . 51 . . 16 GLY H . 18708 1 51 . 1 1 16 16 GLY C C 13 167.726 0.1 . 1 . 53 . . 16 GLY C . 18708 1 52 . 1 1 16 16 GLY CA C 13 43.625 0.1 . 1 . 52 . . 16 GLY CA . 18708 1 53 . 1 1 16 16 GLY N N 15 107.018 0.1 . 1 . 50 . . 16 GLY N . 18708 1 54 . 1 1 17 17 ILE H H 1 7.948 0.05 . 1 . 55 . . 17 ILE H . 18708 1 55 . 1 1 17 17 ILE C C 13 171.194 0.1 . 1 . 57 . . 17 ILE C . 18708 1 56 . 1 1 17 17 ILE CA C 13 58.497 0.1 . 1 . 56 . . 17 ILE CA . 18708 1 57 . 1 1 17 17 ILE N N 15 120.248 0.1 . 1 . 54 . . 17 ILE N . 18708 1 58 . 1 1 18 18 ILE H H 1 8.725 0.05 . 1 . 59 . . 18 ILE H . 18708 1 59 . 1 1 18 18 ILE C C 13 168.889 0.1 . 1 . 61 . . 18 ILE C . 18708 1 60 . 1 1 18 18 ILE CA C 13 53.431 0.1 . 1 . 60 . . 18 ILE CA . 18708 1 61 . 1 1 18 18 ILE N N 15 125.851 0.1 . 1 . 58 . . 18 ILE N . 18708 1 62 . 1 1 19 19 ASN H H 1 8.727 0.05 . 1 . 63 . . 19 ASN H . 18708 1 63 . 1 1 19 19 ASN C C 13 168.903 0.1 . 1 . 65 . . 19 ASN C . 18708 1 64 . 1 1 19 19 ASN CA C 13 49.088 0.1 . 1 . 64 . . 19 ASN CA . 18708 1 65 . 1 1 19 19 ASN N N 15 123.256 0.1 . 1 . 62 . . 19 ASN N . 18708 1 66 . 1 1 20 20 PHE H H 1 8.399 0.05 . 1 . 67 . . 20 PHE H . 18708 1 67 . 1 1 20 20 PHE C C 13 173.219 0.1 . 1 . 69 . . 20 PHE C . 18708 1 68 . 1 1 20 20 PHE CA C 13 52.058 0.1 . 1 . 68 . . 20 PHE CA . 18708 1 69 . 1 1 20 20 PHE N N 15 113.849 0.1 . 1 . 66 . . 20 PHE N . 18708 1 70 . 1 1 21 21 GLU H H 1 9.526 0.05 . 1 . 71 . . 21 GLU H . 18708 1 71 . 1 1 21 21 GLU C C 13 170.280 0.1 . 1 . 73 . . 21 GLU C . 18708 1 72 . 1 1 21 21 GLU CA C 13 53.044 0.1 . 1 . 72 . . 21 GLU CA . 18708 1 73 . 1 1 21 21 GLU N N 15 121.454 0.1 . 1 . 70 . . 21 GLU N . 18708 1 74 . 1 1 22 22 GLN H H 1 9.305 0.05 . 1 . 75 . . 22 GLN H . 18708 1 75 . 1 1 22 22 GLN CA C 13 51.180 0.1 . 1 . 76 . . 22 GLN CA . 18708 1 76 . 1 1 22 22 GLN N N 15 130.340 0.1 . 1 . 74 . . 22 GLN N . 18708 1 77 . 1 1 23 23 LYS H H 1 9.088 0.05 . 1 . 78 . . 23 LYS H . 18708 1 78 . 1 1 23 23 LYS CA C 13 57.241 0.1 . 1 . 79 . . 23 LYS CA . 18708 1 79 . 1 1 23 23 LYS N N 15 128.657 0.1 . 1 . 77 . . 23 LYS N . 18708 1 80 . 1 1 24 24 GLU CA C 13 51.392 0.1 . 1 . 80 . . 24 GLU CA . 18708 1 81 . 1 1 25 25 SER CA C 13 58.078 0.1 . 1 . 81 . . 25 SER CA . 18708 1 82 . 1 1 27 27 GLY H H 1 8.032 0.05 . 1 . 83 . . 27 GLY H . 18708 1 83 . 1 1 27 27 GLY CA C 13 42.925 0.1 . 1 . 84 . . 27 GLY CA . 18708 1 84 . 1 1 27 27 GLY N N 15 108.125 0.1 . 1 . 82 . . 27 GLY N . 18708 1 85 . 1 1 28 28 PRO C C 13 173.128 0.1 . 1 . 85 . . 28 PRO C . 18708 1 86 . 1 1 29 29 VAL H H 1 9.089 0.05 . 1 . 87 . . 29 VAL H . 18708 1 87 . 1 1 29 29 VAL C C 13 172.198 0.1 . 1 . 89 . . 29 VAL C . 18708 1 88 . 1 1 29 29 VAL CA C 13 57.720 0.1 . 1 . 88 . . 29 VAL CA . 18708 1 89 . 1 1 29 29 VAL N N 15 121.267 0.1 . 1 . 86 . . 29 VAL N . 18708 1 90 . 1 1 30 30 LYS H H 1 9.200 0.05 . 1 . 91 . . 30 LYS H . 18708 1 91 . 1 1 30 30 LYS C C 13 172.098 0.1 . 1 . 93 . . 30 LYS C . 18708 1 92 . 1 1 30 30 LYS CA C 13 52.642 0.1 . 1 . 92 . . 30 LYS CA . 18708 1 93 . 1 1 30 30 LYS N N 15 127.589 0.1 . 1 . 90 . . 30 LYS N . 18708 1 94 . 1 1 31 31 VAL H H 1 9.282 0.05 . 1 . 95 . . 31 VAL H . 18708 1 95 . 1 1 31 31 VAL C C 13 172.244 0.1 . 1 . 97 . . 31 VAL C . 18708 1 96 . 1 1 31 31 VAL CA C 13 57.139 0.1 . 1 . 96 . . 31 VAL CA . 18708 1 97 . 1 1 31 31 VAL N N 15 126.037 0.1 . 1 . 94 . . 31 VAL N . 18708 1 98 . 1 1 32 32 TRP H H 1 8.983 0.05 . 1 . 99 . . 32 TRP H . 18708 1 99 . 1 1 32 32 TRP C C 13 170.156 0.1 . 1 . 101 . . 32 TRP C . 18708 1 100 . 1 1 32 32 TRP CA C 13 53.137 0.1 . 1 . 100 . . 32 TRP CA . 18708 1 101 . 1 1 32 32 TRP N N 15 125.414 0.1 . 1 . 98 . . 32 TRP N . 18708 1 102 . 1 1 33 33 GLY H H 1 8.360 0.05 . 1 . 103 . . 33 GLY H . 18708 1 103 . 1 1 33 33 GLY C C 13 168.400 0.1 . 1 . 105 . . 33 GLY C . 18708 1 104 . 1 1 33 33 GLY CA C 13 41.567 0.1 . 1 . 104 . . 33 GLY CA . 18708 1 105 . 1 1 33 33 GLY N N 15 107.848 0.1 . 1 . 102 . . 33 GLY N . 18708 1 106 . 1 1 34 34 SER H H 1 7.838 0.05 . 1 . 107 . . 34 SER H . 18708 1 107 . 1 1 34 34 SER C C 13 169.618 0.1 . 1 . 109 . . 34 SER C . 18708 1 108 . 1 1 34 34 SER CA C 13 53.875 0.1 . 1 . 108 . . 34 SER CA . 18708 1 109 . 1 1 34 34 SER N N 15 114.377 0.1 . 1 . 106 . . 34 SER N . 18708 1 110 . 1 1 35 35 ILE H H 1 8.496 0.05 . 1 . 111 . . 35 ILE H . 18708 1 111 . 