data_813 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 813 _Entry.Title ; Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-04-12 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Lucia Banci . . . 813 2 Ivano Bertini . . . 813 3 Diane Cabelli . . . 813 4 Robert Hallewell . A. . 813 5 Claudio Luchinat . . . 813 6 Maria Viezzoli . Silvia . 813 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 813 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 16 813 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 6 . . 2010-06-11 . revision BMRB 'Complete natural source information' 813 5 . . 2008-09-30 . revision BMRB 'Updating non-standard residue' 813 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 813 3 . . 1996-04-12 . revision BMRB 'Error corrected in abrreviations given to non-polymers' 813 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 813 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 813 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 813 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Banci, Lucia, Bertini, Ivano, Cabelli, Diane, Hallewell, Robert A., Luchinat, Claudio, Viezzoli, Maria Silvia, "Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants," Inorg. Chem. 29, 2398-2403 (1990). ; _Citation.Title 'Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Inorg. Chem.' _Citation.Journal_name_full . _Citation.Journal_volume 29 _Citation.Journal_issue . _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 2398 _Citation.Page_last 2403 _Citation.Year 1990 _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 Lucia Banci . . . 813 1 2 Ivano Bertini . . . 813 1 3 Diane Cabelli . . . 813 1 4 Robert Hallewell . A. . 813 1 5 Claudio Luchinat . . . 813 1 6 Maria Viezzoli . Silvia . 813 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_copper-zinc_superoxide_dismutase _Assembly.Sf_category assembly _Assembly.Sf_framecode system_copper-zinc_superoxide_dismutase _Assembly.Entry_ID 813 _Assembly.ID 1 _Assembly.Name 'copper-zinc superoxide dismutase' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'copper-zinc superoxide dismutase' 1 $copper-zinc_superoxide_dismutase . . . . . . . . . 813 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'copper-zinc superoxide dismutase' system 813 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_copper-zinc_superoxide_dismutase _Entity.Sf_category entity _Entity.Sf_framecode copper-zinc_superoxide_dismutase _Entity.Entry_ID 813 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'copper-zinc superoxide dismutase' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; XTKAVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIE DSVISLSGDHSIIGRTLVVH EKADDLGKGGNEESTKAGNA GSRLACGVIGIAQ ; _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 . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 153 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 15711 . SOD1 . . . . . 99.35 153 97.37 98.03 5.71e-99 . . . . 813 1 2 no BMRB 18509 . Superoxide_dismutase_C6A-C111S_thermostable_mutant . . . . . 99.35 153 99.34 99.34 5.67e-102 . . . . 813 1 3 no BMRB 18708 . SUPEROXIDE_DISMUTASE_CU-ZN . . . . . 99.35 153 99.34 99.34 5.67e-102 . . . . 813 1 4 no BMRB 4202 . Q133M2_SOD . . . . . 99.35 153 97.37 98.03 4.84e-99 . . . . 813 1 5 no BMRB 6821 . dismutase . . . . . 99.35 153 99.34 99.34 5.67e-102 . . . . 813 1 6 no BMRB 814 . copper-zinc_superoxide_dismutase . . . . . 99.35 153 99.34 99.34 9.89e-102 . . . . 