HEADER TRANSFERASE (CARBAMOYL-P,ASPARTATE) 25-AUG-89 8ATC 8ATC 2 COMPND ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCARBAMYLASE) 8ATC 3 COMPND 2 (R STATE) (E.C.2.1.3.2) COMPLEX WITH 8ATC 4 COMPND 3 N-PHOSPHONACETYL-L-ASPARTATE (/PALA$) 8ATC 5 SOURCE (ESCHERICHIA $COLI) 8ATC 6 AUTHOR H.KE,W.N.LIPSCOMB,Y.CHO,R.B.HONZATKO 8ATC 7 REVDAT 1 15-OCT-90 8ATC 0 8ATC 8 JRNL AUTH H.KE,W.N.LIPSCOMB,Y.CHO,R.B.HONZATKO 8ATC 9 JRNL TITL COMPLEX OF N-*PHOSPHONACETYL-*L-ASPARTATE WITH 8ATC 10 JRNL TITL 2 ASPARTATE CARBAMOYLTRANSFERASE. X-RAY REFINEMENT, 8ATC 11 JRNL TITL 3 ANALYSIS OF CONFORMATIONAL CHANGES AND CATALYTIC 8ATC 12 JRNL TITL 4 AND ALLOSTERIC MECHANISMS 8ATC 13 JRNL REF J.MOL.BIOL. V. 204 725 1988 8ATC 14 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 8ATC 15 REMARK 1 8ATC 16 REMARK 1 REFERENCE 1 8ATC 17 REMARK 1 AUTH R.C.STEVENS,J.E.GOUAUX,W.N.LIPSCOMB 8ATC 18 REMARK 1 TITL STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE 8ATC 19 REMARK 1 TITL 2 T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL 8ATC 20 REMARK 1 TITL 3 STRUCTURES OF THE UNLIGATED AND /ATP$-, AND 8ATC 21 REMARK 1 TITL 4 /CTP$-*COMPLEXED ENZYMES AT 2.6-*ANGSTROMS 8ATC 22 REMARK 1 TITL 5 RESOLUTION 8ATC 23 REMARK 1 REF BIOCHEMISTRY V. 29 7691 1990 8ATC 24 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 8ATC 25 REMARK 1 REFERENCE 2 8ATC 26 REMARK 1 AUTH J.E.GOUAUX,R.C.STEVENS,W.N.LIPSCOMB 8ATC 27 REMARK 1 TITL CRYSTAL STRUCTURES OF ASPARTATE 8ATC 28 REMARK 1 TITL 2 CARBAMOYLTRANSFERASE LIGATED WITH 8ATC 29 REMARK 1 TITL 3 PHOSPHONOACETAMIDE, MALONATE, AND /CTP$ OR /ATP$ AT 8ATC 30 REMARK 1 TITL 4 2.8-*ANGSTROMS RESOLUTION AND NEUTRAL $P*H 8ATC 31 REMARK 1 REF BIOCHEMISTRY V. 29 7702 1990 8ATC 32 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 8ATC 33 REMARK 1 REFERENCE 3 8ATC 34 REMARK 1 AUTH J.E.GOUAUX,W.N.LIPSCOMB 8ATC 35 REMARK 1 TITL CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T 8ATC 36 REMARK 1 TITL 2 AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R 8ATC 37 REMARK 1 TITL 3 STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 8ATC 38 REMARK 1 TITL 4 2.8-*ANGSTROMS RESOLUTION AND NEUTRAL $P*H 8ATC 39 REMARK 1 REF BIOCHEMISTRY V. 29 389 1990 8ATC 40 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 8ATC 41 REMARK 1 REFERENCE 4 8ATC 42 REMARK 1 AUTH J.E.GOUAUX,W.N.LIPSCOMB 8ATC 43 REMARK 1 TITL STRUCTURAL TRANSITIONS IN CRYSTALS OF NATIVE 8ATC 44 REMARK 1 TITL 2 ASPARTATE CARBAMOYLTRANSFERASE 8ATC 45 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 86 845 1989 8ATC 46 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 8ATC 47 REMARK 1 REFERENCE 5 8ATC 48 REMARK 1 AUTH J.E.GOUAUX,W.N.LIPSCOMB,S.A.MIDDLETON, 8ATC 49 REMARK 1 AUTH 2 E.R.KANTROWITZ 8ATC 50 REMARK 1 TITL STRUCTURE OF A SINGLE AMINO ACID MUTANT OF 8ATC 51 REMARK 1 TITL 2 ASPARTATE CARBAMOYLTRANSFERASE AT 2.5-*ANGSTROMS 8ATC 52 REMARK 1 TITL 3 RESOLUTION. IMPLICATIONS FOR THE COOPERATIVE 8ATC 53 REMARK 1 TITL 4 MECHANISM 8ATC 54 REMARK 1 REF BIOCHEMISTRY V. 28 1798 1989 8ATC 55 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 8ATC 56 REMARK 1 REFERENCE 6 8ATC 57 REMARK 1 AUTH E.R.KANTROWITZ,W.N.LIPSCOMB 8ATC 58 REMARK 1 TITL ESCHERICHIA $COLI ASPARTATE TRANSCARBAMYLASE. 