data_2229 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 2229 _Entry.Title ; The Role of an Active Site Histidine in the Catalytic Mechanism of Aspartate Transcarbamoylase ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-04-13 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _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 Colin Kleanthous . . . 2229 2 David Wemmer . . . 2229 3 H. Schachman . K. . 2229 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 2229 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 1 2229 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 5 . . 2010-06-16 . revision BMRB 'Complete natural source information' 2229 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 2229 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 2229 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 2229 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 2229 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 2229 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Kleanthous, Colin, Wemmer, David, Schachman, H. K., "The Role of an Active Site Histidine in the Catalytic Mechanism of Aspartate Transcarbamoylase," J. Biol. Chem. 263 (26), 13062-13067 (1988). ; _Citation.Title ; The Role of an Active Site Histidine in the Catalytic Mechanism of Aspartate Transcarbamoylase ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full . _Citation.Journal_volume 263 _Citation.Journal_issue 26 _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 13062 _Citation.Page_last 13067 _Citation.Year 1988 _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 Colin Kleanthous . . . 2229 1 2 David Wemmer . . . 2229 1 3 H. Schachman . K. . 2229 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_aspartate_transcarbamoylase _Assembly.Sf_category assembly _Assembly.Sf_framecode system_aspartate_transcarbamoylase _Assembly.Entry_ID 2229 _Assembly.ID 1 _Assembly.Name 'aspartate transcarbamoylase' _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 'aspartate transcarbamoylase' 1 $aspartate_transcarbamoylase . . . . . . . . . 2229 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'aspartate transcarbamoylase' system 2229 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_aspartate_transcarbamoylase _Entity.Sf_category entity _Entity.Sf_framecode aspartate_transcarbamoylase _Entity.Entry_ID 2229 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'aspartate transcarbamoylase' _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 ; ANPLYQKHIISINDLSRDDL NLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFQ TSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVD AIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLL DLFTIQQTEGRLDNLHVAMV GDLKYGRTVHSLTQALAKFD GNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMA EVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKAN MKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALL ALVLNRDLVL ; _Entity.Polymer_seq_one_letter_code ; ANPLYQKHIISINDLSRDDL NLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFQ TSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVD AIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLL DLFTIQQTEGRLDNLHVAMV GDLKYGRTVHSLTQALAKFD GNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMA EVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKAN MKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALL ALVLNRDLVL ; _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 310 _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 2.1.3.2 _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 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1ACM . "Arginine 54 In The Active Site Of Escherichia Coli Aspartate Transcarbamoylase Is Critical For Catalysis: A Site-Specific Mutag" . . . . . 100.00 310 99.68 99.68 0.00e+00 . . . . 2229 1 2 no PDB 1AT1 . "Crystal Structures Of Phosphonoacetamide Ligated T And Phosphonoacetamide And Malonate Ligated R States Of Aspartate Carbamoylt" . . . . . 