1 1 35 35 ILE C C 13 169.713 0.1 . 1 . 113 . . 35 ILE C . 18708 1 112 . 1 1 35 35 ILE CA C 13 56.769 0.1 . 1 . 112 . . 35 ILE CA . 18708 1 113 . 1 1 35 35 ILE N N 15 123.149 0.1 . 1 . 110 . . 35 ILE N . 18708 1 114 . 1 1 36 36 LYS H H 1 9.091 0.05 . 1 . 115 . . 36 LYS H . 18708 1 115 . 1 1 36 36 LYS C C 13 172.260 0.1 . 1 . 117 . . 36 LYS C . 18708 1 116 . 1 1 36 36 LYS CA C 13 51.150 0.1 . 1 . 116 . . 36 LYS CA . 18708 1 117 . 1 1 36 36 LYS N N 15 123.803 0.1 . 1 . 114 . . 36 LYS N . 18708 1 118 . 1 1 37 37 GLY H H 1 8.237 0.05 . 1 . 119 . . 37 GLY H . 18708 1 119 . 1 1 37 37 GLY C C 13 171.641 0.1 . 1 . 121 . . 37 GLY C . 18708 1 120 . 1 1 37 37 GLY CA C 13 42.361 0.1 . 1 . 120 . . 37 GLY CA . 18708 1 121 . 1 1 37 37 GLY N N 15 105.495 0.1 . 1 . 118 . . 37 GLY N . 18708 1 122 . 1 1 38 38 LEU H H 1 8.156 0.05 . 1 . 123 . . 38 LEU H . 18708 1 123 . 1 1 38 38 LEU C C 13 174.112 0.1 . 1 . 125 . . 38 LEU C . 18708 1 124 . 1 1 38 38 LEU CA C 13 50.471 0.1 . 1 . 124 . . 38 LEU CA . 18708 1 125 . 1 1 38 38 LEU N N 15 120.966 0.1 . 1 . 122 . . 38 LEU N . 18708 1 126 . 1 1 39 39 THR H H 1 8.660 0.05 . 1 . 127 . . 39 THR H . 18708 1 127 . 1 1 39 39 THR C C 13 173.102 0.1 . 1 . 129 . . 39 THR C . 18708 1 128 . 1 1 39 39 THR CA C 13 58.194 0.1 . 1 . 128 . . 39 THR CA . 18708 1 129 . 1 1 39 39 THR N N 15 110.363 0.1 . 1 . 126 . . 39 THR N . 18708 1 130 . 1 1 40 40 GLU H H 1 8.804 0.05 . 1 . 131 . . 40 GLU H . 18708 1 131 . 1 1 40 40 GLU C C 13 173.134 0.1 . 1 . 133 . . 40 GLU C . 18708 1 132 . 1 1 40 40 GLU CA C 13 54.356 0.1 . 1 . 132 . . 40 GLU CA . 18708 1 133 . 1 1 40 40 GLU N N 15 125.818 0.1 . 1 . 130 . . 40 GLU N . 18708 1 134 . 1 1 41 41 GLY H H 1 8.763 0.05 . 1 . 135 . . 41 GLY H . 18708 1 135 . 1 1 41 41 GLY C C 13 170.046 0.1 . 1 . 137 . . 41 GLY C . 18708 1 136 . 1 1 41 41 GLY CA C 13 40.054 0.1 . 1 . 136 . . 41 GLY CA . 18708 1 137 . 1 1 41 41 GLY N N 15 113.875 0.1 . 1 . 134 . . 41 GLY N . 18708 1 138 . 1 1 42 42 LEU H H 1 8.313 0.05 . 1 . 139 . . 42 LEU H . 18708 1 139 . 1 1 42 42 LEU C C 13 174.218 0.1 . 1 . 141 . . 42 LEU C . 18708 1 140 . 1 1 42 42 LEU CA C 13 52.155 0.1 . 1 . 140 . . 42 LEU CA . 18708 1 141 . 1 1 42 42 LEU N N 15 120.137 0.1 . 1 . 138 . . 42 LEU N . 18708 1 142 . 1 1 43 43 HIS H H 1 8.712 0.05 . 1 . 143 . . 43 HIS H . 18708 1 143 . 1 1 43 43 HIS C C 13 171.504 0.1 . 1 . 145 . . 43 HIS C . 18708 1 144 . 1 1 43 43 HIS CA C 13 50.985 0.1 . 1 . 144 . . 43 HIS CA . 18708 1 145 . 1 1 43 43 HIS N N 15 114.385 0.1 . 1 . 142 . . 43 HIS N . 18708 1 146 . 1 1 44 44 GLY H H 1 8.875 0.05 . 1 . 147 . . 44 GLY H . 18708 1 147 . 1 1 44 44 GLY C C 13 168.656 0.1 . 1 . 149 . . 44 GLY C . 18708 1 148 . 1 1 44 44 GLY CA C 13 44.195 0.1 . 1 . 148 . . 44 GLY CA . 18708 1 149 . 1 1 44 44 GLY N N 15 108.872 0.1 . 1 . 146 . . 44 GLY N . 18708 1 150 . 1 1 45 45 PHE H H 1 8.111 0.05 . 1 . 151 . . 45 PHE H . 18708 1 151 . 1 1 45 45 PHE CA C 13 53.098 0.1 . 1 . 152 . . 45 PHE CA . 18708 1 152 . 1 1 45 45 PHE N N 15 126.439 0.1 . 1 . 150 . . 45 PHE N . 18708 1 153 . 1 1 46 46 HIS H H 1 8.107 0.05 . 1 . 154 . . 46 HIS H . 18708 1 154 . 1 1 46 46 HIS C C 13 172.415 0.1 . 1 . 156 . . 46 HIS C . 18708 1 155 . 1 1 46 46 HIS CA C 13 49.206 0.1 . 1 . 155 . . 46 HIS CA . 18708 1 156 . 1 1 46 46 HIS N N 15 115.353 0.1 . 1 . 153 . . 46 HIS N . 18708 1 157 . 1 1 47 47 VAL H H 1 9.366 0.05 . 1 . 158 . . 47 VAL H . 18708 1 158 . 1 1 47 47 VAL C C 13 173.900 0.1 . 1 . 160 . . 47 VAL C . 18708 1 159 . 1 1 47 47 VAL CA C 13 58.792 0.1 . 1 . 159 . . 47 VAL CA . 18708 1 160 . 1 1 47 47 VAL N N 15 120.548 0.1 . 1 . 157 . . 47 VAL N . 18708 1 161 . 1 1 48 48 HIS H H 1 10.210 0.05 . 1 . 162 . . 48 HIS H . 18708 1 162 . 1 1 48 48 HIS C C 13 171.084 0.1 . 1 . 164 . . 48 HIS C . 18708 1 163 . 1 1 48 48 HIS CA C 13 52.756 0.1 . 1 . 163 . . 48 HIS CA . 18708 1 164 . 1 1 48 48 HIS N N 15 129.236 0.1 . 1 . 161 . . 48 HIS N . 18708 1 165 . 1 1 49 49 GLU H H 1 8.492 0.05 . 1 . 166 . . 49 GLU H . 18708 1 166 . 1 1 49 49 GLU C C 13 171.635 0.1 . 1 . 168 . . 49 GLU C . 18708 1 167 . 1 1 49 49 GLU CA C 13 57.759 0.1 . 1 . 167 . . 49 GLU CA . 18708 1 168 . 1 1 49 49 GLU N N 15 118.119 0.1 . 1 . 165 . . 49 GLU N . 18708 1 169 . 1 1 50 50 PHE H H 1 8.580 0.05 . 1 . 170 . . 50 PHE H . 18708 1 170 . 1 1 50 50 PHE C C 13 175.252 0.1 . 