8ATC 59 REMARK 1 TITL 2 THE RELATION BETWEEN STRUCTURE AND FUNCTION 8ATC 60 REMARK 1 REF SCIENCE V. 241 669 1988 8ATC 61 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 038 8ATC 62 REMARK 1 REFERENCE 7 8ATC 63 REMARK 1 AUTH J.E.GOUAUX,W.N.LIPSCOMB 8ATC 64 REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF CARBAMOYL PHOSPHATE 8ATC 65 REMARK 1 TITL 2 AND SUCCINATE BOUND TO ASPARTATE 8ATC 66 REMARK 1 TITL 3 CARBAMOYLTRANSFERASE 8ATC 67 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 85 4205 1988 8ATC 68 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 8ATC 69 REMARK 1 REFERENCE 8 8ATC 70 REMARK 1 AUTH K.H.KIM,Z.PAN,R.B.HONZATKO,H.KE,W.N.LIPSCOMB 8ATC 71 REMARK 1 TITL STRUCTURAL ASYMMETRY IN THE /CTP$-LIGANDED FORM OF 8ATC 72 REMARK 1 TITL 2 ASPARTATE CARBAMOYLTRANSFERASE FROM ESCHERICHIA 8ATC 73 REMARK 1 TITL 3 $COLI 8ATC 74 REMARK 1 REF J.MOL.BIOL. V. 196 853 1987 8ATC 75 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 8ATC 76 REMARK 1 REFERENCE 9 8ATC 77 REMARK 1 AUTH K.L.KRAUSE,K.W.VOLZ,W.N.LIPSCOMB 8ATC 78 REMARK 1 TITL 2.5 ANGSTROMS STRUCTURE OF ASPARTATE 8ATC 79 REMARK 1 TITL 2 CARBAMOYLTRANSFERASE COMPLEXED WITH THE BISUBSTRATE 8ATC 80 REMARK 1 TITL 3 ANALOG N-(PHOSPHONACETYL)-*L-ASPARTATE 8ATC 81 REMARK 1 REF J.MOL.BIOL. V. 193 527 1987 8ATC 82 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 8ATC 83 REMARK 1 REFERENCE 10 8ATC 84 REMARK 1 AUTH J.E.GOUAUX,K.L.KRAUSE,W.N.LIPSCOMB 8ATC 85 REMARK 1 TITL THE CATALYTIC MECHANISM OF ESCHERICHIA $COLI 8ATC 86 REMARK 1 TITL 2 ASPARTATE CARBAMOYLTRANSFERASE. A MOLECULAR 8ATC 87 REMARK 1 TITL 3 MODELLING STUDY 8ATC 88 REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMM. V. 142 893 1987 8ATC 89 REMARK 1 REFN ASTM BBRCA9 US ISSN 0006-291X 146 8ATC 90 REMARK 1 REFERENCE 11 8ATC 91 REMARK 1 AUTH K.L.KRAUSE,K.W.VOLZ,W.N.LIPSCOMB 8ATC 92 REMARK 1 TITL STRUCTURE AT 2.9-*ANGSTROMS RESOLUTION OF ASPARTATE 8ATC 93 REMARK 1 TITL 2 CARBAMOYLTRANSFERASE COMPLEXED WITH THE BISUBSTRATE 8ATC 94 REMARK 1 TITL 3 ANALOGUE N-(PHOSPHONACETYL)-*L-ASPARTATE 8ATC 95 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 82 1643 1985 8ATC 96 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 8ATC 97 REMARK 1 REFERENCE 12 8ATC 98 REMARK 1 AUTH H.KE,R.B.HONZATKO,W.N.LIPSCOMB 8ATC 99 REMARK 1 TITL STRUCTURE OF UNLIGATED ASPARTATE 8ATC 100 REMARK 1 TITL 2 CARBAMOYLTRANSFERASE OF ESCHERICHIA $COLI AT 8ATC 101 REMARK 1 TITL 3 2.6-*ANGSTROMS RESOLUTION 8ATC 102 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 81 4037 1984 8ATC 103 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 8ATC 104 REMARK 1 REFERENCE 13 8ATC 105 REMARK 1 AUTH R.B.HONZATKO,J.L.CRAWFORD,H.L.MONACO,J.E.LADNER, 8ATC 106 REMARK 1 AUTH 2 B.F.P.EDWARDS,D.R.EVANS,S.G.WARREN,D.C.WILEY, 8ATC 107 REMARK 1 AUTH 3 