100.00 310 100.00 100.00 0.00e+00 . . . . 2229 1 3 no PDB 1D09 . "Aspartate Transcarbamoylase Complexed With N-Phosphonacetyl-L- Aspartate (Pala)" . . . . . 100.00 310 99.35 100.00 0.00e+00 . . . . 2229 1 4 no PDB 1EKX . "The Isolated, Unregulated Catalytic Trimer Of Aspartate Transcarbamoylase Complexed With Bisubstrate Analog Pala (N-(Phosphonac" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 5 no PDB 1EZZ . "Crystal Structure Of E. Coli Aspartate Transcarbamoylase P268a Mutant In The T-State" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 6 no PDB 1F1B . "Crystal Structure Of E. Coli Aspartate Transcarbamoylase P268a Mutant In The R-state In The Presence Of N-phosphonacetyl-l-aspa" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 7 no PDB 1GQ3 . "Structure Of The R105a Mutant Catalytic Trimer Of Escherichia Coli Aspartate Transcarbamoylase At 2.0-A Resolution" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 8 no PDB 1I5O . "Crystal Structure Of Mutant R105a Of E. Coli Aspartate Transcarbamoylase" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 9 no PDB 1NBE . "Aspartate Transcarbamoylase Regulatory Chain Mutant (T82a)" . . . . . 100.00 310 100.00 100.00 0.00e+00 . . . . 2229 1 10 no PDB 1Q95 . "Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosp" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 11 no PDB 1R0B . "Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosp" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 12 no PDB 1R0C . "Products In The T State Of Aspartate Transcarbamylase: Crystal Structure Of The Phosphate And N-Carbamyl-L-Aspartate Ligated En" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 13 no PDB 1RAA . "Crystal Structure Of Ctp-ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutan" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 14 no PDB 1RAB . "Crystal Structure Of Ctp-ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutan" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 15 no PDB 1RAC . "Crystal Structure Of Ctp-ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutan" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 16 no PDB 1RAD . "Crystal Structure Of Ctp-ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutan" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 17 no PDB 1RAE . "Crystal Structure Of Ctp-ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutan" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 18 no PDB 1RAF . "Crystal Structure Of Ctp-ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutan" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 19 no PDB 1RAG . "Crystal Structure Of Ctp-ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutan" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 20 no PDB 1RAH . "Crystal Structure Of Ctp-ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutan" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 21 no PDB 1RAI . "Crystal Structure Of Ctp-ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutan" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 22 no PDB 1SKU . "E. Coli Aspartate Transcarbamylase 240's Loop Mutant (K244n)" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 23 no PDB 1TTH . "Aspartate Transcarbamoylase Catalytic Chain Mutant Glu50ala Complexed With N-(Phosphonacetyl-L-Aspartate) (Pala)" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 24 no PDB 1TU0 . "Aspartate Transcarbamoylase Catalytic Chain Mutant E50a Complex With Phosphonoacetamide" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 25 no PDB 1TUG . "Aspartate Transcarbamoylase Catalytic Chain Mutant E50a Complex With Phosphonoacetamide, Malonate, And Cytidine-5- Prime-Tripho" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 26 no PDB 1XJW . "The Structure Of E. Coli Aspartate Transcarbamoylase Q137a Mutant In The