data_2229 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Role of an Active Site Histidine in the Catalytic Mechanism of Aspartate Transcarbamoylase ; _BMRB_accession_number 2229 _BMRB_flat_file_name bmr2229.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kleanthous Colin . . 2 Wemmer David . . 3 Schachman H. K. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 1 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-16 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kleanthous Colin . . 2 Wemmer David . . 3 Schachman H. K. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 263 _Journal_issue 26 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 13062 _Page_last 13067 _Year 1988 _Details . save_ ################################## # Molecular system description # ################################## save_system_aspartate_transcarbamoylase _Saveframe_category molecular_system _Mol_system_name 'aspartate transcarbamoylase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'aspartate transcarbamoylase' $aspartate_transcarbamoylase stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_aspartate_transcarbamoylase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'aspartate transcarbamoylase' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 310 _Mol_residue_sequence ; ANPLYQKHIISINDLSRDDL NLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFQ TSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVD AIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLL DLFTIQQTEGRLDNLHVAMV GDLKYGRTVHSLTQALAKFD GNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMA EVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKAN MKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALL ALVLNRDLVL ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASN 3 PRO 4 LEU 5 TYR 6 GLN 7 LYS 8 HIS 9 ILE 10 ILE 11 SER 12 ILE 13 ASN 14 ASP 15 LEU 16 SER 17 ARG 18 ASP 19 ASP 20 LEU 21 ASN 22 LEU 23 VAL 24 LEU 25 ALA 26 THR 27 ALA 28 ALA 29 LYS 30 LEU 31 LYS 32 ALA 33 ASN 34 PRO 35 GLN 36 PRO 37 GLU 38 LEU 39 LEU 40 LYS 41 HIS 42 LYS 43 VAL 44 ILE 45 ALA 46 SER 47 CYS 48 PHE 49 PHE 50 GLU 51 ALA 52 SER 53 THR 54 ARG 55 THR 56 ARG 57 LEU 58 SER 59 PHE 60 GLN 61 THR 62 SER 63 MET 64 HIS 65 ARG 66 LEU 67 GLY 68 ALA 69 SER 70 VAL 71 VAL 72 GLY 73 PHE 74 SER 75 ASP 76 SER 77 ALA 78 ASN 79 THR 80 SER 81 LEU 82 GLY 83 LYS 84 LYS 85 GLY 86 GLU 87 THR 88 LEU 89 ALA 90 ASP 91 THR 92 ILE 93 SER 94 VAL 95 ILE 96 SER 97 THR 98 TYR 99 VAL 100 ASP 101 ALA 102 ILE 103 VAL 104 MET 105 ARG 106 HIS 107 PRO 108 GLN 109 GLU 110 GLY 111 ALA 112 ALA 113 ARG 114 LEU 115 ALA 116 THR 117 GLU 118 PHE 119 SER 120 GLY 121 ASN 122 VAL 123 PRO 124 VAL 125 LEU 126 ASN 127 ALA 128 GLY 129 ASP 130 GLY 131 SER 132 ASN 133 GLN 134 HIS 135 PRO 136 THR 137 GLN 138 THR 139 LEU 140 LEU 141 ASP 142 LEU 143 PHE 144 THR 145 ILE 146 GLN 147 GLN 148 THR 149 GLU 150 GLY 151 ARG 152 LEU 153 ASP 154 ASN 155 LEU 156 HIS 157 VAL 158 ALA 159 MET 160 VAL 161 GLY 162 ASP 163 LEU 164 LYS 165 TYR 166 GLY 167 ARG 168 THR 169 VAL 170 HIS 171 SER 172 LEU 173 THR 174 GLN 175 ALA 176 LEU 177 ALA 178 LYS 179 PHE 180 ASP 181 GLY 182 ASN 183 ARG 184 PHE 185 TYR 186 PHE 187 ILE 188 ALA 189 PRO 190 ASP 191 ALA 192 LEU 193 ALA 194 MET 195 PRO 196 GLU 197 TYR 198 ILE 199 LEU 200 ASP 201 MET 202 LEU 203 ASP 204 GLU 205 LYS 206 GLY 207 ILE 208 ALA 209 TRP 210 SER 211 LEU 212 HIS 213 SER 214 SER 215 ILE 216 GLU 217 GLU 218 VAL 219 MET 220 ALA 221 GLU 222 VAL 223 ASP 224 ILE 225 LEU 226 TYR 227 MET 228 THR 229 ARG 230 VAL 231 GLN 232 LYS 233 GLU 234 ARG 235 LEU 236 ASP 237 PRO 238 SER 239 GLU 240 TYR 241 ALA 242 ASN 243 VAL 244 LYS 245 ALA 246 GLN 247 PHE 248 VAL 249 LEU 250 ARG 251 ALA 252 SER 253 ASP 254 LEU 255 HIS 256 ASN 257 ALA 258 LYS 259 ALA 260 ASN 261 MET 262 LYS 263 VAL 264 LEU 265 HIS 266 PRO 267 LEU 268 PRO 269 ARG 270 VAL 271 ASP 272 GLU 273 ILE 274 ALA 275 THR 276 ASP 277 VAL 278 ASP 279 LYS 280 THR 281 PRO 282 HIS 283 ALA 284 TRP 285 TYR 286 PHE 287 GLN 288 GLN 289 ALA 290 GLY 291 ASN 292 GLY 293 ILE 294 PHE 295 ALA 296 ARG 297 GLN 298 ALA 299 LEU 300 LEU 301 ALA 302 LEU 303 VAL 304 LEU 305 ASN 306 ARG 307 ASP 308 LEU 309 VAL 310 