R.C.LADNER,W.N.LIPSCOMB 8ATC 108 REMARK 1 TITL CRYSTAL AND MOLECULAR STRUCTURES OF NATIVE AND 8ATC 109 REMARK 1 TITL 2 /CTP$-LIGANDED ASPARTATE CARBAMOYLTRANSFERASE FROM 8ATC 110 REMARK 1 TITL 3 ESCHERICHIA $COLI 8ATC 111 REMARK 1 REF J.MOL.BIOL. V. 160 219 1982 8ATC 112 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 8ATC 113 REMARK 1 REFERENCE 14 8ATC 114 REMARK 1 AUTH R.B.HONZATKO,W.N.LIPSCOMB 8ATC 115 REMARK 1 TITL INTERACTIONS OF PHOSPHATE LIGANDS WITH ESCHERICHIA 8ATC 116 REMARK 1 TITL 2 $COLI ASPARTATE CARBAMOYLTRANSFERASE IN THE 8ATC 117 REMARK 1 TITL 3 CRYSTALLINE STATE 8ATC 118 REMARK 1 REF J.MOL.BIOL. V. 160 265 1982 8ATC 119 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 8ATC 120 REMARK 1 REFERENCE 15 8ATC 121 REMARK 1 AUTH R.B.HONZATKO,W.N.LIPSCOMB 8ATC 122 REMARK 1 TITL INTERACTIONS OF METAL-NUCLEOTIDE COMPLEXES WITH 8ATC 123 REMARK 1 TITL 2 ASPARTATE CARBAMOYLTRANSFERASE IN THE CRYSTALLINE 8ATC 124 REMARK 1 TITL 3 STATE 8ATC 125 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 79 7171 1982 8ATC 126 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 8ATC 127 REMARK 1 REFERENCE 16 8ATC 128 REMARK 1 AUTH J.E.LADNER,J.P.KITCHELL,R.B.HONZATKO,H.M.KE, 8ATC 129 REMARK 1 AUTH 2 K.W.VOLZ,A.J.KALB(GILBOA),R.C.LADNER,W.N.LIPSCOMB 8ATC 130 REMARK 1 TITL GROSS QUATERNARY CHANGES IN ASPARTATE 8ATC 131 REMARK 1 TITL 2 CARBAMOYLTRANSFERASE ARE INDUCED BY THE BINDING OF 8ATC 132 REMARK 1 TITL 3 N-($PHOSPHONACETYL)-*L-ASPARTATE. A 3.5-*ANGSTROMS 8ATC 133 REMARK 1 TITL 4 RESOLUTION STUDY 8ATC 134 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 79 3125 1982 8ATC 135 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 8ATC 136 REMARK 1 REFERENCE 17 8ATC 137 REMARK 1 AUTH R.B.HONZATKO,H.L.MONACO,W.N.LIPSCOMB 8ATC 138 REMARK 1 TITL A 3.0-*ANGSTROMS RESOLUTION STUDY OF NUCLEOTIDE 8ATC 139 REMARK 1 TITL 2 COMPLEXES WITH ASPARTATE CARBAMOYLTRANSFERASE 8ATC 140 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 76 5105 1979 8ATC 141 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 8ATC 142 REMARK 1 REFERENCE 18 8ATC 143 REMARK 1 AUTH H.L.MONACO,J.L.CRAWFORD,W.N.LIPSCOMB 8ATC 144 REMARK 1 TITL THREE-DIMENSIONAL STRUCTURES OF ASPARTATE 8ATC 145 REMARK 1 TITL 2 CARBAMOYLTRANSFERASE FROM ESCHERICHIA $COLI AND OF 8ATC 146 REMARK 1 TITL 3 ITS COMPLEX WITH CYTIDINE TRIPHOSPHATE 8ATC 147 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 75 5276 1978 8ATC 148 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 8ATC 149 REMARK 1 REFERENCE 19 8ATC 150 REMARK 1 AUTH W.N.LIPSCOMB,B.F.P.EDWARDS,D.R.EVANS, 8ATC 151 REMARK 1 AUTH 2 S.C.PASTRA-*LANDIS 8ATC 152 REMARK 1 TITL BINDING SITE AT 5.5 ANGSTROMS RESOLUTION OF 8ATC 153 REMARK 1 TITL 2 CYTIDINE TRIPHOSPHATE, THE ALLOSTERIC INHIBITOR OF 8ATC 154 REMARK 1 TITL 3 ASPARTATE TRANSCARBAMYLASE FROM ESCHERICHIA $COLI. 8ATC 155 REMARK 1 TITL 4 RELATION TO MECHANISMS OF CONTROL 8ATC 156 REMARK 1 EDIT M.SUNDARALINGAM,S.T.RAO 8ATC 157 REMARK 1 REF STRUCTURE AND CONFORMATION 333 1975 8ATC 158 REMARK 