813 1 7 no PDB 1AZV . "Familial Als Mutant G37r Cuznsod (Human)" . . . . . 99.35 153 97.37 97.37 1.94e-99 . . . . 813 1 8 no PDB 1BA9 . "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" . . . . . 99.35 153 97.37 98.03 5.00e-99 . . . . 813 1 9 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)" . . . . . 99.35 153 98.68 99.34 2.64e-101 . . . . 813 1 10 no PDB 1HL4 . "The Structure Of Apo Type Human Cu, Zn Superoxide Dismutase" . . . . . 99.35 154 98.03 98.03 1.87e-100 . . . . 813 1 11 no PDB 1HL5 . "The Structure Of Holo Type Human Cu, Zn Superoxide Dismutase" . . . . . 99.35 153 98.03 98.03 1.81e-100 . . . . 813 1 12 no PDB 1KMG . "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" . . . . . 99.35 153 97.37 98.03 4.84e-99 . . . . 813 1 13 no PDB 1L3N . "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" . . . . . 99.35 153 99.34 99.34 5.67e-102 . . . . 813 1 14 no PDB 1MFM . "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" . . . . . 99.35 153 97.37 98.03 4.84e-99 . . . . 813 1 15 no PDB 1N18 . "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" . . . . . 99.35 154 99.34 99.34 5.55e-102 . . . . 813 1 16 no PDB 1N19 . "Structure Of The Hsod A4v Mutant" . . . . . 99.35 154 98.68 98.68 2.76e-101 . . . . 813 1 17 no PDB 1OEZ . "Zn His46arg Mutant Of Human Cu, Zn Superoxide Dismutase" . . . . . 99.35 153 97.37 97.37 1.89e-99 . . . . 813 1 18 no PDB 1OZT . "Crystal Structure Of Apo-H46r Familial Als Mutant Human Cu, Zn Superoxide Dismutase (Cuznsod) To 2.5a Resolution" . . . . . 99.35 153 97.37 97.37 1.89e-99 . . . . 813 1 19 no PDB 1OZU . "Crystal Structure Of Familial Als Mutant S134n Of Human Cu, Zn Superoxide Dismutase (Cuznsod) To 1.3a Resolution" . . . . . 99.35 153 97.37 98.03 8.53e-100 . . . . 813 1 20 no PDB 1P1V . "Crystal Structure Of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125h To 1.4a" . . . . . 99.35 153 97.37 97.37 3.89e-99 . . . . 813 1 21 no PDB 1PTZ . "Crystal Structure Of The Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43r" . . . . . 99.35 153 98.68 98.68 5.68e-101 . . . . 813 1 22 no PDB 1PU0 . "Structure Of Human Cu,Zn Superoxide Dismutase" . . . . . 99.35 153 98.03 98.03 1.81e-100 . . . . 813 1 23 no PDB 1RK7 . "Solution Structure Of Apo Cu,Zn Superoxide Dismutase: Role Of Metal Ions In Protein Folding" . . . . . 99.35 153 97.37 98.03 4.84e-99 . . . . 813 1 24 no PDB 1SOS . "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" . . . . . 99.35 154 99.34 99.34 5.86e-102 . . . . 813 1 25 no PDB 1SPD . "Amyotrophic Lateral Sclerosis And Structural Defects In Cu,Zn Superoxide Dismutase" . . . . . 99.35 154 98.03 98.03 1.87e-100 . . . . 813 1 26 no PDB 1UXL . "I113t Mutant Of Human Sod1" . . . . . 99.35 153 97.37 97.37 9.31e-100 . . . . 813 1 27 no PDB 1UXM . "A4v Mutant Of Human Sod1" . . . . . 99.35 153 97.37 97.37 1.13e-99 . . . . 813 1 28 no PDB 2AF2 . "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" . . . . . 99.35 153 99.34 99.34 5.67e-102 . . . . 813 1 29 no PDB 2C9S . "1.24 Angstroms Resolution Structure Of Zn-Zn Human Superoxide Dismutase" . . . . . 99.35 153 98.03 98.03 2.11e-100 . . . . 813 1 30 no PDB 2C9U . "1.24 Angstroms Resolution Structure Of As-Isolated Cu-Zn Human Superoxide Dismutase" . . . . . 99.35 153 98.03 98.03 1.81e-100 . . . . 813 1 31 no PDB 2C9V . "Atomic Resolution Structure Of Cu-Zn Human Superoxide Dismutase" . . . . . 99.35 153 98.03 98.03 1.81e-100 . . . . 813 1 32 no PDB 2GBT . "C6aC111A CUZN SUPEROXIDE DISMUTASE" . . . . . 