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value 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 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 PDB 1D09 "Aspartate Transcarbamoylase Complexed With N-Phosphonacetyl-L- Aspartate (Pala)" 100.00 310 99.35 100.00 0.00e+00 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 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 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 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 PDB 1I5O "Crystal Structure Of Mutant R105a Of E. Coli Aspartate Transcarbamoylase" 100.00 310 98.39 99.68 0.00e+00 PDB 1NBE "Aspartate Transcarbamoylase Regulatory Chain Mutant (T82a)" 100.00 310 100.00 100.00 0.00e+00 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 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 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 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 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 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 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 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 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 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 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 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 PDB 1SKU "E. Coli Aspartate Transcarbamylase 240's Loop Mutant (K244n)" 100.00 310 98.39 99.68 0.00e+00 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 PDB 1TU0 "Aspartate Transcarbamoylase Catalytic Chain Mutant E50a Complex With Phosphonoacetamide" 100.00 310 98.39 99.68 0.00e+00 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 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 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 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 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 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 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 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 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 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 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 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 PDB 2IPO "E. Coli Aspartate Transcarbamoylase Complexed With N- Phosphonacetyl-l-asparagine" 100.00 310 98.71 100.00 0.00e+00 PDB 2QG9 "Structure Of A Regulatory Subunit Mutant D19a Of Atcase From E. Coli" 100.00 310 98.71 100.00 0.00e+00 PDB 2QGF "Structure Of Regulatory Chain Mutant H20a Of Asparate Transcarbamoylase From E. Coli" 100.00 310 98.71 100.00 0.00e+00 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 PDB 3CSU "Catalytic Trimer Of Escherichia Coli Aspartate Transcarbamoylase" 100.00 310 98.71 100.00 0.00e+00 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 PDB 3MPU "Crystal Structure Of The C47aA241C DISULFIDE-Linked E. Coli Aspartate Transcarbamoylase Holoenzyme" 100.00 310 98.06 99.35 0.00e+00 PDB 3NPM "Crystal Structure Of The C47aA241C DISULFIDE-Linked C6 Aspartate Transcarbamoylase Enzyme" 100.00 310 98.06 99.35 0.00e+00 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 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 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 PDB 4FYV "Aspartate Transcarbamoylase Complexed With Dctp" 100.00 310 98.71 100.00 0.00e+00 PDB 4FYW "E. Coli Aspartate Transcarbamoylase Complexed With Ctp" 100.00 310 98.71 100.00 0.00e+00 PDB 4FYX "E. Coli Aspartate Transcarbamoylase Complexed With Dctp, Utp, And Mg2+" 100.00 310 98.71 100.00 0.00e+00 PDB 4FYY "E. Coli Aspartate Transcarbamoylase Complexed With Ctp, Utp, And Mg2+" 100.00 310 98.71 100.00 0.00e+00 PDB 4KGV "The R State Structure Of E. Coli Atcase With Atp Bound" 100.00 310 98.71 100.00 0.00e+00 PDB 4KGX "The R State Structure Of E. Coli Atcase With Ctp Bound" 100.00 310 98.71 100.00 0.00e+00 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 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 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 PDB 4WTO "Natural Source Aspartate Carbamoyltransferase In E.coil (ligand-free And Zinc-free)" 100.00 310 98.39 99.68 0.00e+00 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 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 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 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 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 PDB 9ATC "Atcase Y165f Mutant" 100.00 310 98.39 100.00 0.00e+00 DBJ BAB38645 "aspartate carbamoyltransferase catalytic subunit [Escherichia coli O157:H7 str. Sakai]" 100.00 311 98.71 100.00 0.00e+00 DBJ BAE78244 "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli str. K12 substr. W3110]" 100.00 311 98.71 100.00 0.00e+00 DBJ BAG80076 "aspartate carbamoyltransferase catalytic subunit [Escherichia coli SE11]" 100.00 311 98.71 100.00 0.00e+00 DBJ BAI28551 "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli O26:H11 str. 11368]" 100.00 311 98.71 100.00 0.00e+00 DBJ BAI33723 "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli O103:H2 str. 12009]" 100.00 311 98.71 100.00 0.00e+00 EMBL CAP78763 "Aspartate carbamoyltransferase catalytic chain [Escherichia coli LF82]" 100.00 311 98.39 99.68 0.00e+00 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 EMBL CAQ91746 "aspartate carbamoyltransferase, catalytic subunit [Escherichia fergusonii ATCC 35469]" 100.00 311 97.74 99.68 0.00e+00 EMBL CAR01219 "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli IAI1]" 100.00 311 98.71 100.00 0.00e+00 EMBL CAR05983 "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli S88]" 100.00 311 98.71 100.00 0.00e+00 GB AAA24474 "aspartate transcarbamoylase catalytic chain [Escherichia coli K-12]" 100.00 311 98.39 99.35 0.00e+00 GB AAA24476 "aspartate transcarbamoylase catalytic chain (pyrB) [Escherichia coli]" 100.00 311 99.03 100.00 0.00e+00 GB AAA97142 "aspartate carbomoyltransferase catalytic subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 311 98.39 99.68 0.00e+00 GB AAC77202 "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 311 98.71 100.00 0.00e+00 GB AAG59443 "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli O157:H7 str. EDL933]" 100.00 311 98.39 99.68 0.00e+00 PIR G86122 "hypothetical protein pyrB [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 100.00 311 98.39 99.68 0.00e+00 REF NP_313249 "aspartate carbamoyltransferase [Escherichia coli O157:H7 str. Sakai]" 100.00 311 98.71 100.00 0.00e+00 REF NP_418666 "aspartate carbamoyltransferase, catalytic subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 311 98.71 100.00 0.00e+00 REF NP_709956 "aspartate carbamoyltransferase [Shigella flexneri 2a str. 301]" 100.00 311 98.71 100.00 0.00e+00 REF WP_000002014 "aspartate carbamoyltransferase catalytic subunit [Escherichia coli]" 100.00 311 98.39 99.68 0.00e+00 REF WP_000013029 "aspartate carbamoyltransferase catalytic subunit [Escherichia coli]" 100.00 311 98.06 99.35 0.00e+00 SP A1AJF0 "RecName: Full=Aspartate carbamoyltransferase; AltName: Full=Aspartate transcarbamylase; Short=ATCase" 100.00 311 98.71 100.00 0.00e+00 SP A7ZVC7 "RecName: Full=Aspartate carbamoyltransferase; AltName: Full=Aspartate transcarbamylase; Short=ATCase" 100.00 311 98.71 100.00 0.00e+00 SP A8A803 "RecName: Full=Aspartate carbamoyltransferase; AltName: Full=Aspartate transcarbamylase; Short=ATCase" 100.00 311 98.71 100.00 0.00e+00 SP B1ISW0 "RecName: Full=Aspartate carbamoyltransferase; AltName: Full=Aspartate transcarbamylase; Short=ATCase" 100.00 311 98.71 100.00 0.00e+00 SP B1LRD2 "RecName: Full=Aspartate carbamoyltransferase; AltName: Full=Aspartate transcarbamylase; Short=ATCase" 100.00 311 98.71 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $aspartate_transcarbamoylase 'E. coli' 562 Eubacteria . Escherichia coli TR4363 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $aspartate_transcarbamoylase 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 . na temperature 283 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label p-dioxane C . . ppm 67.8 . . . . . $entry_citation $entry_citation 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'aspartate transcarbamoylase' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 134 HIS CG C 136.8 . 1 stop_ save_