1 REF 2 OF NUCLEIC ACIDS AND 8ATC 159 REMARK 1 REF 3 PROTEIN-NUCLEIC ACID 8ATC 160 REMARK 1 REF 4 INTERACTIONS 8ATC 161 REMARK 1 PUBL UNIVERSITY PARK PRESS,BALTIMORE 8ATC 162 REMARK 1 REFN ASTM ISBN 0-8391-0764-1 992 8ATC 163 REMARK 1 REFERENCE 20 8ATC 164 REMARK 1 AUTH S.G.WARREN,B.F.P.EDWARDS,D.R.EVANS,D.C.WILEY, 8ATC 165 REMARK 1 AUTH 2 W.N.LIPSCOMB 8ATC 166 REMARK 1 TITL ASPARTATE TRANSCARBAMOYLASE FROM ESCHERICHIA $COLI. 8ATC 167 REMARK 1 TITL 2 ELECTRON DENSITY AT 5.5 ANGSTROMS RESOLUTION 8ATC 168 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 70 1117 1973 8ATC 169 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 8ATC 170 REMARK 2 8ATC 171 REMARK 2 RESOLUTION. 2.5 ANGSTROMS. 8ATC 172 REMARK 3 8ATC 173 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST-SQUARES PROCEDURE OF J. 8ATC 174 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*) WITH SLIGHT 8ATC 175 REMARK 3 MODIFICATIONS TO ACCOMMODATE THE ROUTINES OF JACK AND 8ATC 176 REMARK 3 LEVITT (1978). THE R VALUE IS 0.165. 8ATC 177 REMARK 3 8ATC 178 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 8ATC 179 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 8ATC 180 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 8ATC 181 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 8ATC 182 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 8ATC 183 REMARK 3 BOND DISTANCE 0.014(0.02) 8ATC 184 REMARK 3 ANGLE DISTANCE 0.037(0.03) 8ATC 185 REMARK 3 PLANAR 1-4 DISTANCE 0.055(0.06) 8ATC 186 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.011(0.02) 8ATC 187 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.149(0.15) 8ATC 188 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 8ATC 189 REMARK 3 SINGLE TORSION CONTACT 0.206(0.50) 8ATC 190 REMARK 3 MULTIPLE TORSION CONTACT 0.243(0.50) 8ATC 191 REMARK 3 POSSIBLE HYDROGEN BOND 0.224(0.50) 8ATC 192 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 8ATC 193 REMARK 3 PLANAR (OMEGA) 2.1(3.0) 8ATC 194 REMARK 3 STAGGERED 17.7(15.0) 8ATC 195 REMARK 3 ORTHONORMAL 31.1(20.0) 8ATC 196 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 8ATC 197 REMARK 3 MAIN-CHAIN BOND 1.599(1.5) 8ATC 198 REMARK 3 MAIN-CHAIN ANGLE 2.815(2.0) 8ATC 199 REMARK 3 SIDE-CHAIN BOND 2.396(2.0) 8ATC 200 REMARK 3 SIDE-CHAIN ANGLE 4.085(3.0) 8ATC 201 REMARK 4 8ATC 202 REMARK 4 THE ENZYME IS A DODECAMER COMPOSED OF SIX CATALYTIC CHAINS 8ATC 203 REMARK 4 AND SIX REGULATORY CHAINS THAT CAN BE DISSOCIATED INTO 8ATC 204 REMARK 4 SUBUNITS. THE ASYMMETRIC UNIT OF THE CRYSTAL CONSISTS OF 8ATC 205 REMARK 4 ONE THIRD OF THE MOLECULE - TWO CATALYTIC AND TWO 8ATC 206 REMARK 4 REGULATORY CHAINS. CHAINS *A* AND *C* (REFERRED TO AS C1 8ATC 207 REMARK 4 AND C6 RESPECTIVELY IN THE *JRNL* REFERENCE ABOVE) ARE THE 8ATC 208 REMARK 4 CATALYTIC CHAINS CONSISTING OF 310 RESIDUES EACH. CHAINS 8ATC 209 REMARK 4 *B* AND *D* (REFERRED TO AS R1 AND R6 RESPECTIVELY IN THE 8ATC 210 REMARK 4 *JRNL* REFERENCE ABOVE) ARE THE REGULATORY CHAINS 8ATC 211 REMARK 4 CONSISTING OF 153 RESIDUES EACH. 8ATC 212 REMARK 5 8ATC 213 REMARK 5 THERE IS A NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS WHICH 8ATC 214 REMARK 5 RELATES THE *A* AND *B* CHAINS TO THE *C* AND *D* CHAINS. 