R-State" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 27 no PDB 1ZA1 . "Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of Ctp At 2.20 A Resolution" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 28 no PDB 1ZA2 . "Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of Ctp, Carbamoyl Phosphate At 2.50 A Resolution" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 29 no PDB 2A0F . "Structure Of D236a Mutant E. Coli Aspartate Transcarbamoylase In Presence Of Phosphonoacetamide At 2.90 A Resolution" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 30 no PDB 2AIR . "T-State Active Site Of Aspartate Transcarbamylase:crystal Structure Of The Carbamyl Phosphate And L-Alanosine Ligated Enzyme" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 31 no PDB 2AT1 . "Crystal Structures Of Phosphonoacetamide Ligated T And Phosphonoacetamide And Malonate Ligated R States Of Aspartate Carbamoylt" . . . . . 100.00 310 100.00 100.00 0.00e+00 . . . . 2229 1 32 no PDB 2FZC . "The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.10 Resolution" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 33 no PDB 2FZG . "The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.25 Resolution" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 34 no PDB 2FZK . "The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.50 Resolution" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 35 no PDB 2H3E . "Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of N-Phosphonacetyl-L-Isoasparagine At 2.3a Resoluti" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 36 no PDB 2HSE . "Structure Of D236a E. Coli Aspartate Transcarbamoylase In The Presence Of Phosphonoacetamide And L-Aspartate At 2.60 A Resoluti" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 37 no PDB 2IPO . "E. Coli Aspartate Transcarbamoylase Complexed With N- Phosphonacetyl-l-asparagine" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 38 no PDB 2QG9 . "Structure Of A Regulatory Subunit Mutant D19a Of Atcase From E. Coli" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 39 no PDB 2QGF . "Structure Of Regulatory Chain Mutant H20a Of Asparate Transcarbamoylase From E. Coli" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 40 no PDB 3AT1 . "Crystal Structures Of Phosphonoacetamide Ligated T And Phosphonoacetamide And Malonate Ligated R States Of Aspartate Carbamoylt" . . . . . 100.00 310 100.00 100.00 0.00e+00 . . . . 2229 1 41 no PDB 3CSU . "Catalytic Trimer Of Escherichia Coli Aspartate Transcarbamoylase" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 42 no PDB 3D7S . "Crystal Structure Of Wild-Type E. Coli Asparate Transcarbamoylase At Ph 8.5 At 2.80 A Resolution" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 43 no PDB 3MPU . "Crystal Structure Of The C47aA241C DISULFIDE-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme" . . . . . 100.00 310 98.06 99.35 0.00e+00 . . . . 2229 1 44 no PDB 3NPM . "Crystal Structure Of The C47aA241C DISULFIDE-Linked C6 Aspartate Transcarbamoylase Enzyme" . . . . . 100.00 310 98.06 99.35 0.00e+00 . . . . 2229 1 45 no PDB 4AT1 . "Structural Consequences Of Effector Binding To The T State Of Aspartate Carbamoyltransferase. Crystal Structures Of The Unligat" . . . . . 100.00 310 100.00 100.00 0.00e+00 . . . . 2229 1 46 no PDB 4E2F . "Crystal Structure Of E. Coli Aspartate Transcarbamoylase K164eE239K Mutant In An Intermediate State" . . . . . 100.00 310 98.06 100.00 0.00e+00 . . . . 