1 . 172 . . 50 PHE C . 18708 1 171 . 1 1 50 50 PHE CA C 13 52.900 0.1 . 1 . 171 . . 50 PHE CA . 18708 1 172 . 1 1 50 50 PHE N N 15 110.329 0.1 . 1 . 169 . . 50 PHE N . 18708 1 173 . 1 1 51 51 GLY H H 1 10.208 0.05 . 1 . 174 . . 51 GLY H . 18708 1 174 . 1 1 51 51 GLY C C 13 168.248 0.1 . 1 . 175 . . 51 GLY C . 18708 1 175 . 1 1 51 51 GLY N N 15 119.251 0.1 . 1 . 173 . . 51 GLY N . 18708 1 176 . 1 1 52 52 ASP H H 1 5.834 0.05 . 1 . 177 . . 52 ASP H . 18708 1 177 . 1 1 52 52 ASP CA C 13 48.891 0.1 . 1 . 178 . . 52 ASP CA . 18708 1 178 . 1 1 52 52 ASP N N 15 114.958 0.1 . 1 . 176 . . 52 ASP N . 18708 1 179 . 1 1 53 53 ASN H H 1 9.360 0.05 . 1 . 180 . . 53 ASN H . 18708 1 180 . 1 1 53 53 ASN CA C 13 48.233 0.1 . 1 . 181 . . 53 ASN CA . 18708 1 181 . 1 1 53 53 ASN N N 15 128.224 0.1 . 1 . 179 . . 53 ASN N . 18708 1 182 . 1 1 54 54 THR C C 13 168.656 0.1 . 1 . 182 . . 54 THR C . 18708 1 183 . 1 1 55 55 ALA H H 1 8.390 0.05 . 1 . 184 . . 55 ALA H . 18708 1 184 . 1 1 55 55 ALA C C 13 174.185 0.1 . 1 . 186 . . 55 ALA C . 18708 1 185 . 1 1 55 55 ALA CA C 13 46.155 0.1 . 1 . 185 . . 55 ALA CA . 18708 1 186 . 1 1 55 55 ALA N N 15 126.661 0.1 . 1 . 183 . . 55 ALA N . 18708 1 187 . 1 1 56 56 GLY H H 1 7.282 0.05 . 1 . 188 . . 56 GLY H . 18708 1 188 . 1 1 56 56 GLY C C 13 171.578 0.1 . 1 . 190 . . 56 GLY C . 18708 1 189 . 1 1 56 56 GLY CA C 13 42.580 0.1 . 1 . 189 . . 56 GLY CA . 18708 1 190 . 1 1 56 56 GLY N N 15 107.903 0.1 . 1 . 187 . . 56 GLY N . 18708 1 191 . 1 1 57 57 CYS H H 1 8.900 0.05 . 1 . 192 . . 57 CYS H . 18708 1 192 . 1 1 57 57 CYS C C 13 175.209 0.1 . 1 . 194 . . 57 CYS C . 18708 1 193 . 1 1 57 57 CYS CA C 13 49.088 0.1 . 1 . 193 . . 57 CYS CA . 18708 1 194 . 1 1 57 57 CYS N N 15 117.952 0.1 . 1 . 191 . . 57 CYS N . 18708 1 195 . 1 1 58 58 THR H H 1 8.505 0.05 . 1 . 196 . . 58 THR H . 18708 1 196 . 1 1 58 58 THR CA C 13 58.239 0.1 . 1 . 197 . . 58 THR CA . 18708 1 197 . 1 1 58 58 THR N N 15 119.852 0.1 . 1 . 195 . . 58 THR N . 18708 1 198 . 1 1 59 59 SER C C 13 170.763 0.1 . 1 . 199 . . 59 SER C . 18708 1 199 . 1 1 59 59 SER CA C 13 55.609 0.1 . 1 . 198 . . 59 SER CA . 18708 1 200 . 1 1 60 60 ALA H H 1 6.898 0.05 . 1 . 201 . . 60 ALA H . 18708 1 201 . 1 1 60 60 ALA CA C 13 49.940 0.1 . 1 . 202 . . 60 ALA CA . 18708 1 202 . 1 1 60 60 ALA N N 15 119.753 0.1 . 1 . 200 . . 60 ALA N . 18708 1 203 . 1 1 61 61 GLY H H 1 7.730 0.05 . 1 . 204 . . 61 GLY H . 18708 1 204 . 1 1 61 61 GLY CA C 13 42.805 0.1 . 1 . 205 . . 61 GLY CA . 18708 1 205 . 1 1 61 61 GLY N N 15 101.351 0.1 . 1 . 203 . . 61 GLY N . 18708 1 206 . 1 1 62 62 PRO C C 13 172.276 0.1 . 1 . 206 . . 62 PRO C . 18708 1 207 . 1 1 63 63 HIS H H 1 7.474 0.05 . 1 . 208 . . 63 HIS H . 18708 1 208 . 1 1 63 63 HIS CA C 13 52.119 0.1 . 1 . 209 . . 63 HIS CA . 18708 1 209 . 1 1 63 63 HIS N N 15 115.023 0.1 . 1 . 207 . . 63 HIS N . 18708 1 210 . 1 1 64 64 PHE C C 13 171.731 0.1 . 1 . 210 . . 64 PHE C . 18708 1 211 . 1 1 65 65 ASN H H 1 9.426 0.05 . 1 . 212 . . 65 ASN H . 18708 1 212 . 1 1 65 65 ASN CA C 13 47.753 0.1 . 1 . 213 . . 65 ASN CA . 18708 1 213 . 1 1 65 65 ASN N N 15 126.978 0.1 . 1 . 211 . . 65 ASN N . 18708 1 214 . 1 1 67 67 LEU H H 1 7.720 0.05 . 1 . 215 . . 67 LEU H . 18708 1 215 . 1 1 67 67 LEU C C 13 172.580 0.1 . 1 . 217 . . 67 LEU C . 18708 1 216 . 1 1 67 67 LEU CA C 13 50.911 0.1 . 1 . 216 . . 67 LEU CA . 18708 1 217 . 1 1 67 67 LEU N N 15 117.937 0.1 . 1 . 214 . . 67 LEU N . 18708 1 218 . 1 1 68 68 SER H H 1 7.428 0.05 . 1 . 219 . . 68 SER H . 18708 1 219 . 1 1 68 68 SER CA C 13 55.953 0.1 . 1 . 220 . . 68 SER CA . 18708 1 220 . 1 1 68 68 SER N N 15 110.842 0.1 . 1 . 218 . . 68 SER N . 18708 1 221 . 1 1 69 69 ARG H H 1 8.508 0.05 . 1 . 222 . . 69 ARG H . 18708 1 222 . 1 1 69 69 ARG C C 13 173.381 0.1 . 1 . 224 . . 69 ARG C . 18708 1 223 . 1 1 69 69 ARG CA C 13 50.543 0.1 . 1 . 223 . . 69 ARG CA . 18708 1 224 . 1 1 69 69 ARG N N 15 120.782 0.1 . 1 . 221 . . 69 ARG N . 18708 1 225 . 1 1 70 70 LYS H H 1 8.745 0.05 . 1 . 226 . . 70 LYS H . 18708 1 226 . 1 1 70 70 LYS C C 13 169.994 0.1 . 1 . 228 . . 70 LYS C . 18708 1 227 . 1 1 70 70 LYS CA C 13 52.596 0.1 . 1 . 227 . . 70 LYS CA . 18708 1 228 . 1 1 70 70 LYS N N 15 118.055 0.1 . 1 . 225 . . 70 LYS N . 18708 1 229 . 1 1 71 71 HIS H H 1 7.152 0.05 . 