99.35 153 98.68 99.34 1.69e-101 . . . . 813 1 33 no PDB 2GBU . "C6a/c111a/c57a/c146a Apo Cuzn Superoxide Dismutase" . . . . . 99.35 153 97.37 98.03 2.36e-99 . . . . 813 1 34 no PDB 2GBV . "C6aC111AC57AC146A HOLO CUZN SUPEROXIDE DISMUTASE" . . . . . 99.35 153 97.37 98.03 2.36e-99 . . . . 813 1 35 no PDB 2LU5 . "Structure And Chemical Shifts Of Cu(I),Zn(Ii) Superoxide Dismutase By Solid-State Nmr" . . . . . 99.35 153 99.34 99.34 5.67e-102 . . . . 813 1 36 no PDB 2R27 . "Constitutively Zinc-Deficient Mutant Of Human Superoxide Dismutase (Sod), C6a, H80s, H83s, C111s" . . . . . 99.35 154 98.03 98.03 2.65e-100 . . . . 813 1 37 no PDB 2V0A . "Atomic Resolution Crystal Structure Of Human Superoxide Dismutase" . . . . . 99.35 153 98.03 98.03 1.81e-100 . . . . 813 1 38 no PDB 2VR6 . "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.3 A Resolution" . . . . . 99.35 153 97.37 97.37 1.94e-99 . . . . 813 1 39 no PDB 2VR7 . "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.58 A Resolution" . . . . . 99.35 154 97.37 97.37 2.00e-99 . . . . 813 1 40 no PDB 2VR8 . "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.36 A Resolution" . . . . . 99.35 154 97.37 97.37 1.94e-99 . . . . 813 1 41 no PDB 2WKO . "Structure Of Metal Loaded Pathogenic Sod1 Mutant G93a" . . . . . 99.35 154 97.37 97.37 7.82e-100 . . . . 813 1 42 no PDB 2WYT . "1.0 A Resolution Structure Of L38v Sod1 Mutant" . . . . . 99.35 153 97.37 98.03 5.76e-100 . . . . 813 1 43 no PDB 2WYZ . "L38v Sod1 Mutant Complexed With Ump" . . . . . 99.35 153 97.37 98.03 6.71e-100 . . . . 813 1 44 no PDB 2WZ0 . "L38v Sod1 Mutant Complexed With Aniline." . . . . . 99.35 153 97.37 98.03 5.76e-100 . . . . 813 1 45 no PDB 2WZ5 . "L38v Sod1 Mutant Complexed With L-Methionine" . . . . . 99.35 153 97.37 98.03 5.76e-100 . . . . 813 1 46 no PDB 2WZ6 . "G93a Sod1 Mutant Complexed With Quinazoline" . . . . . 99.35 153 97.37 97.37 7.65e-100 . . . . 813 1 47 no PDB 2XJK . "Monomeric Human Cu,Zn Superoxide Dismutase" . . . . . 99.35 153 97.37 98.03 5.71e-99 . . . . 813 1 48 no PDB 2ZKW . "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group P21" . . . . . 99.35 159 97.37 97.37 2.58e-99 . . . . 813 1 49 no PDB 2ZKX . "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group I212121" . . . . . 99.35 159 97.37 97.37 2.58e-99 . . . . 813 1 50 no PDB 2ZKY . "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G93a" . . . . . 99.35 159 97.37 97.37 1.01e-99 . . . . 813 1 51 no PDB 3CQP . "Human Sod1 G85r Variant, Structure I" . . . . . 99.35 153 97.37 97.37 1.94e-99 . . . . 813 1 52 no PDB 3CQQ . "Human Sod1 G85r Variant, Structure Ii" . . . . . 99.35 153 97.37 97.37 1.87e-99 . . . . 813 1 53 no PDB 3ECU . "Crystal Structure Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" . . . . . 99.35 153 98.03 98.03 1.81e-100 . . . . 813 1 54 no PDB 3ECV . "Crystal Structure Of The Als-Related Pathological Mutant I113t Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" . . . . . 99.35 153 97.37 97.37 9.31e-100 . . . . 813 1 55 no PDB 3ECW . "Crystal Structure Of The Als-Related Pathological Mutant T54r Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" . . . . . 99.35 153 97.37 97.37 1.66e-99 . . . . 813 1 56 no PDB 3GZO . "Human Sod1 G93a Variant" . . . . . 99.35 154 97.37 97.37 7.91e-100 . . . . 813 1 57 no PDB 3GZP . "Human Sod1 G93a Metal-Free Variant" . . . . . 99.35 153 97.37 97.37 7.65e-100 . . . . 813 1 58 no PDB 3GZQ . "Human Sod1 A4v Metal-Free Variant" . . . . . 