2229 1 47 no PDB 4F04 . "A Second Allosteric Site In E. Coli Aspartate Transcarbamoylase: R- State Atcase With Utp Bound" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 48 no PDB 4FYV . "Aspartate Transcarbamoylase Complexed With Dctp" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 49 no PDB 4FYW . "E. Coli Aspartate Transcarbamoylase Complexed With Ctp" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 50 no PDB 4FYX . "E. Coli Aspartate Transcarbamoylase Complexed With Dctp, Utp, And Mg2+" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 51 no PDB 4FYY . "E. Coli Aspartate Transcarbamoylase Complexed With Ctp, Utp, And Mg2+" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 52 no PDB 4KGV . "The R State Structure Of E. Coli Atcase With Atp Bound" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 53 no PDB 4KGX . "The R State Structure Of E. Coli Atcase With Ctp Bound" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 54 no PDB 4KGZ . "The R State Structure Of E. Coli Atcase With Utp And Magnesium Bound" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 55 no PDB 4KH0 . "The R State Structure Of E. Coli Atcase With Atp And Magnesium Bound" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 56 no PDB 4KH1 . "The R State Structure Of E. Coli Atcase With Ctp,utp, And Magnesium Bound" . . . . . 100.00 310 98.71 100.00 0.00e+00 . . . . 2229 1 57 no PDB 4WTO . "Natural Source Aspartate Carbamoyltransferase In E.coil (ligand-free And Zinc-free)" . . . . . 100.00 310 98.39 99.68 0.00e+00 . . . . 2229 1 58 no PDB 5AT1 . "Structural Consequences Of Effector Binding To The T State Of Aspartate Carbamoyltransferase. Crystal Structures Of The Unligat" . . . . . 100.00 310 100.00 100.00 0.00e+00 . . . . 2229 1 59 no PDB 6AT1 . "Structural Consequences Of Effector Binding To The T State Of Aspartate Carbamoyltransferase. Crystal Structures Of The Unligat" . . . . . 100.00 310 100.00 100.00 0.00e+00 . . . . 2229 1 60 no PDB 7AT1 . "Crystal Structures Of Aspartate Carbamoyltransferase Ligated With Phosphonoacetamide, Malonate, And Ctp Or Atp At 2.8-angstroms" . . . . . 100.00 310 100.00 100.00 0.00e+00 . . . . 2229 1 61 no PDB 8AT1 . "Crystal Structures Of Aspartate Carbamoyltransferase Ligated With Phosphonoacetamide, Malonate, And Ctp Or Atp At 2.8-Angstroms" . . . . . 100.00 310 100.00 100.00 0.00e+00 . . . . 2229 1 62 no PDB 8ATC . "Complex Of N-Phosphonacetyl-L-Aspartate With Aspartate Carbamoyltransferase. X-Ray Refinement, Analysis Of Conformational Chang" . . . . . 100.00 310 100.00 100.00 0.00e+00 . . . . 2229 1 63 no PDB 9ATC . "Atcase Y165f Mutant" . . . . . 100.00 310 98.39 100.00 0.00e+00 . . . . 2229 1 64 no DBJ BAB38645 . "aspartate carbamoyltransferase catalytic subunit [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 65 no DBJ BAE78244 . "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 66 no DBJ BAG80076 . "aspartate carbamoyltransferase catalytic subunit [Escherichia coli SE11]" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 67 no DBJ BAI28551 . "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 68 no DBJ BAI33723 . "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli O103:H2 str. 12009]" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 69 no EMBL CAP78763 . "Aspartate carbamoyltransferase catalytic chain [Escherichia coli LF82]" . . . . . 100.00 311 98.39 99.68 0.00e+00 . . . . 2229 1 70 no EMBL CAQ34594 . "aspartate carbamoyltransferase, PyrB subunit, subunit of aspartate carbamoyltransferase, catalytic subunit and aspartate transc" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 71 no EMBL CAQ91746 . "aspartate carbamoyltransferase, catalytic subunit [Escherichia fergusonii ATCC 35469]" . . . . . 100.00 311 97.74 99.68 0.00e+00 . . . . 2229 1 72 no EMBL CAR01219 . "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli IAI1]" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 73 no EMBL CAR05983 . "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli S88]" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 74 no GB AAA24474 . "aspartate transcarbamoylase catalytic chain [Escherichia coli K-12]" . . . . . 100.00 311 98.39 99.35 0.00e+00 . . . . 2229 1 75 no GB AAA24476 . "aspartate transcarbamoylase catalytic chain (pyrB) [Escherichia coli]" . . . . . 100.00 311 99.03 100.00 0.00e+00 . . . . 