1 . 230 . . 71 HIS H . 18708 1 230 . 1 1 71 71 HIS C C 13 171.534 0.1 . 1 . 232 . . 71 HIS C . 18708 1 231 . 1 1 71 71 HIS CA C 13 52.549 0.1 . 1 . 231 . . 71 HIS CA . 18708 1 232 . 1 1 71 71 HIS N N 15 111.871 0.1 . 1 . 229 . . 71 HIS N . 18708 1 233 . 1 1 72 72 GLY H H 1 7.209 0.05 . 1 . 234 . . 72 GLY H . 18708 1 234 . 1 1 72 72 GLY C C 13 168.634 0.1 . 1 . 236 . . 72 GLY C . 18708 1 235 . 1 1 72 72 GLY CA C 13 41.274 0.1 . 1 . 235 . . 72 GLY CA . 18708 1 236 . 1 1 72 72 GLY N N 15 112.910 0.1 . 1 . 233 . . 72 GLY N . 18708 1 237 . 1 1 73 73 GLY H H 1 8.789 0.05 . 1 . 238 . . 73 GLY H . 18708 1 238 . 1 1 73 73 GLY CA C 13 41.221 0.1 . 1 . 239 . . 73 GLY CA . 18708 1 239 . 1 1 73 73 GLY N N 15 105.207 0.1 . 1 . 237 . . 73 GLY N . 18708 1 240 . 1 1 74 74 PRO C C 13 175.753 0.1 . 1 . 240 . . 74 PRO C . 18708 1 241 . 1 1 75 75 LYS H H 1 8.651 0.05 . 1 . 242 . . 75 LYS H . 18708 1 242 . 1 1 75 75 LYS C C 13 173.640 0.1 . 1 . 244 . . 75 LYS C . 18708 1 243 . 1 1 75 75 LYS CA C 13 51.103 0.1 . 1 . 243 . . 75 LYS CA . 18708 1 244 . 1 1 75 75 LYS N N 15 114.868 0.1 . 1 . 241 . . 75 LYS N . 18708 1 245 . 1 1 76 76 ASP H H 1 7.461 0.05 . 1 . 246 . . 76 ASP H . 18708 1 246 . 1 1 76 76 ASP C C 13 172.557 0.1 . 1 . 248 . . 76 ASP C . 18708 1 247 . 1 1 76 76 ASP CA C 13 51.309 0.1 . 1 . 247 . . 76 ASP CA . 18708 1 248 . 1 1 76 76 ASP N N 15 120.414 0.1 . 1 . 245 . . 76 ASP N . 18708 1 249 . 1 1 77 77 GLU H H 1 8.315 0.05 . 1 . 250 . . 77 GLU H . 18708 1 250 . 1 1 77 77 GLU C C 13 174.101 0.1 . 1 . 252 . . 77 GLU C . 18708 1 251 . 1 1 77 77 GLU CA C 13 55.513 0.1 . 1 . 251 . . 77 GLU CA . 18708 1 252 . 1 1 77 77 GLU N N 15 120.820 0.1 . 1 . 249 . . 77 GLU N . 18708 1 253 . 1 1 78 78 GLU H H 1 8.109 0.05 . 1 . 254 . . 78 GLU H . 18708 1 254 . 1 1 78 78 GLU C C 13 168.285 0.1 . 1 . 256 . . 78 GLU C . 18708 1 255 . 1 1 78 78 GLU CA C 13 52.078 0.1 . 1 . 255 . . 78 GLU CA . 18708 1 256 . 1 1 78 78 GLU N N 15 119.251 0.1 . 1 . 253 . . 78 GLU N . 18708 1 257 . 1 1 79 79 ARG H H 1 6.999 0.05 . 1 . 258 . . 79 ARG H . 18708 1 258 . 1 1 79 79 ARG C C 13 172.123 0.1 . 1 . 260 . . 79 ARG C . 18708 1 259 . 1 1 79 79 ARG CA C 13 51.074 0.1 . 1 . 259 . . 79 ARG CA . 18708 1 260 . 1 1 79 79 ARG N N 15 118.991 0.1 . 1 . 257 . . 79 ARG N . 18708 1 261 . 1 1 80 80 HIS H H 1 8.355 0.05 . 1 . 262 . . 80 HIS H . 18708 1 262 . 1 1 80 80 HIS CA C 13 49.953 0.1 . 1 . 263 . . 80 HIS CA . 18708 1 263 . 1 1 80 80 HIS N N 15 118.000 0.1 . 1 . 261 . . 80 HIS N . 18708 1 264 . 1 1 81 81 VAL C C 13 173.460 0.1 . 1 . 264 . . 81 VAL C . 18708 1 265 . 1 1 82 82 GLY H H 1 8.487 0.05 . 1 . 266 . . 82 GLY H . 18708 1 266 . 1 1 82 82 GLY C C 13 170.370 0.1 . 1 . 268 . . 82 GLY C . 18708 1 267 . 1 1 82 82 GLY CA C 13 42.688 0.1 . 1 . 267 . . 82 GLY CA . 18708 1 268 . 1 1 82 82 GLY N N 15 97.322 0.1 . 1 . 265 . . 82 GLY N . 18708 1 269 . 1 1 83 83 ASP H H 1 7.127 0.05 . 1 . 270 . . 83 ASP H . 18708 1 270 . 1 1 83 83 ASP C C 13 168.737 0.1 . 1 . 272 . . 83 ASP C . 18708 1 271 . 1 1 83 83 ASP CA C 13 52.918 0.1 . 1 . 271 . . 83 ASP CA . 18708 1 272 . 1 1 83 83 ASP N N 15 120.890 0.1 . 1 . 269 . . 83 ASP N . 18708 1 273 . 1 1 84 84 LEU H H 1 7.128 0.05 . 1 . 274 . . 84 LEU H . 18708 1 274 . 1 1 84 84 LEU C C 13 173.212 0.1 . 1 . 276 . . 84 LEU C . 18708 1 275 . 1 1 84 84 LEU CA C 13 50.433 0.1 . 1 . 275 . . 84 LEU CA . 18708 1 276 . 1 1 84 84 LEU N N 15 120.154 0.1 . 1 . 273 . . 84 LEU N . 18708 1 277 . 1 1 85 85 GLY H H 1 8.260 0.05 . 1 . 278 . . 85 GLY H . 18708 1 278 . 1 1 85 85 GLY C C 13 167.654 0.1 . 1 . 280 . . 85 GLY C . 18708 1 279 . 1 1 85 85 GLY CA C 13 43.011 0.1 . 1 . 279 . . 85 GLY CA . 18708 1 280 . 1 1 85 85 GLY N N 15 106.867 0.1 . 1 . 277 . . 85 GLY N . 18708 1 281 . 1 1 86 86 ASN H H 1 8.041 0.05 . 1 . 282 . . 86 ASN H . 18708 1 282 . 1 1 86 86 ASN C C 13 173.942 0.1 . 1 . 284 . . 86 ASN C . 18708 1 283 . 1 1 86 86 ASN CA C 13 49.266 0.1 . 1 . 283 . . 86 ASN CA . 18708 1 284 . 1 1 86 86 ASN N N 15 117.454 0.1 . 1 . 281 . . 86 ASN N . 18708 1 285 . 1 1 87 87 VAL H H 1 8.960 0.05 . 1 . 286 . . 87 VAL H . 18708 1 286 . 1 1 87 87 VAL C C 13 171.526 0.1 . 1 . 288 . . 87 VAL C . 18708 1 287 . 1 1 87 87 VAL CA C 13 55.708 0.1 . 1 . 287 . . 87 VAL CA . 18708 1 288 . 1 1 87 87 VAL N N 15 113.370 0.1 . 1 . 285 . . 