99.35 154 97.37 97.37 1.17e-99 . . . . 813 1 59 no PDB 3H2P . "Human Sod1 D124v Variant" . . . . . 99.35 153 97.37 97.37 3.98e-99 . . . . 813 1 60 no PDB 3H2Q . "Human Sod1 H80r Variant, P21 Crystal Form" . . . . . 99.35 153 97.37 97.37 1.89e-99 . . . . 813 1 61 no PDB 3KH3 . "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P212121 Crystal Form Cont" . . . . . 99.35 153 98.03 98.03 1.81e-100 . . . . 813 1 62 no PDB 3KH4 . "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P6522 Crystal Form Contai" . . . . . 99.35 153 98.03 98.03 1.81e-100 . . . . 813 1 63 no PDB 3QQD . "Human Sod1 H80r Variant, P212121 Crystal Form" . . . . . 99.35 154 97.37 97.37 1.70e-99 . . . . 813 1 64 no PDB 3RE0 . "Crystal Structure Of Human Apo Cu,zn Superoxide Dismutase (sod1) Complexed With Cisplatin" . . . . . 99.35 153 98.03 98.03 1.81e-100 . . . . 813 1 65 no PDB 3T5W . "2me Modified Human Sod1" . . . . . 99.35 153 98.03 98.03 2.11e-100 . . . . 813 1 66 no PDB 4A7G . "Structure Of Human I113t Sod1 Mutant Complexed With 4- Methylpiperazin-1-yl)quinazoline In The P21 Space Group." . . . . . 99.35 153 97.37 97.37 9.31e-100 . . . . 813 1 67 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." . . . . . 99.35 153 97.37 97.37 9.31e-100 . . . . 813 1 68 no PDB 4A7S . "Structure Of Human I113t Sod1 Mutant Complexed With 5- Fluorouridine In The P21 Space Group" . . . . . 99.35 153 97.37 97.37 9.31e-100 . . . . 813 1 69 no PDB 4A7T . "Structure Of Human I113t Sod1 Mutant Complexed With Isoproteranol In The P21 Space Group" . . . . . 99.35 153 97.37 97.37 9.31e-100 . . . . 813 1 70 no PDB 4A7U . "Structure Of Human I113t Sod1 Complexed With Adrenaline In The P21 Space Group." . . . . . 99.35 153 97.37 97.37 9.31e-100 . . . . 813 1 71 no PDB 4A7V . "Structure Of Human I113t Sod1 Mutant Complexed With Dopamine In The P21 Space Group" . . . . . 99.35 153 97.37 97.37 9.31e-100 . . . . 813 1 72 no PDB 4B3E . "Structure Of Copper-Zinc Superoxide Dismutase Complexed With Bicarbonate." . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 73 no PDB 4FF9 . "Crystal Structure Of Cysteinylated Wt Sod1" . . . . . 99.35 153 98.03 98.03 1.81e-100 . . . . 813 1 74 no PDB 4MCM . "Human Sod1 C57s Mutant, As-isolated" . . . . . 99.35 153 97.37 97.37 6.80e-99 . . . . 813 1 75 no PDB 4MCN . "Human Sod1 C57s Mutant, Metal-free" . . . . . 99.35 153 97.37 97.37 6.80e-99 . . . . 813 1 76 no PDB 4OH2 . "Crystal Structure Of Cu/zn Superoxide Dismutase I149t" . . . . . 99.35 153 98.68 98.68 2.79e-101 . . . . 813 1 77 no DBJ BAA14373 . "unnamed protein product [Schizosaccharomyces pombe]" . . . . . 98.04 179 98.00 98.00 8.47e-99 . . . . 813 1 78 no DBJ BAC20345 . "Cu,Zn-superoxide dismutase [Pan troglodytes]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 79 no DBJ BAG35052 . "unnamed protein product [Homo sapiens]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 80 no DBJ BAG73767 . "superoxide dismutase 1, soluble [synthetic construct]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 81 no EMBL CAA26182 . "unnamed protein product [Homo sapiens]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 82 no EMBL CAG29351 . "SOD1 [Homo sapiens]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 83 no EMBL CAG46542 . "SOD1 [Homo sapiens]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 84 no GB AAA72747 . "CuZn superoxide dismutase [synthetic construct]" . . . . . 99.35 154 99.34 99.34 5.55e-102 . . . . 