2229 1 76 no GB AAA97142 . "aspartate carbomoyltransferase catalytic subunit [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 311 98.39 99.68 0.00e+00 . . . . 2229 1 77 no GB AAC77202 . "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 78 no GB AAG59443 . "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 311 98.39 99.68 0.00e+00 . . . . 2229 1 79 no PIR G86122 . "hypothetical protein pyrB [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" . . . . . 100.00 311 98.39 99.68 0.00e+00 . . . . 2229 1 80 no REF NP_313249 . "aspartate carbamoyltransferase [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 81 no REF NP_418666 . "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 82 no REF NP_709956 . "aspartate carbamoyltransferase [Shigella flexneri 2a str. 301]" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 83 no REF WP_000002014 . "aspartate carbamoyltransferase catalytic subunit [Escherichia coli]" . . . . . 100.00 311 98.39 99.68 0.00e+00 . . . . 2229 1 84 no REF WP_000013029 . "aspartate carbamoyltransferase catalytic subunit [Escherichia coli]" . . . . . 100.00 311 98.06 99.35 0.00e+00 . . . . 2229 1 85 no SP A1AJF0 . "RecName: Full=Aspartate carbamoyltransferase; AltName: Full=Aspartate transcarbamylase; Short=ATCase" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 86 no SP A7ZVC7 . "RecName: Full=Aspartate carbamoyltransferase; AltName: Full=Aspartate transcarbamylase; Short=ATCase" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 87 no SP A8A803 . "RecName: Full=Aspartate carbamoyltransferase; AltName: Full=Aspartate transcarbamylase; Short=ATCase" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 88 no SP B1ISW0 . "RecName: Full=Aspartate carbamoyltransferase; AltName: Full=Aspartate transcarbamylase; Short=ATCase" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 89 no SP B1LRD2 . "RecName: Full=Aspartate carbamoyltransferase; AltName: Full=Aspartate transcarbamylase; Short=ATCase" . . . . . 100.00 311 98.71 100.00 0.00e+00 . . . . 2229 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'aspartate transcarbamoylase' common 2229 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 . 2229 1 2 . ASN . 2229 1 3 . PRO . 2229 1 4 . LEU . 2229 1 5 . TYR . 2229 1 6 . GLN . 2229 1 7 . LYS . 2229 1 8 . HIS . 2229 1 9 . ILE . 2229 1 10 . ILE . 2229 1 11 . SER . 2229 1 12 . ILE . 2229 1 13 . ASN . 2229 1 14 . ASP . 2229 1 15 . LEU . 2229 1 16 . SER . 2229 1 17 . ARG . 2229 1 18 . ASP . 2229 1 19 . ASP . 2229 1 20 . LEU . 2229 1 21 . ASN . 2229 1 22 . LEU . 2229 1 23 . VAL . 2229 1 24 . LEU . 2229 1 25 . ALA . 2229 1 26 . THR . 2229 1 27 . ALA . 2229 1 28 . ALA . 2229 1 29 . LYS . 2229 1 30 . LEU . 2229 1 31 . LYS . 2229 1 32 . ALA . 2229 1 33 . ASN . 2229 1 34 . PRO . 2229 1 35 . GLN . 2229 1 36 . PRO . 2229 1 37 . GLU . 2229 1 38 . LEU . 2229 1 39 . LEU . 2229 1 40 . LYS . 2229 1 41 . HIS . 2229 1 42 . LYS . 2229 1 43 . VAL . 2229 1 44 . ILE . 2229 1 45 . ALA . 2229 1 46 . SER . 2229 1 47 . CYS . 2229 1 48 . PHE . 2229 1 49 . PHE . 2229 1 50 . GLU . 2229 1 51 . ALA . 2229 1 52 . SER . 2229 1 53 . THR . 2229 1 54 . ARG . 2229 1 55 . THR . 2229 1 56 . ARG . 2229 1 57 . LEU . 2229 1 58 . SER . 2229 1 59 . PHE . 2229 1 60 . GLN . 2229 1 61 . THR . 2229 1 62 . SER . 2229 1 63 . MET . 2229 1 64 . HIS . 2229 1 65 . ARG . 2229 1 66 . LEU . 2229 1 67 . GLY . 2229 1 68 . ALA . 2229 1 69 . SER . 2229 1 70 . VAL . 2229 1 71 . VAL . 2229 1 72 . GLY . 2229 1 73 . PHE . 2229 1 74 . SER . 2229 1 75 . ASP . 2229 1 76 . SER . 2229 1 77 . ALA . 2229 1 78 . ASN . 2229 1 79 . THR . 2229 1 80 . SER . 2229 1 81 . LEU . 2229 1 82 . GLY . 2229 1 83 . LYS . 2229 1 84 . LYS . 2229 1 85 . GLY . 2229 1 86 . GLU . 2229 1 87 . THR . 2229 1 88 . LEU . 2229 1 89 . ALA . 2229 1 90 . ASP . 2229 1 91 . THR . 2229 1 92 . ILE . 2229 1 93 . SER . 2229 1 94 . VAL . 2229 1 95 . ILE . 2229 1 96 . SER . 2229 1 97 . THR . 2229 1 98 . TYR . 2229 1 99 . VAL . 2229 1 100 . ASP . 2229 1 101 . ALA . 2229 1 102 . ILE . 