87 VAL N . 18708 1 289 . 1 1 88 88 THR H H 1 8.681 0.05 . 1 . 290 . . 88 THR H . 18708 1 290 . 1 1 88 88 THR C C 13 170.367 0.1 . 1 . 292 . . 88 THR C . 18708 1 291 . 1 1 88 88 THR CA C 13 58.694 0.1 . 1 . 291 . . 88 THR CA . 18708 1 292 . 1 1 88 88 THR N N 15 117.939 0.1 . 1 . 289 . . 88 THR N . 18708 1 293 . 1 1 89 89 ALA H H 1 9.377 0.05 . 1 . 294 . . 89 ALA H . 18708 1 294 . 1 1 89 89 ALA C C 13 174.480 0.1 . 1 . 296 . . 89 ALA C . 18708 1 295 . 1 1 89 89 ALA CA C 13 46.369 0.1 . 1 . 295 . . 89 ALA CA . 18708 1 296 . 1 1 89 89 ALA N N 15 128.674 0.1 . 1 . 293 . . 89 ALA N . 18708 1 297 . 1 1 90 90 ASP H H 1 8.455 0.05 . 1 . 298 . . 90 ASP H . 18708 1 298 . 1 1 90 90 ASP C C 13 173.825 0.1 . 1 . 300 . . 90 ASP C . 18708 1 299 . 1 1 90 90 ASP CA C 13 49.347 0.1 . 1 . 299 . . 90 ASP CA . 18708 1 300 . 1 1 90 90 ASP N N 15 124.235 0.1 . 1 . 297 . . 90 ASP N . 18708 1 301 . 1 1 91 91 LYS H H 1 8.231 0.05 . 1 . 302 . . 91 LYS H . 18708 1 302 . 1 1 91 91 LYS C C 13 174.101 0.1 . 1 . 304 . . 91 LYS C . 18708 1 303 . 1 1 91 91 LYS CA C 13 55.279 0.1 . 1 . 303 . . 91 LYS CA . 18708 1 304 . 1 1 91 91 LYS N N 15 114.942 0.1 . 1 . 301 . . 91 LYS N . 18708 1 305 . 1 1 92 92 ASP H H 1 8.109 0.05 . 1 . 306 . . 92 ASP H . 18708 1 306 . 1 1 92 92 ASP C C 13 173.020 0.1 . 1 . 308 . . 92 ASP C . 18708 1 307 . 1 1 92 92 ASP CA C 13 51.127 0.1 . 1 . 307 . . 92 ASP CA . 18708 1 308 . 1 1 92 92 ASP N N 15 119.251 0.1 . 1 . 305 . . 92 ASP N . 18708 1 309 . 1 1 93 93 GLY H H 1 8.405 0.05 . 1 . 310 . . 93 GLY H . 18708 1 310 . 1 1 93 93 GLY C C 13 169.706 0.1 . 1 . 312 . . 93 GLY C . 18708 1 311 . 1 1 93 93 GLY CA C 13 43.763 0.1 . 1 . 311 . . 93 GLY CA . 18708 1 312 . 1 1 93 93 GLY N N 15 110.868 0.1 . 1 . 309 . . 93 GLY N . 18708 1 313 . 1 1 94 94 VAL H H 1 7.814 0.05 . 1 . 314 . . 94 VAL H . 18708 1 314 . 1 1 94 94 VAL C C 13 173.510 0.1 . 1 . 316 . . 94 VAL C . 18708 1 315 . 1 1 94 94 VAL CA C 13 58.185 0.1 . 1 . 315 . . 94 VAL CA . 18708 1 316 . 1 1 94 94 VAL N N 15 118.755 0.1 . 1 . 313 . . 94 VAL N . 18708 1 317 . 1 1 95 95 ALA H H 1 9.763 0.05 . 1 . 318 . . 95 ALA H . 18708 1 318 . 1 1 95 95 ALA C C 13 171.635 0.1 . 1 . 320 . . 95 ALA C . 18708 1 319 . 1 1 95 95 ALA CA C 13 46.914 0.1 . 1 . 319 . . 95 ALA CA . 18708 1 320 . 1 1 95 95 ALA N N 15 131.313 0.1 . 1 . 317 . . 95 ALA N . 18708 1 321 . 1 1 96 96 ASP H H 1 8.515 0.05 . 1 . 322 . . 96 ASP H . 18708 1 322 . 1 1 96 96 ASP C C 13 172.336 0.1 . 1 . 323 . . 96 ASP C . 18708 1 323 . 1 1 96 96 ASP N N 15 125.170 0.1 . 1 . 321 . . 96 ASP N . 18708 1 324 . 1 1 97 97 VAL H H 1 8.703 0.05 . 1 . 325 . . 97 VAL H . 18708 1 325 . 1 1 97 97 VAL C C 13 173.488 0.1 . 1 . 327 . . 97 VAL C . 18708 1 326 . 1 1 97 97 VAL CA C 13 58.243 0.1 . 1 . 326 . . 97 VAL CA . 18708 1 327 . 1 1 97 97 VAL N N 15 125.879 0.1 . 1 . 324 . . 97 VAL N . 18708 1 328 . 1 1 98 98 SER H H 1 8.784 0.05 . 1 . 329 . . 98 SER H . 18708 1 329 . 1 1 98 98 SER C C 13 169.715 0.1 . 1 . 331 . . 98 SER C . 18708 1 330 . 1 1 98 98 SER CA C 13 55.068 0.1 . 1 . 330 . . 98 SER CA . 18708 1 331 . 1 1 98 98 SER N N 15 123.017 0.1 . 1 . 328 . . 98 SER N . 18708 1 332 . 1 1 99 99 ILE H H 1 9.411 0.05 . 1 . 333 . . 99 ILE H . 18708 1 333 . 1 1 99 99 ILE C C 13 171.321 0.1 . 1 . 335 . . 99 ILE C . 18708 1 334 . 1 1 99 99 ILE CA C 13 57.155 0.1 . 1 . 334 . . 99 ILE CA . 18708 1 335 . 1 1 99 99 ILE N N 15 125.807 0.1 . 1 . 332 . . 99 ILE N . 18708 1 336 . 1 1 100 100 GLU H H 1 8.652 0.05 . 1 . 337 . . 100 GLU H . 18708 1 337 . 1 1 100 100 GLU C C 13 172.098 0.1 . 1 . 339 . . 100 GLU C . 18708 1 338 . 1 1 100 100 GLU CA C 13 52.290 0.1 . 1 . 338 . . 100 GLU CA . 18708 1 339 . 1 1 100 100 GLU N N 15 124.068 0.1 . 1 . 336 . . 100 GLU N . 18708 1 340 . 1 1 101 101 ASP H H 1 9.317 0.05 . 1 . 341 . . 101 ASP H . 18708 1 341 . 1 1 101 101 ASP C C 13 171.144 0.1 . 1 . 343 . . 101 ASP C . 18708 1 342 . 1 1 101 101 ASP CA C 13 51.419 0.1 . 1 . 342 . . 101 ASP CA . 18708 1 343 . 1 1 101 101 ASP N N 15 126.109 0.1 . 1 . 340 . . 101 ASP N . 18708 1 344 . 1 1 102 102 SER H H 1 8.933 0.05 . 1 . 345 . . 102 SER H . 18708 1 345 . 1 1 102 102 SER C C 13 171.596 0.1 . 1 . 347 . . 102 SER C . 18708 1 346 . 1 1 102 102 SER CA C 13 55.245 0.1 . 1 . 346 . . 102 SER CA . 18708 1 347 . 1 1 102 102 SER N N 15 118.470 0.1 . 