813 1 85 no GB AAA80237 . "HSOD-GlyProGly-A+, partial [synthetic construct]" . . . . . 99.35 171 99.34 99.34 1.88e-101 . . . . 813 1 86 no GB AAB05661 . "Cu/Zn-superoxide dismutase [Homo sapiens]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 87 no GB AAB05662 . "Cu/Zn-superoxide dismutase [Homo sapiens]" . . . . . 99.35 154 97.37 97.37 2.09e-99 . . . . 813 1 88 no GB AAB27818 . "Cu,Zn superoxide dismutase, SOD=SOD1 gene product {A to V single-site mutation} [human, Peptide Mutant, 153 aa]" . . . . . 99.35 153 97.37 97.37 1.13e-99 . . . . 813 1 89 no REF NP_000445 . "superoxide dismutase [Cu-Zn] [Homo sapiens]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 90 no REF NP_001009025 . "superoxide dismutase [Cu-Zn] [Pan troglodytes]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 91 no REF XP_003813274 . "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 92 no REF XP_004062735 . "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" . . . . . 99.35 154 97.37 97.37 1.74e-99 . . . . 813 1 93 no REF XP_004062736 . "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" . . . . . 99.35 154 97.37 97.37 1.74e-99 . . . . 813 1 94 no SP P00441 . "RecName: Full=Superoxide dismutase [Cu-Zn]; AltName: Full=Superoxide dismutase 1; Short=hSod1 [Homo sapiens]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 95 no SP P60052 . "RecName: Full=Superoxide dismutase [Pan troglodytes]" . . . . . 99.35 154 98.03 98.03 1.59e-100 . . . . 813 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID A137 variant 813 1 'copper-zinc superoxide dismutase' common 813 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 . AYA . 813 1 2 . THR . 813 1 3 . LYS . 813 1 4 . ALA . 813 1 5 . VAL . 813 1 6 . ALA . 813 1 7 . VAL . 813 1 8 . LEU . 813 1 9 . LYS . 813 1 10 . GLY . 813 1 11 . ASP . 813 1 12 . GLY . 813 1 13 . PRO . 813 1 14 . VAL . 813 1 15 . GLN . 813 1 16 . GLY . 813 1 17 . ILE . 813 1 18 . ILE . 813 1 19 . ASN . 813 1 20 . PHE . 813 1 21 . GLU . 813 1 22 . GLN . 813 1 23 . LYS . 813 1 24 . GLU . 813 1 25 . SER . 813 1 26 . ASN . 813 1 27 . GLY . 813 1 28 . PRO . 813 1 29 . VAL . 813 1 30 . LYS . 813 1 31 . VAL . 813 1 32 . TRP . 813 1 33 . GLY . 813 1 34 . SER . 813 1 35 . ILE . 813 1 36 . LYS . 813 1 37 . GLY . 813 1 38 . LEU . 813 1 39 . THR . 813 1 40 . GLU . 813 1 41 . GLY . 813 1 42 . LEU . 813 1 43 . HIS . 813 1 44 . GLY . 813 1 45 . PHE . 813 1 46 . HIS . 813 1 47 . VAL . 813 1 48 . HIS . 813 1 49 . GLU . 813 1 50 . PHE . 813 1 51 . GLY . 813 1 52 . ASP . 813 1 53 . ASN . 813 1 54 . THR . 813 1 55 . ALA . 813 1 56 . GLY . 813 1 57 . CYS . 813 1 58 . THR . 813 1 59 . SER . 813 1 60 . ALA . 813 1 61 . GLY . 813 1 62 . PRO . 813 1 63 . HIS . 813 1 64 . PHE . 813 1 65 . ASN . 813 1 66 . PRO . 813 1 67 . LEU . 813 1 68 . SER . 813 1 69 . ARG . 813 1 70 . LYS . 813 1 71 . HIS . 813 1 72 . GLY . 813 1 73 . GLY . 813 1 74 . PRO . 813 1 75 . LYS . 813 1 76 . ASP . 813 1 77 . GLU . 813 1 78 . GLU . 813 1 79 . ARG . 813 1 80 . HIS . 813 1 81 . VAL . 813 1 82 . GLY . 813 1 83 . ASP . 813 1 84 . LEU . 813 1 85 . GLY . 813 1 86 . ASN . 813 1 87 . VAL . 813 1 88 . THR . 813 1 89 . ALA . 813 1 90 . ASP . 813 1 91 . LYS . 813 1 92 . ASP . 813 1 93 . GLY . 813 1 94 . VAL . 813 1 95 . ALA . 813 1 96 . ASP . 813 1 97 . VAL . 813 1 98 . SER . 813 1 99 . ILE . 813 1 100 . GLU . 813 1 101 . ASP . 813 1 102 . SER . 813 1 103 . VAL . 813 1 104 . ILE . 813 1 105 . SER . 813 1 106 . LEU . 813 1 107 . SER . 813 1 108 . GLY . 813 1 109 . ASP . 813 1 110 . HIS . 