2229 1 103 . VAL . 2229 1 104 . MET . 2229 1 105 . ARG . 2229 1 106 . HIS . 2229 1 107 . PRO . 2229 1 108 . GLN . 2229 1 109 . GLU . 2229 1 110 . GLY . 2229 1 111 . ALA . 2229 1 112 . ALA . 2229 1 113 . ARG . 2229 1 114 . LEU . 2229 1 115 . ALA . 2229 1 116 . THR . 2229 1 117 . GLU . 2229 1 118 . PHE . 2229 1 119 . SER . 2229 1 120 . GLY . 2229 1 121 . ASN . 2229 1 122 . VAL . 2229 1 123 . PRO . 2229 1 124 . VAL . 2229 1 125 . LEU . 2229 1 126 . ASN . 2229 1 127 . ALA . 2229 1 128 . GLY . 2229 1 129 . ASP . 2229 1 130 . GLY . 2229 1 131 . SER . 2229 1 132 . ASN . 2229 1 133 . GLN . 2229 1 134 . HIS . 2229 1 135 . PRO . 2229 1 136 . THR . 2229 1 137 . GLN . 2229 1 138 . THR . 2229 1 139 . LEU . 2229 1 140 . LEU . 2229 1 141 . ASP . 2229 1 142 . LEU . 2229 1 143 . PHE . 2229 1 144 . THR . 2229 1 145 . ILE . 2229 1 146 . GLN . 2229 1 147 . GLN . 2229 1 148 . THR . 2229 1 149 . GLU . 2229 1 150 . GLY . 2229 1 151 . ARG . 2229 1 152 . LEU . 2229 1 153 . ASP . 2229 1 154 . ASN . 2229 1 155 . LEU . 2229 1 156 . HIS . 2229 1 157 . VAL . 2229 1 158 . ALA . 2229 1 159 . MET . 2229 1 160 . VAL . 2229 1 161 . GLY . 2229 1 162 . ASP . 2229 1 163 . LEU . 2229 1 164 . LYS . 2229 1 165 . TYR . 2229 1 166 . GLY . 2229 1 167 . ARG . 2229 1 168 . THR . 2229 1 169 . VAL . 2229 1 170 . HIS . 2229 1 171 . SER . 2229 1 172 . LEU . 2229 1 173 . THR . 2229 1 174 . GLN . 2229 1 175 . ALA . 2229 1 176 . LEU . 2229 1 177 . ALA . 2229 1 178 . LYS . 2229 1 179 . PHE . 2229 1 180 . ASP . 2229 1 181 . GLY . 2229 1 182 . ASN . 2229 1 183 . ARG . 2229 1 184 . PHE . 2229 1 185 . TYR . 2229 1 186 . PHE . 2229 1 187 . ILE . 2229 1 188 . ALA . 2229 1 189 . PRO . 2229 1 190 . ASP . 2229 1 191 . ALA . 2229 1 192 . LEU . 2229 1 193 . ALA . 2229 1 194 . MET . 2229 1 195 . PRO . 2229 1 196 . GLU . 2229 1 197 . TYR . 2229 1 198 . ILE . 2229 1 199 . LEU . 2229 1 200 . ASP . 2229 1 201 . MET . 2229 1 202 . LEU . 2229 1 203 . ASP . 2229 1 204 . GLU . 2229 1 205 . LYS . 2229 1 206 . GLY . 2229 1 207 . ILE . 2229 1 208 . ALA . 2229 1 209 . TRP . 2229 1 210 . SER . 2229 1 211 . LEU . 2229 1 212 . HIS . 2229 1 213 . SER . 2229 1 214 . SER . 2229 1 215 . ILE . 2229 1 216 . GLU . 2229 1 217 . GLU . 2229 1 218 . VAL . 2229 1 219 . MET . 2229 1 220 . ALA . 2229 1 221 . GLU . 2229 1 222 . VAL . 2229 1 223 . ASP . 2229 1 224 . ILE . 2229 1 225 . LEU . 2229 1 226 . TYR . 2229 1 227 . MET . 2229 1 228 . THR . 2229 1 229 . ARG . 2229 1 230 . VAL . 2229 1 231 . GLN . 2229 1 232 . LYS . 2229 1 233 . GLU . 2229 1 234 . ARG . 2229 1 235 . LEU . 2229 1 236 . ASP . 2229 1 237 . PRO . 2229 1 238 . SER . 2229 1 239 . GLU . 2229 1 240 . TYR . 2229 1 241 . ALA . 2229 1 242 . ASN . 2229 1 243 . VAL . 2229 1 244 . LYS . 2229 1 245 . ALA . 2229 1 246 . GLN . 2229 1 247 . PHE . 2229 1 248 . VAL . 2229 1 249 . LEU . 2229 1 250 . ARG . 2229 1 251 . ALA . 2229 1 252 . SER . 2229 1 253 . ASP . 2229 1 254 . LEU . 2229 1 255 . HIS . 2229 1 256 . ASN . 2229 1 257 . ALA . 2229 1 258 . LYS . 2229 1 259 . ALA . 2229 1 260 . ASN . 2229 1 261 . MET . 2229 1 262 . LYS . 2229 1 263 . VAL . 2229 1 264 . LEU . 2229 1 265 . HIS . 2229 1 266 . PRO . 2229 1 267 . LEU . 2229 1 268 . PRO . 2229 1 269 . ARG . 2229 1 270 . VAL . 2229 1 271 . ASP . 2229 1 272 . GLU . 2229 1 273 . ILE . 2229 1 274 . ALA . 2229 1 275 . THR . 2229 1 276 . ASP . 2229 1 277 . VAL . 2229 1 278 . ASP . 2229 1 279 . LYS . 2229 1 280 . THR . 2229 1 281 . PRO . 2229 1 282 . HIS . 2229 1 283 . ALA . 2229 1 284 . TRP . 2229 1 285 . TYR . 2229 1 286 . PHE . 2229 1 287 . GLN . 2229 1 288 . GLN . 2229 1 289 . ALA . 2229 1 290 . GLY . 2229 1 291 . ASN . 2229 1 292 . GLY . 2229 1 293 . ILE . 2229 1 294 . PHE . 2229 1 295 . ALA . 2229 1 296 . ARG . 2229 1 297 . GLN . 2229 1 298 . ALA . 2229 1 299 . LEU . 2229 1 300 . LEU . 2229 1 301 . ALA . 2229 1 302 . LEU . 2229 1 303 . VAL . 2229 1 304 . LEU . 2229 1 305 . ASN . 2229 1 306 . ARG . 2229 1 307 . ASP . 2229 1 308 . LEU . 