1 . 344 . . 102 SER N . 18708 1 348 . 1 1 103 103 VAL H H 1 8.148 0.05 . 1 . 349 . . 103 VAL H . 18708 1 349 . 1 1 103 103 VAL CA C 13 61.450 0.1 . 1 . 350 . . 103 VAL CA . 18708 1 350 . 1 1 103 103 VAL N N 15 123.179 0.1 . 1 . 348 . . 103 VAL N . 18708 1 351 . 1 1 104 104 ILE C C 13 169.576 0.1 . 1 . 352 . . 104 ILE C . 18708 1 352 . 1 1 104 104 ILE CA C 13 60.194 0.1 . 1 . 351 . . 104 ILE CA . 18708 1 353 . 1 1 105 105 SER H H 1 6.988 0.05 . 1 . 354 . . 105 SER H . 18708 1 354 . 1 1 105 105 SER C C 13 170.046 0.1 . 1 . 356 . . 105 SER C . 18708 1 355 . 1 1 105 105 SER CA C 13 52.550 0.1 . 1 . 355 . . 105 SER CA . 18708 1 356 . 1 1 105 105 SER N N 15 107.618 0.1 . 1 . 353 . . 105 SER N . 18708 1 357 . 1 1 106 106 LEU H H 1 8.313 0.05 . 1 . 358 . . 106 LEU H . 18708 1 358 . 1 1 106 106 LEU N N 15 120.137 0.1 . 1 . 357 . . 106 LEU N . 18708 1 359 . 1 1 107 107 SER C C 13 170.701 0.1 . 1 . 360 . . 107 SER C . 18708 1 360 . 1 1 107 107 SER CA C 13 54.540 0.1 . 1 . 359 . . 107 SER CA . 18708 1 361 . 1 1 108 108 GLY H H 1 8.717 0.05 . 1 . 362 . . 108 GLY H . 18708 1 362 . 1 1 108 108 GLY C C 13 173.128 0.1 . 1 . 364 . . 108 GLY C . 18708 1 363 . 1 1 108 108 GLY CA C 13 41.287 0.1 . 1 . 363 . . 108 GLY CA . 18708 1 364 . 1 1 108 108 GLY N N 15 107.603 0.1 . 1 . 361 . . 108 GLY N . 18708 1 365 . 1 1 109 109 ASP H H 1 9.019 0.05 . 1 . 366 . . 109 ASP H . 18708 1 366 . 1 1 109 109 ASP C C 13 171.904 0.1 . 1 . 367 . . 109 ASP C . 18708 1 367 . 1 1 109 109 ASP N N 15 120.664 0.1 . 1 . 365 . . 109 ASP N . 18708 1 368 . 1 1 110 110 HIS H H 1 9.283 0.05 . 1 . 369 . . 110 HIS H . 18708 1 369 . 1 1 110 110 HIS N N 15 116.324 0.1 . 1 . 368 . . 110 HIS N . 18708 1 370 . 1 1 111 111 SER H H 1 7.156 0.05 . 1 . 371 . . 111 SER H . 18708 1 371 . 1 1 111 111 SER CA C 13 54.681 0.1 . 1 . 372 . . 111 SER CA . 18708 1 372 . 1 1 111 111 SER N N 15 110.225 0.1 . 1 . 370 . . 111 SER N . 18708 1 373 . 1 1 112 112 ILE H H 1 7.837 0.05 . 1 . 374 . . 112 ILE H . 18708 1 374 . 1 1 112 112 ILE C C 13 171.419 0.1 . 1 . 376 . . 112 ILE C . 18708 1 375 . 1 1 112 112 ILE CA C 13 57.239 0.1 . 1 . 375 . . 112 ILE CA . 18708 1 376 . 1 1 112 112 ILE N N 15 117.053 0.1 . 1 . 373 . . 112 ILE N . 18708 1 377 . 1 1 113 113 ILE H H 1 7.592 0.05 . 1 . 378 . . 113 ILE H . 18708 1 378 . 1 1 113 113 ILE C C 13 173.604 0.1 . 1 . 380 . . 113 ILE C . 18708 1 379 . 1 1 113 113 ILE CA C 13 58.318 0.1 . 1 . 379 . . 113 ILE CA . 18708 1 380 . 1 1 113 113 ILE N N 15 121.032 0.1 . 1 . 377 . . 113 ILE N . 18708 1 381 . 1 1 114 114 GLY H H 1 9.575 0.05 . 1 . 382 . . 114 GLY H . 18708 1 382 . 1 1 114 114 GLY C C 13 169.739 0.1 . 1 . 384 . . 114 GLY C . 18708 1 383 . 1 1 114 114 GLY CA C 13 41.910 0.1 . 1 . 383 . . 114 GLY CA . 18708 1 384 . 1 1 114 114 GLY N N 15 112.661 0.1 . 1 . 381 . . 114 GLY N . 18708 1 385 . 1 1 115 115 ARG H H 1 7.464 0.05 . 1 . 386 . . 115 ARG H . 18708 1 386 . 1 1 115 115 ARG C C 13 171.079 0.1 . 1 . 388 . . 115 ARG C . 18708 1 387 . 1 1 115 115 ARG CA C 13 51.663 0.1 . 1 . 387 . . 115 ARG CA . 18708 1 388 . 1 1 115 115 ARG N N 15 118.398 0.1 . 1 . 385 . . 115 ARG N . 18708 1 389 . 1 1 116 116 THR H H 1 6.677 0.05 . 1 . 390 . . 116 THR H . 18708 1 390 . 1 1 116 116 THR C C 13 169.821 0.1 . 1 . 392 . . 116 THR C . 18708 1 391 . 1 1 116 116 THR CA C 13 59.633 0.1 . 1 . 391 . . 116 THR CA . 18708 1 392 . 1 1 116 116 THR N N 15 112.218 0.1 . 1 . 389 . . 116 THR N . 18708 1 393 . 1 1 117 117 LEU H H 1 8.799 0.05 . 1 . 394 . . 117 LEU H . 18708 1 394 . 1 1 117 117 LEU C C 13 171.126 0.1 . 1 . 396 . . 117 LEU C . 18708 1 395 . 1 1 117 117 LEU CA C 13 50.415 0.1 . 1 . 395 . . 117 LEU CA . 18708 1 396 . 1 1 117 117 LEU N N 15 129.477 0.1 . 1 . 393 . . 117 LEU N . 18708 1 397 . 1 1 118 118 VAL H H 1 8.906 0.05 . 1 . 398 . . 118 VAL H . 18708 1 398 . 1 1 118 118 VAL C C 13 170.267 0.1 . 1 . 400 . . 118 VAL C . 18708 1 399 . 1 1 118 118 VAL CA C 13 58.139 0.1 . 1 . 399 . . 118 VAL CA . 18708 1 400 . 1 1 118 118 VAL N N 15 125.091 0.1 . 1 . 397 . . 118 VAL N . 18708 1 401 . 1 1 119 119 VAL H H 1 7.982 0.05 . 1 . 402 . . 119 VAL H . 18708 1 402 . 1 1 119 119 VAL C C 13 171.175 0.1 . 1 . 404 . . 119 VAL C . 18708 1 403 . 1 1 119 119 VAL CA C 13 55.271 0.1 . 1 . 403 . . 119 VAL CA . 18708 1 404 . 