813 1 111 . SER . 813 1 112 . ILE . 813 1 113 . ILE . 813 1 114 . GLY . 813 1 115 . ARG . 813 1 116 . THR . 813 1 117 . LEU . 813 1 118 . VAL . 813 1 119 . VAL . 813 1 120 . HIS . 813 1 121 . GLU . 813 1 122 . LYS . 813 1 123 . ALA . 813 1 124 . ASP . 813 1 125 . ASP . 813 1 126 . LEU . 813 1 127 . GLY . 813 1 128 . LYS . 813 1 129 . GLY . 813 1 130 . GLY . 813 1 131 . ASN . 813 1 132 . GLU . 813 1 133 . GLU . 813 1 134 . SER . 813 1 135 . THR . 813 1 136 . LYS . 813 1 137 . ALA . 813 1 138 . GLY . 813 1 139 . ASN . 813 1 140 . ALA . 813 1 141 . GLY . 813 1 142 . SER . 813 1 143 . ARG . 813 1 144 . LEU . 813 1 145 . ALA . 813 1 146 . CYS . 813 1 147 . GLY . 813 1 148 . VAL . 813 1 149 . ILE . 813 1 150 . GLY . 813 1 151 . ILE . 813 1 152 . ALA . 813 1 153 . GLN . 813 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 . AYA 1 1 813 1 . THR 2 2 813 1 . LYS 3 3 813 1 . ALA 4 4 813 1 . VAL 5 5 813 1 . ALA 6 6 813 1 . VAL 7 7 813 1 . LEU 8 8 813 1 . LYS 9 9 813 1 . GLY 10 10 813 1 . ASP 11 11 813 1 . GLY 12 12 813 1 . PRO 13 13 813 1 . VAL 14 14 813 1 . GLN 15 15 813 1 . GLY 16 16 813 1 . ILE 17 17 813 1 . ILE 18 18 813 1 . ASN 19 19 813 1 . PHE 20 20 813 1 . GLU 21 21 813 1 . GLN 22 22 813 1 . LYS 23 23 813 1 . GLU 24 24 813 1 . SER 25 25 813 1 . ASN 26 26 813 1 . GLY 27 27 813 1 . PRO 28 28 813 1 . VAL 29 29 813 1 . LYS 30 30 813 1 . VAL 31 31 813 1 . TRP 32 32 813 1 . GLY 33 33 813 1 . SER 34 34 813 1 . ILE 35 35 813 1 . LYS 36 36 813 1 . GLY 37 37 813 1 . LEU 38 38 813 1 . THR 39 39 813 1 . GLU 40 40 813 1 . GLY 41 41 813 1 . LEU 42 42 813 1 . HIS 43 43 813 1 . GLY 44 44 813 1 . PHE 45 45 813 1 . HIS 46 46 813 1 . VAL 47 47 813 1 . HIS 48 48 813 1 . GLU 49 49 813 1 . PHE 50 50 813 1 . GLY 51 51 813 1 . ASP 52 52 813 1 . ASN 53 53 813 1 . THR 54 54 813 1 . ALA 55 55 813 1 . GLY 56 56 813 1 . CYS 57 57 813 1 . THR 58 58 813 1 . SER 59 59 813 1 . ALA 60 60 813 1 . GLY 61 61 813 1 . PRO 62 62 813 1 . HIS 63 63 813 1 . PHE 64 64 813 1 . ASN 65 65 813 1 . PRO 66 66 813 1 . LEU 67 67 813 1 . SER 68 68 813 1 . ARG 69 69 813 1 . LYS 70 70 813 1 . HIS 71 71 813 1 . GLY 72 72 813 1 . GLY 73 73 813 1 . PRO 74 74 813 1 . LYS 75 75 813 1 . ASP 76 76 813 1 . GLU 77 77 813 1 . GLU 78 78 813 1 . ARG 79 79 813 1 . HIS 80 80 813 1 . VAL 81 81 813 1 . GLY 82 82 813 1 . ASP 83 83 813 1 . LEU 84 84 813 1 . GLY 85 85 813 1 . ASN 86 86 813 1 . VAL 87 87 813 1 . THR 88 88 813 1 . ALA 89 89 813 1 . ASP 90 90 813 1 . LYS 91 91 813 1 . ASP 92 92 813 1 . GLY 93 93 813 1 . VAL 94 94 813 1 . ALA 95 95 813 1 . ASP 96 96 813 1 . VAL 97 97 813 1 . SER 98 98 813 1 . ILE 99 99 813 1 . GLU 100 100 813 1 . ASP 101 101 813 1 . SER 102 102 813 1 . VAL 103 103 813 1 . ILE 104 104 813 1 . SER 105 105 813 1 . LEU 106 106 813 1 . SER 107 107 813 1 . GLY 108 108 813 1 . ASP 109 109 813 1 . HIS 110 110 813 1 . SER 111 111 813 1 . ILE 112 112 813 1 . ILE 113 113 813 1 . GLY 114 114 813 1 . ARG 115 115 813 1 . THR 116 116 813 1 . LEU 117 117 813 1 . VAL 118 118 813 1 . VAL 119 119 813 1 . HIS 120 120 813 1 . GLU 121 121 813 1 . LYS 122 122 813 1 . ALA 123 123 813 1 . ASP 124 124 813 1 . ASP 125 125 813 1 . LEU 126 126 813 1 . GLY 127 127 813 1 . LYS 128 128 813 1 . GLY 129 129 813 1 . GLY 130 130 813 1 . ASN 131 131 813 1 . GLU 132 132 813 1 . GLU 133 133 813 1 . SER 134 134 813 1 . THR 135 135 813 1 . LYS 136 136 813 1 . ALA 137 137 813 1 . GLY 138 138 813 1 . ASN 139 139 813 1 . ALA 140 140 813 1 . GLY 141 141 813 1 . SER 142 142 813 1 . ARG 143 143 813 1 . LEU 144 144 813 1 . ALA 145 145 813 1 . CYS 146 146 813 1 . GLY 147 147 813 1 . VAL 148 148 813 1 . ILE 149 149 813 1 . GLY 150 150 813 1 . ILE 151 151 813 1 . ALA 152 152 813 1 . GLN 153 153 813 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 813 _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 $copper-zinc_superoxide_dismutase . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens generic . . . . . . . . . . . . . . . . . . . . 813 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 813 _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 $copper-zinc_superoxide_dismutase . 'not available' 'Saccharomyces cerevisiae' yeast . . Saccharomyces cerevisiae 2150-2-3 . . . . . . . . . . . . . . . . . . . . . . 813 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_AYA _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_AYA _Chem_comp.Entry_ID 813 _Chem_comp.ID AYA _Chem_comp.Provenance PDB _Chem_comp.Name N-ACETYLALANINE _Chem_comp.Type 'L-PEPTIDE LINKING' _Chem_comp.BMRB_code AYA _Chem_comp.PDB_code AYA _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-12-14 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code A _Chem_comp.Three_letter_code AYA _Chem_comp.Number_atoms_all 18 _Chem_comp.Number_atoms_nh 9 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/C5H9NO3/c1-3(5(8)9)6-4(2)7/h3H,1-2H3,(H,6,7)(H,8,9)/t3-/m0/s1 _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 ALA _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 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C5 H9 N O3' _Chem_comp.Formula_weight 131.130 _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 1AH4 _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 CC(C(=O)O)NC(=O)C SMILES 'OpenEye OEToolkits' 1.5.0 813 AYA C[C@@H](C(=O)O)NC(=O)C SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 813 AYA C[C@H](NC(C)=O)C(O)=O SMILES_CANONICAL CACTVS 3.341 813 AYA C[CH](NC(C)=O)C(O)=O SMILES CACTVS 3.341 813 AYA InChI=1S/C5H9NO3/c1-3(5(8)9)6-4(2)7/h3H,1-2H3,(H,6,7)(H,8,9)/t3-/m0/s1 InChI InChI 1.03 813 AYA KTHDTJVBEPMMGL-VKHMYHEASA-N InChIKey InChI 1.03 813 AYA O=C(NC(C(=O)O)C)C SMILES ACDLabs 10.04 813 AYA 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 '(2S)-2-acetamidopropanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 813 AYA N-acetyl-L-alanine 'SYSTEMATIC NAME' ACDLabs 10.04 813 AYA 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 N N N N . N . . N 0 . . . 1 no no . . . . 44.622 . 32.559 . 107.594 . -0.348 -0.312 0.665 1 . 813 AYA CA CA CA CA . C . . S 0 . . . 1 no no . . . . 43.401 . 33.356 . 107.549 . 0.492 0.079 -0.468 2 . 813 AYA CB CB CB CB . C . . N 0 . . . 1 no no . . . . 43.788 . 34.825 . 107.681 . 1.614 -0.945 -0.648 3 . 813 AYA C C C C . C . . N 0 . . . 1 no no . . . . 42.519 . 33.186 . 106.308 . -0.344 0.133 -1.719 4 . 813 AYA O O O O . O . . N 0 . . . 1 no no . . . . 41.309 . 33.373 . 106.377 . -1.523 -0.128 -1.669 5 . 813 AYA OXT OXT OXT OXT . O . . N 0 . . . 1 no yes . . . . 43.167 . 32.860 . 105.184 . 0.218 0.471 -2.890 6 . 813 AYA CT CT CT CT . C . . N 0 . . . 1 no no . . . . 44.582 . 31.225 . 107.628 . -0.054 0.126 1.905 7 . 813 AYA OT OT OT OT . O . . N 0 . . . 1 no no . . . . 43.881 . 30.626 . 108.445 . 0.906 0.845 2.083 8 . 813 AYA CM CM CM CM . C . . N 0 . . . 1 no no . . . . 45.343 . 30.495 . 106.529 . -0.919 -0.276 3.072 9 . 813 AYA H H H HN . H . . N 0 . . . 1 no no . . . . 45.386 . 32.953 . 108.073 . -1.116 -0.887 0.524 10 . 