2229 1 309 . VAL . 2229 1 310 . LEU . 2229 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 2229 1 . ASN 2 2 2229 1 . PRO 3 3 2229 1 . LEU 4 4 2229 1 . TYR 5 5 2229 1 . GLN 6 6 2229 1 . LYS 7 7 2229 1 . HIS 8 8 2229 1 . ILE 9 9 2229 1 . ILE 10 10 2229 1 . SER 11 11 2229 1 . ILE 12 12 2229 1 . ASN 13 13 2229 1 . ASP 14 14 2229 1 . LEU 15 15 2229 1 . SER 16 16 2229 1 . ARG 17 17 2229 1 . ASP 18 18 2229 1 . ASP 19 19 2229 1 . LEU 20 20 2229 1 . ASN 21 21 2229 1 . LEU 22 22 2229 1 . VAL 23 23 2229 1 . LEU 24 24 2229 1 . ALA 25 25 2229 1 . THR 26 26 2229 1 . ALA 27 27 2229 1 . ALA 28 28 2229 1 . LYS 29 29 2229 1 . LEU 30 30 2229 1 . LYS 31 31 2229 1 . ALA 32 32 2229 1 . ASN 33 33 2229 1 . PRO 34 34 2229 1 . GLN 35 35 2229 1 . PRO 36 36 2229 1 . GLU 37 37 2229 1 . LEU 38 38 2229 1 . LEU 39 39 2229 1 . LYS 40 40 2229 1 . HIS 41 41 2229 1 . LYS 42 42 2229 1 . VAL 43 43 2229 1 . ILE 44 44 2229 1 . ALA 45 45 2229 1 . SER 46 46 2229 1 . CYS 47 47 2229 1 . PHE 48 48 2229 1 . PHE 49 49 2229 1 . GLU 50 50 2229 1 . ALA 51 51 2229 1 . SER 52 52 2229 1 . THR 53 53 2229 1 . ARG 54 54 2229 1 . THR 55 55 2229 1 . ARG 56 56 2229 1 . LEU 57 57 2229 1 . SER 58 58 2229 1 . PHE 59 59 2229 1 . GLN 60 60 2229 1 . THR 61 61 2229 1 . SER 62 62 2229 1 . MET 63 63 2229 1 . HIS 64 64 2229 1 . ARG 65 65 2229 1 . LEU 66 66 2229 1 . GLY 67 67 2229 1 . ALA 68 68 2229 1 . SER 69 69 2229 1 . VAL 70 70 2229 1 . VAL 71 71 2229 1 . GLY 72 72 2229 1 . PHE 73 73 2229 1 . SER 74 74 2229 1 . ASP 75 75 2229 1 . SER 76 76 2229 1 . ALA 77 77 2229 1 . ASN 78 78 2229 1 . THR 79 79 2229 1 . SER 80 80 2229 1 . LEU 81 81 2229 1 . GLY 82 82 2229 1 . LYS 83 83 2229 1 . LYS 84 84 2229 1 . GLY 85 85 2229 1 . GLU 86 86 2229 1 . THR 87 87 2229 1 . LEU 88 88 2229 1 . ALA 89 89 2229 1 . ASP 90 90 2229 1 . THR 91 91 2229 1 . ILE 92 92 2229 1 . SER 93 93 2229 1 . VAL 94 94 2229 1 . ILE 95 95 2229 1 . SER 96 96 2229 1 . THR 97 97 2229 1 . TYR 98 98 2229 1 . VAL 99 99 2229 1 . ASP 100 100 2229 1 . ALA 101 101 2229 1 . ILE 102 102 2229 1 . VAL 103 103 2229 1 . MET 104 104 2229 1 . ARG 105 105 2229 1 . HIS 106 106 2229 1 . PRO 107 107 2229 1 . GLN 108 108 2229 1 . GLU 109 109 2229 1 . GLY 110 110 2229 1 . ALA 111 111 2229 1 . ALA 112 112 2229 1 . ARG 113 113 2229 1 . LEU 114 114 2229 1 . ALA 115 115 2229 1 . THR 116 116 2229 1 . GLU 117 117 2229 1 . PHE 118 118 2229 1 . SER 119 119 2229 1 . GLY 120 120 2229 1 . ASN 121 121 2229 1 . VAL 122 122 2229 1 . PRO 123 123 2229 1 . VAL 124 124 2229 1 . LEU 125 125 2229 1 . ASN 126 126 2229 1 . ALA 127 127 2229 1 . GLY 128 128 2229 1 . ASP 129 129 2229 1 . GLY 130 130 2229 1 . SER 131 131 2229 1 . ASN 132 132 2229 1 . GLN 133 133 2229 1 . HIS 134 134 2229 1 . PRO 135 135 2229 1 . THR 136 136 2229 1 . GLN 137 137 2229 1 . THR 138 138 2229 1 . LEU 139 139 2229 1 . LEU 140 140 2229 1 . ASP 141 141 2229 1 . LEU 142 142 2229 1 . PHE 143 143 2229 1 . THR 144 144 2229 1 . ILE 145 145 2229 1 . GLN 146 146 2229 1 . GLN 147 147 2229 1 . THR 148 148 2229 1 . GLU 149 149 2229 1 . GLY 150 150 2229 1 . ARG 151 151 2229 1 . LEU 152 152 2229 1 . ASP 153 153 2229 1 . ASN 154 154 2229 1 . LEU 155 155 2229 1 . HIS 156 156 2229 1 . VAL 157 157 2229 1 . ALA 158 158 2229 1 . MET 159 159 2229 1 . VAL 160 160 2229 1 . GLY 161 161 2229 1 . ASP 162 162 2229 1 . LEU 163 163 2229 1 . LYS 164 164 2229 1 . TYR 165 165 2229 1 . GLY 166 166 2229 1 . ARG 167 167 2229 1 . THR 168 168 2229 1 . VAL 169 169 2229 1 . HIS 170 170 2229 1 . SER 171 171 2229 1 . LEU 172 172 2229 1 . THR 173 173 2229 1 . GLN 174 174 2229 1 . ALA 175 175 2229 1 . LEU 176 176 2229 1 . ALA 177 177 2229 1 . LYS 178 178 2229 1 . PHE 179 179 2229 1 . ASP 180 180 2229 1 . GLY 181 181 2229 1 . ASN 182 182 2229 1 . ARG 183 183 2229 1 . PHE 184 184 2229 1 . TYR 185 185 2229 1 . PHE 186 186 2229 1 . ILE 187 187 2229 1 . ALA 188 188 2229 1 . PRO 189 189 2229 1 . ASP 190 190 2229 1 . ALA 191 191 2229 1 . LEU 192 192 2229 1 . ALA 193 193 2229 1 . MET 194 194 2229 1 . PRO 195 195 2229 1 . GLU 196 196 2229 1 . TYR 197 197 2229 1 . ILE 198 198 2229 1 . LEU 199 199 2229 1 . ASP 200 200 2229 1 . MET 201 201 2229 1 . LEU 202 202 2229 1 . ASP 203 203 2229 1 . GLU 204 204 2229 1 . LYS 205 205 2229 1 . GLY 206 206 2229 1 . ILE 207 207 2229 1 . ALA 208 208 2229 1 . TRP 209 209 2229 1 . SER 210 210 2229 1 . LEU 211 211 2229 1 . HIS 212 212 2229 1 . SER 213 213 2229 1 . SER 214 214 2229 1 . ILE 215 215 2229 1 . GLU 216 216 2229 1 . GLU 217 217 2229 1 . VAL 218 218 2229 1 . MET 219 219 2229 1 . ALA 220 220 2229 1 . GLU 221 221 2229 1 . VAL 222 222 2229 1 . ASP 223 223 2229 1 . ILE 224 224 2229 1 . LEU 225 225 2229 1 . TYR 226 226 2229 1 . MET 227 227 2229 1 . THR 228 228 2229 1 . ARG 229 229 2229 1 . VAL 230 230 2229 1 . GLN 231 231 2229 1 . LYS 232 232 2229 1 . GLU 233 233 2229 1 . ARG 234 234 2229 1 . LEU 235 235 2229 1 . ASP 236 236 2229 1 . PRO 237 237 2229 1 . SER 238 238 2229 1 . GLU 239 239 2229 1 . TYR 240 240 2229 1 . ALA 241 241 2229 1 . ASN 242 242 2229 1 . VAL 243 243 2229 1 . LYS 244 244 2229 1 . ALA 245 245 2229 1 . GLN 246 246 2229 1 . PHE 247 247 2229 1 . VAL 248 248 2229 1 . LEU 249 249 2229 1 . ARG 250 250 2229 1 . ALA 251 251 2229 1 . SER 252 252 2229 1 . ASP 253 253 2229 1 . LEU 254 254 2229 1 . HIS 255 255 2229 1 . ASN 256 256 2229 1 . ALA 257 257 2229 1 . LYS 258 258 2229 1 . ALA 259 259 2229 1 . ASN 260 260 2229 1 . MET 261 261 2229 1 . LYS 262 262 2229 1 . VAL 263 263 2229 1 . LEU 264 264 2229 1 . HIS 265 265 2229 1 . PRO 266 266 2229 1 . LEU 267 267 2229 1 . PRO 268 268 2229 1 . ARG 269 269 2229 1 . VAL 270 270 2229 1 . ASP 271 271 2229 1 . GLU 272 272 2229 1 . ILE 273 273 2229 1 . ALA 274 274 2229 1 . THR 275 275 2229 1 . ASP 276 276 2229 1 . VAL 277 277 2229 1 . ASP 278 278 2229 1 . LYS 279 279 2229 1 . THR 280 280 2229 1 . PRO 281 281 2229 1 . HIS 282 282 2229 1 . ALA 283 283 2229 1 . TRP 284 284 2229 1 . TYR 285 285 2229 1 . PHE 286 286 2229 1 . GLN 287 287 2229 1 . GLN 288 288 2229 1 . ALA 289 289 2229 1 . GLY 290 290 2229 1 . ASN 291 291 2229 1 . GLY 292 292 2229 1 . ILE 293 293 2229 1 . PHE 294 294 2229 1 . ALA 295 295 2229 1 . ARG 296 296 2229 1 . GLN 297 297 2229 1 . ALA 298 298 2229 1 . LEU 299 299 2229 1 . LEU 300 300 2229 1 . ALA 301 301 2229 1 . LEU 302 302 2229 1 . VAL 303 303 2229 1 . LEU 304 304 2229 1 . ASN 305 305 2229 1 . ARG 306 306 2229 1 . ASP 307 307 2229 1 . LEU 308 308 2229 1 . VAL 309 309 2229 1 . LEU 310 310 2229 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 2229 _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 $aspartate_transcarbamoylase . 562 organism . 'Escherichia coli' 'E. coli' . . Eubacteria . Escherichia coli TR4363 . . . . . . . . . . . . . . . . . . . . 2229 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 2229 _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 $aspartate_transcarbamoylase . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 2229 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 2229 _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 2229 _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 6.4 . na 2229 1 temperature 283 . K 2229 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 2229 _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 2229 _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' . . 2229 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 2229 _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 . . . . . . . . . . . . . . . . 2229 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 2229 _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 . p-dioxane . . . . . ppm 67.8 . . . . . . 1 $entry_citation . . 1 $entry_citation 2229 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 2229 _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 . 2229 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 1 134 134 HIS CG C 13 136.8 . . 1 . . . . . . . . 2229 1 stop_ save_