1 1 119 119 VAL N N 15 120.716 0.1 . 1 . 401 . . 119 VAL N . 18708 1 405 . 1 1 120 120 HIS H H 1 8.935 0.05 . 1 . 406 . . 120 HIS H . 18708 1 406 . 1 1 120 120 HIS C C 13 172.599 0.1 . 1 . 408 . . 120 HIS C . 18708 1 407 . 1 1 120 120 HIS CA C 13 53.394 0.1 . 1 . 407 . . 120 HIS CA . 18708 1 408 . 1 1 120 120 HIS N N 15 125.052 0.1 . 1 . 405 . . 120 HIS N . 18708 1 409 . 1 1 121 121 GLU H H 1 9.178 0.05 . 1 . 410 . . 121 GLU H . 18708 1 410 . 1 1 121 121 GLU C C 13 172.304 0.1 . 1 . 412 . . 121 GLU C . 18708 1 411 . 1 1 121 121 GLU CA C 13 56.090 0.1 . 1 . 411 . . 121 GLU CA . 18708 1 412 . 1 1 121 121 GLU N N 15 121.453 0.1 . 1 . 409 . . 121 GLU N . 18708 1 413 . 1 1 122 122 LYS H H 1 8.478 0.05 . 1 . 414 . . 122 LYS H . 18708 1 414 . 1 1 122 122 LYS C C 13 171.523 0.1 . 1 . 416 . . 122 LYS C . 18708 1 415 . 1 1 122 122 LYS CA C 13 50.619 0.1 . 1 . 415 . . 122 LYS CA . 18708 1 416 . 1 1 122 122 LYS N N 15 115.248 0.1 . 1 . 413 . . 122 LYS N . 18708 1 417 . 1 1 123 123 ALA H H 1 7.796 0.05 . 1 . 418 . . 123 ALA H . 18708 1 418 . 1 1 123 123 ALA C C 13 173.219 0.1 . 1 . 420 . . 123 ALA C . 18708 1 419 . 1 1 123 123 ALA CA C 13 48.850 0.1 . 1 . 419 . . 123 ALA CA . 18708 1 420 . 1 1 123 123 ALA N N 15 120.866 0.1 . 1 . 417 . . 123 ALA N . 18708 1 421 . 1 1 124 124 ASP H H 1 10.165 0.05 . 1 . 422 . . 124 ASP H . 18708 1 422 . 1 1 124 124 ASP C C 13 174.458 0.1 . 1 . 424 . . 124 ASP C . 18708 1 423 . 1 1 124 124 ASP CA C 13 49.408 0.1 . 1 . 423 . . 124 ASP CA . 18708 1 424 . 1 1 124 124 ASP N N 15 121.799 0.1 . 1 . 421 . . 124 ASP N . 18708 1 425 . 1 1 125 125 ASP H H 1 10.055 0.05 . 1 . 426 . . 125 ASP H . 18708 1 426 . 1 1 125 125 ASP C C 13 175.231 0.1 . 1 . 428 . . 125 ASP C . 18708 1 427 . 1 1 125 125 ASP CA C 13 50.939 0.1 . 1 . 427 . . 125 ASP CA . 18708 1 428 . 1 1 125 125 ASP N N 15 129.369 0.1 . 1 . 425 . . 125 ASP N . 18708 1 429 . 1 1 126 126 LEU H H 1 10.483 0.05 . 1 . 430 . . 126 LEU H . 18708 1 430 . 1 1 126 126 LEU C C 13 173.964 0.1 . 1 . 431 . . 126 LEU C . 18708 1 431 . 1 1 126 126 LEU N N 15 117.190 0.1 . 1 . 429 . . 126 LEU N . 18708 1 432 . 1 1 127 127 GLY H H 1 8.637 0.05 . 1 . 433 . . 127 GLY H . 18708 1 433 . 1 1 127 127 GLY CA C 13 42.878 0.1 . 1 . 434 . . 127 GLY CA . 18708 1 434 . 1 1 127 127 GLY N N 15 103.809 0.1 . 1 . 432 . . 127 GLY N . 18708 1 435 . 1 1 128 128 LYS H H 1 7.158 0.05 . 1 . 436 . . 128 LYS H . 18708 1 436 . 1 1 128 128 LYS CA C 13 51.740 0.1 . 1 . 437 . . 128 LYS CA . 18708 1 437 . 1 1 128 128 LYS N N 15 118.290 0.1 . 1 . 435 . . 128 LYS N . 18708 1 438 . 1 1 129 129 GLY H H 1 8.913 0.05 . 1 . 439 . . 129 GLY H . 18708 1 439 . 1 1 129 129 GLY C C 13 171.524 0.1 . 1 . 441 . . 129 GLY C . 18708 1 440 . 1 1 129 129 GLY CA C 13 42.113 0.1 . 1 . 440 . . 129 GLY CA . 18708 1 441 . 1 1 129 129 GLY N N 15 108.507 0.1 . 1 . 438 . . 129 GLY N . 18708 1 442 . 1 1 130 130 GLY H H 1 8.723 0.05 . 1 . 443 . . 130 GLY H . 18708 1 443 . 1 1 130 130 GLY C C 13 169.994 0.1 . 1 . 445 . . 130 GLY C . 18708 1 444 . 1 1 130 130 GLY CA C 13 42.419 0.1 . 1 . 444 . . 130 GLY CA . 18708 1 445 . 1 1 130 130 GLY N N 15 108.537 0.1 . 1 . 442 . . 130 GLY N . 18708 1 446 . 1 1 131 131 ASN H H 1 7.152 0.05 . 1 . 447 . . 131 ASN H . 18708 1 447 . 1 1 131 131 ASN C C 13 172.236 0.1 . 1 . 448 . . 131 ASN C . 18708 1 448 . 1 1 131 131 ASN N N 15 111.951 0.1 . 1 . 446 . . 131 ASN N . 18708 1 449 . 1 1 132 132 GLU H H 1 8.935 0.05 . 1 . 450 . . 132 GLU H . 18708 1 450 . 1 1 132 132 GLU C C 13 171.084 0.1 . 1 . 451 . . 132 GLU C . 18708 1 451 . 1 1 132 132 GLU N N 15 120.461 0.1 . 1 . 449 . . 132 GLU N . 18708 1 452 . 1 1 133 133 GLU H H 1 8.775 0.05 . 1 . 453 . . 133 GLU H . 18708 1 453 . 1 1 133 133 GLU C C 13 176.239 0.1 . 1 . 454 . . 133 GLU C . 18708 1 454 . 1 1 133 133 GLU N N 15 120.137 0.1 . 1 . 452 . . 133 GLU N . 18708 1 455 . 1 1 134 134 SER H H 1 8.117 0.05 . 1 . 456 . . 134 SER H . 18708 1 456 . 1 1 134 134 SER CA C 13 59.046 0.1 . 1 . 457 . . 134 SER CA . 18708 1 457 . 1 1 134 134 SER N N 15 114.981 0.1 . 1 . 455 . . 134 SER N . 18708 1 458 . 1 1 135 135 THR H H 1 7.206 0.05 . 1 . 459 . . 135 THR H . 18708 1 459 . 1 1 135 135 THR C C 13 172.804 0.1 . 1 . 461 . . 135 THR C . 18708 1 460 . 1 1 135 135 THR CA C 13 60.029 0.1 . 1 . 460 . . 135 THR CA . 18708 1 461 . 