813 AYA HA HA HA HA . H . . N 0 . . . 1 no no . . . . 42.773 . 32.983 . 108.392 . 0.925 1.061 -0.277 11 . 813 AYA HB1 HB1 HB1 1HB . H . . N 0 . . . 1 no no . . . . 42.854 . 35.434 . 107.646 . 1.182 -1.927 -0.839 12 . 813 AYA HB2 HB2 HB2 2HB . H . . N 0 . . . 1 no no . . . . 44.401 . 35.028 . 108.589 . 2.240 -0.653 -1.492 13 . 813 AYA HB3 HB3 HB3 3HB . H . . N 0 . . . 1 no no . . . . 44.537 . 35.142 . 106.919 . 2.220 -0.984 0.256 14 . 813 AYA HXT HXT HXT HXT . H . . N 0 . . . 1 no yes . . . . 42.620 . 32.754 . 104.414 . -0.319 0.506 -3.693 15 . 813 AYA HM1 HM1 HM1 1HM . H . . N 0 . . . 1 no no . . . . 45.309 . 29.380 . 106.557 . -0.528 0.171 3.986 16 . 813 AYA HM2 HM2 HM2 2HM . H . . N 0 . . . 1 no no . . . . 44.999 . 30.855 . 105.531 . -1.938 0.070 2.905 17 . 813 AYA HM3 HM3 HM3 3HM . H . . N 0 . . . 1 no no . . . . 46.403 . 30.838 . 106.515 . -0.915 -1.362 3.169 18 . 813 AYA stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N CA no N 1 . 813 AYA 2 . SING N CT no N 2 . 813 AYA 3 . SING N H no N 3 . 813 AYA 4 . SING CA CB no N 4 . 813 AYA 5 . SING CA C no N 5 . 813 AYA 6 . SING CA HA no N 6 . 813 AYA 7 . SING CB HB1 no N 7 . 813 AYA 8 . SING CB HB2 no N 8 . 813 AYA 9 . SING CB HB3 no N 9 . 813 AYA 10 . DOUB C O no N 10 . 813 AYA 11 . SING C OXT no N 11 . 813 AYA 12 . SING OXT HXT no N 12 . 813 AYA 13 . DOUB CT OT no N 13 . 813 AYA 14 . SING CT CM no N 14 . 813 AYA 15 . SING CM HM1 no N 15 . 813 AYA 16 . SING CM HM2 no N 16 . 813 AYA 17 . SING CM HM3 no N 17 . 813 AYA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 813 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 813 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 5.3 . na 813 1 temperature 300 . K 813 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 813 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 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 813 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 813 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 813 _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 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 813 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 813 _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 H . TMS . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 813 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_chemical_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 813 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 813 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 46 46 HIS HB2 H 1 18.5 . . 1 . . . . . . . . 813 1 2 . 1 1 46 46 HIS HB3 H 1 -5.3 . . 1 . . . . . . . . 813 1 3 . 1 1 46 46 HIS HD2 H 1 40.5 . . 1 . . . . . . . . 813 1 4 . 1 1 46 46 HIS HE1 H 1 25.5 . . 1 . . . . . . . . 813 1 5 . 1 1 46 46 HIS HE2 H 1 48.6 . . 1 . . . . . . . . 813 1 6 . 1 1 48 48 HIS HD1 H 1 36.3 . . 1 . . . . . . . . 813 1 7 . 1 1 48 48 HIS HD2 H 1 29.9 . . 1 . . . . . . . . 813 1 8 . 1 1 48 48 HIS HE1 H 1 21.4 . . 1 . . . . . . . . 813 1 9 . 1 1 63 63 HIS HD2 H 1 65.4 . . 1 . . . . . . . . 813 1 10 . 1 1 71 71 HIS HD2 H 1 50.2 . . 1 . . . . . . . . 813 1 11 . 1 1 80 80 HIS HD2 H 1 48.6 . . 1 . . . . . . . . 813 1 12 . 1 1 83 83 ASP HB2 H 1 36.3 . . 1 . . . . . . . . 813 1 13 . 1 1 83 83 ASP HB3 H 1 36.3 . . 1 . . . . . . . . 813 1 14 . 1 1 120 120 HIS HD1 H 1 56.9 . . 1 . . . . . . . . 813 1 15 . 1 1 120 120 HIS HD2 H 1 24.5 . . 1 . . . . . . . . 813 1 16 . 1 1 120 120 HIS HE1 H 1 38.7 . . 1 . . . . . . . . 813 1 stop_ save_