1 1 135 135 THR N N 15 102.263 0.1 . 1 . 458 . . 135 THR N . 18708 1 462 . 1 1 136 136 LYS H H 1 7.884 0.05 . 1 . 463 . . 136 LYS H . 18708 1 463 . 1 1 136 136 LYS N N 15 122.108 0.1 . 1 . 462 . . 136 LYS N . 18708 1 464 . 1 1 137 137 THR H H 1 8.630 0.05 . 1 . 465 . . 137 THR H . 18708 1 465 . 1 1 137 137 THR N N 15 105.718 0.1 . 1 . 464 . . 137 THR N . 18708 1 466 . 1 1 138 138 GLY H H 1 7.426 0.05 . 1 . 467 . . 138 GLY H . 18708 1 467 . 1 1 138 138 GLY CA C 13 42.483 0.1 . 1 . 468 . . 138 GLY CA . 18708 1 468 . 1 1 138 138 GLY N N 15 111.372 0.1 . 1 . 466 . . 138 GLY N . 18708 1 469 . 1 1 139 139 ASN H H 1 7.545 0.05 . 1 . 470 . . 139 ASN H . 18708 1 470 . 1 1 139 139 ASN N N 15 107.496 0.1 . 1 . 469 . . 139 ASN N . 18708 1 471 . 1 1 140 140 ALA H H 1 6.368 0.05 . 1 . 472 . . 140 ALA H . 18708 1 472 . 1 1 140 140 ALA C C 13 173.571 0.1 . 1 . 473 . . 140 ALA C . 18708 1 473 . 1 1 140 140 ALA N N 15 114.542 0.1 . 1 . 471 . . 140 ALA N . 18708 1 474 . 1 1 141 141 GLY H H 1 8.271 0.05 . 1 . 475 . . 141 GLY H . 18708 1 475 . 1 1 141 141 GLY C C 13 173.542 0.1 . 1 . 476 . . 141 GLY C . 18708 1 476 . 1 1 141 141 GLY N N 15 105.287 0.1 . 1 . 474 . . 141 GLY N . 18708 1 477 . 1 1 142 142 SER H H 1 9.196 0.05 . 1 . 478 . . 142 SER H . 18708 1 478 . 1 1 142 142 SER C C 13 170.188 0.1 . 1 . 479 . . 142 SER C . 18708 1 479 . 1 1 142 142 SER N N 15 118.771 0.1 . 1 . 477 . . 142 SER N . 18708 1 480 . 1 1 143 143 ARG H H 1 8.943 0.05 . 1 . 481 . . 143 ARG H . 18708 1 481 . 1 1 143 143 ARG C C 13 171.596 0.1 . 1 . 482 . . 143 ARG C . 18708 1 482 . 1 1 143 143 ARG N N 15 120.189 0.1 . 1 . 480 . . 143 ARG N . 18708 1 483 . 1 1 144 144 LEU H H 1 8.395 0.05 . 1 . 484 . . 144 LEU H . 18708 1 484 . 1 1 144 144 LEU C C 13 174.393 0.1 . 1 . 486 . . 144 LEU C . 18708 1 485 . 1 1 144 144 LEU CA C 13 53.375 0.1 . 1 . 485 . . 144 LEU CA . 18708 1 486 . 1 1 144 144 LEU N N 15 122.907 0.1 . 1 . 483 . . 144 LEU N . 18708 1 487 . 1 1 145 145 ALA H H 1 7.356 0.05 . 1 . 488 . . 145 ALA H . 18708 1 488 . 1 1 145 145 ALA C C 13 171.752 0.1 . 1 . 490 . . 145 ALA C . 18708 1 489 . 1 1 145 145 ALA CA C 13 48.129 0.1 . 1 . 489 . . 145 ALA CA . 18708 1 490 . 1 1 145 145 ALA N N 15 114.159 0.1 . 1 . 487 . . 145 ALA N . 18708 1 491 . 1 1 146 146 CYS H H 1 9.008 0.05 . 1 . 492 . . 146 CYS H . 18708 1 492 . 1 1 146 146 CYS C C 13 170.087 0.1 . 1 . 494 . . 146 CYS C . 18708 1 493 . 1 1 146 146 CYS CA C 13 51.077 0.1 . 1 . 493 . . 146 CYS CA . 18708 1 494 . 1 1 146 146 CYS N N 15 110.738 0.1 . 1 . 491 . . 146 CYS N . 18708 1 495 . 1 1 147 147 GLY H H 1 8.018 0.05 . 1 . 496 . . 147 GLY H . 18708 1 496 . 1 1 147 147 GLY C C 13 167.909 0.1 . 1 . 498 . . 147 GLY C . 18708 1 497 . 1 1 147 147 GLY CA C 13 42.674 0.1 . 1 . 497 . . 147 GLY CA . 18708 1 498 . 1 1 147 147 GLY N N 15 106.461 0.1 . 1 . 495 . . 147 GLY N . 18708 1 499 . 1 1 148 148 VAL H H 1 8.434 0.05 . 1 . 500 . . 148 VAL H . 18708 1 500 . 1 1 148 148 VAL C C 13 172.084 0.1 . 1 . 502 . . 148 VAL C . 18708 1 501 . 1 1 148 148 VAL CA C 13 59.635 0.1 . 1 . 501 . . 148 VAL CA . 18708 1 502 . 1 1 148 148 VAL N N 15 124.054 0.1 . 1 . 499 . . 148 VAL N . 18708 1 503 . 1 1 149 149 ILE H H 1 8.613 0.05 . 1 . 504 . . 149 ILE H . 18708 1 504 . 1 1 149 149 ILE C C 13 171.804 0.1 . 1 . 506 . . 149 ILE C . 18708 1 505 . 1 1 149 149 ILE CA C 13 59.184 0.1 . 1 . 505 . . 149 ILE CA . 18708 1 506 . 1 1 149 149 ILE N N 15 126.918 0.1 . 1 . 503 . . 149 ILE N . 18708 1 507 . 1 1 150 150 GLY H H 1 9.283 0.05 . 1 . 508 . . 150 GLY H . 18708 1 508 . 1 1 150 150 GLY C C 13 170.188 0.1 . 1 . 510 . . 150 GLY C . 18708 1 509 . 1 1 150 150 GLY CA C 13 40.120 0.1 . 1 . 509 . . 150 GLY CA . 18708 1 510 . 1 1 150 150 GLY N N 15 116.493 0.1 . 1 . 507 . . 150 GLY N . 18708 1 511 . 1 1 151 151 ILE H H 1 8.943 0.05 . 1 . 512 . . 151 ILE H . 18708 1 512 . 1 1 151 151 ILE C C 13 172.231 0.1 . 1 . 514 . . 151 ILE C . 18708 1 513 . 1 1 151 151 ILE CA C 13 60.372 0.1 . 1 . 513 . . 151 ILE CA . 18708 1 514 . 1 1 151 151 ILE N N 15 120.189 0.1 . 1 . 511 . . 151 ILE N . 18708 1 515 . 1 1 152 152 ALA H H 1 8.170 0.05 . 1 . 516 . . 152 ALA H . 18708 1 516 . 1 1 152 152 ALA CA C 13 46.772 0.1 . 1 . 517 . . 152 ALA CA . 18708 1 517 . 1 1 152 152 ALA N N 15 129.719 0.1 . 1 . 515 . . 152 ALA N . 18708 1 stop_ save_