8ATC 215 REMARK 6 8ATC 216 REMARK 6 DUE TO WEAK ELECTRON DENSITY FOR RESIDUES 1 THROUGH 7 OF 8ATC 217 REMARK 6 CHAINS *B* AND *D*, THESE RESIDUES HAVE BEEN OMITTED FROM 8ATC 218 REMARK 6 THE MODEL. 8ATC 219 REMARK 7 8ATC 220 REMARK 7 SITES *PAA* AND *PAC* AS SPECIFIED ON THE *SITE* RECORDS 8ATC 221 REMARK 7 BELOW ARE THE *PAL* BINDING SITES OF CHAINS *A* AND *C* 8ATC 222 REMARK 7 RESPECTIVELY. SITES *ZNB* AND *ZND* ARE THE *ZN* BINDING 8ATC 223 REMARK 7 SITES OF CHAINS *B* AND *D* RESPECTIVELY. 8ATC 224 REMARK 8 8ATC 225 REMARK 8 COORDINATES FOR UNLIGANDED FORMS OF THIS ENZYME ARE 8ATC 226 REMARK 8 AVAILABLE AS SEPARATE ENTRIES IN THE PROTEIN DATA BANK. 8ATC 227 SEQRES 1 A 310 ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN 8ATC 228 SEQRES 2 A 310 ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR 8ATC 229 SEQRES 3 A 310 ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU 8ATC 230 SEQRES 4 A 310 LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER 8ATC 231 SEQRES 5 A 310 THR ARG THR ARG LEU SER PHE GLN THR SER MET HIS ARG 8ATC 232 SEQRES 6 A 310 LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN 8ATC 233 SEQRES 7 A 310 THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR 8ATC 234 SEQRES 8 A 310 ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET 8ATC 235 SEQRES 9 A 310 ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU 8ATC 236 SEQRES 10 A 310 PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY 8ATC 237 SEQRES 11 A 310 SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE 8ATC 238 SEQRES 12 A 310 THR ILE GLN GLN THR GLU GLY ARG LEU ASP ASN LEU HIS 8ATC 239 SEQRES 13 A 310 VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL 8ATC 240 SEQRES 14 A 310 HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN 8ATC 241 SEQRES 15 A 310 ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO 8ATC 242 SEQRES 16 A 310 GLU TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA 8ATC 243 SEQRES 17 A 310 TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU 8ATC 244 SEQRES 18 A 310 VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG 8ATC 245 SEQRES 19 A 310 LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE 8ATC 246 SEQRES 20 A 310 VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN 8ATC 247 SEQRES 21 A 310 MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE 8ATC 248 SEQRES 22 A 310 ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE 8ATC 249 SEQRES 23 A 310 GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU 8ATC 250 SEQRES 24 A 310 LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU 8ATC 251 SEQRES 1 B 153 MET THR HIS ASP ASN LYS LEU GLY VAL GLU ALA ILE LYS 8ATC 252 SEQRES 2 B 153 ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY 8ATC 253 SEQRES 3 B 153 PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP 8ATC 254 SEQRES 4 B 153 GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU 8ATC 255 SEQRES 5 B 153 MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE 8ATC 256 SEQRES 6 B 153 LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA 8ATC 257 SEQRES 7 B 153 PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL 8ATC 258 SEQRES 8 B 153 VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASN 8ATC 259 SEQRES 9 B 153 ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS 8ATC 260 SEQRES 10 B 153 ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG 8ATC 261 SEQRES 11 B 153 ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS 8ATC 262 SEQRES 12 B 153 GLU PHE SER HIS ASN VAL VAL LEU ALA ASN 8ATC 263 SEQRES 1 C 310 ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN 8ATC 264 SEQRES 2 C 310 ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR 8ATC 265 SEQRES 3 C 310 ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU 8ATC 266 SEQRES 4 C 310 LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER 8ATC 267 SEQRES 5 C 310 THR ARG THR ARG LEU SER PHE GLN THR SER MET HIS ARG 8ATC 268 SEQRES 6 C 310 LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN 8ATC 269 SEQRES 7 C 310 THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR 8ATC 270 SEQRES 8 C 310 ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET 8ATC 271 SEQRES 9 C 310 ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU 8ATC 272 SEQRES 10 C 310 PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY 8ATC 273 SEQRES 11 C 310 SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE 8ATC 274 SEQRES 12 C 310 THR ILE GLN GLN THR GLU GLY ARG LEU ASP ASN LEU HIS 8ATC 275 SEQRES 13 C 310 VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL 8ATC 276 SEQRES 14 C 310 HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN 8ATC 277 SEQRES 15 C 310 ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO 8ATC 278 SEQRES 16 C 310 GLU TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA 8ATC 279 SEQRES 17 C 310 TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU 8ATC 280 SEQRES 18 C 310 VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG 8ATC 281 SEQRES 19 C 310 LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE 8ATC 282 SEQRES 20 C 310 VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN 8ATC 283 SEQRES 21 C 310 MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE 8ATC 284 SEQRES 22 C 310 ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE 8ATC 285 SEQRES 23 C 310 GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU 8ATC 286 SEQRES 24 C 310 LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU 8ATC 287 SEQRES 1 D 153 MET THR HIS ASP ASN LYS LEU GLY VAL GLU ALA ILE LYS 8ATC 288 SEQRES 2 D 153 ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY 8ATC 289 SEQRES 3 D 153 PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP 8ATC 290 SEQRES 4 D 153 GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU 8ATC 291 SEQRES 5 D 153 MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE 8ATC 292 SEQRES 6 D 153 LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA 8ATC 293 SEQRES 7 D 153 PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL 8ATC 294 SEQRES 8 D 153 VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASN 8ATC 295 SEQRES 9 D 153 ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS 8ATC 296 SEQRES 10 D 153 ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG 8ATC 297 SEQRES 11 D 153 ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS 8ATC 298 SEQRES 12 D 153 GLU PHE SER HIS ASN VAL VAL LEU ALA ASN 8ATC 299 FTNOTE 1 8ATC 300 FTNOTE 1 RESIDUES PRO A 268 AND PRO C 268 ARE CIS-PROLINES. 8ATC 301 HET PAL A 311 16 N-(PHOSPHONACETYL)-L-ASPARTATE 8ATC 302 HET ZN B 154 1 ZINC ION BOUND TO THE REGULATORY CHAIN 8ATC 303 HET PAL C 311 16 N-(PHOSPHONACETYL)-L-ASPARTATE 8ATC 304 HET ZN D 154 1 ZINC ION BOUND TO THE REGULATORY CHAIN 8ATC 305 FORMUL 5 PAL 2(C6 H7 N1 O8 P1) 8ATC 306 FORMUL 6 ZN 2(ZN1 ++) 8ATC 307 FORMUL 7 HOH *932(H2 O1) 8ATC 308 HELIX 1 H1A ARG A 17 ALA A 32 1 8ATC 309 HELIX 2 H2A THR A 53 LEU A 66 1 8ATC 310 HELIX 3 H3A ALA A 89 VAL A 99 1 8ATC 311 HELIX 4 H4A ALA A 111 SER A 119 1 8ATC 312 HELIX 5 H5A PRO A 135 GLU A 149 1 8ATC 313 HELIX 6 H6A ARG A 167 PHE A 179 1 8ATC 314 HELIX 7 H7A GLU A 196 LYS A 205 1 8ATC 315 HELIX 8 H8A ILE A 215 ALA A 220 1 8ATC 316 HELIX 9 H0A ALA A 251 ASN A 256 1 8ATC 317 HELIX 10 HEA THR A 275 LYS A 279 1 8ATC 318 HELIX 11 HTA TYR A 285 LEU A 304 1 8ATC 319 HELIX 12 H1B ILE B 25 PHE B 33 1 8ATC 320 HELIX 13 H2B ASP B 69 TYR B 77 5 ENDS TYPE 1 8ATC 321 HELIX 14 H3B HIS B 147 VAL B 150 1 8ATC 322 HELIX 15 H1C ARG C 17 ALA C 32 1 8ATC 323 HELIX 16 H2C THR C 53 LEU C 66 1 8ATC 324 HELIX 17 H3C ALA C 89 VAL C 99 1 8ATC 325 HELIX 18 H4C ALA C 111 SER C 119 1 8ATC 326 HELIX 19 H5C PRO C 135 GLU C 149 1 8ATC 327 HELIX 20 H6C ARG C 167 PHE C 179 1 8ATC 328 HELIX 21 H7C GLU C 196 LYS C 205 1 8ATC 329 HELIX 22 H8C ILE C 215 ALA C 220 1 8ATC 330 HELIX 23 H0C ALA C 251 ASN C 256 1 8ATC 331 HELIX 24 HEC THR C 275 LYS C 279 1 8ATC 332 HELIX 25 HTC TYR C 285 LEU C 304 1 8ATC 333 HELIX 26 H1D ILE D 25 PHE D 33 1 8ATC 334 HELIX 27 H2D ASP D 69 TYR D 77 5 ENDS TYPE 1 8ATC 335 HELIX 28 H3D HIS D 147 VAL D 150 1 8ATC 336 SHEET 1 C1A 5 LYS A 7 ILE A 9 0 8ATC 337 SHEET 2 C1A 5 PRO A 123 ALA A 127 1 8ATC 338 SHEET 3 C1A 5 ALA A 101 HIS A 106 1 8ATC 339 SHEET 4 C1A 5 LYS A 42 PHE A 48 1 8ATC 340 SHEET 5 C1A 5 ALA A 68 SER A 74 1 8ATC 341 SHEET 1 C2A 6 ALA A 208 HIS A 212 0 8ATC 342 SHEET 2 C2A 6 ASN A 182 ALA A 188 1 8ATC 343 SHEET 3 C2A 6 LEU A 155 VAL A 160 1 8ATC 344 SHEET 4 C2A 6 ILE A 224 VAL A 230 1 8ATC 345 SHEET 5 C2A 6 LYS A 262 HIS A 265 1 8ATC 346 SHEET 6 C2A 6 PRO A 281 ALA A 283 1 8ATC 347 SHEET 1 R1B 5 ARG B 41 LEU B 46 0 8ATC 348 SHEET 2 R1B 5 ARG B 55 GLU B 62 -1 8ATC 349 SHEET 3 R1B 5 ARG B 14 ASP B 19 -1 8ATC 350 SHEET 4 R1B 5 THR B 82 ASP B 87 -1 8ATC 351 SHEET 5 R1B 5 GLY B 93 PRO B 97 -1 8ATC 352 SHEET 1 R2B 4 GLU B 101 ASP B 104 0 8ATC 353 SHEET 2 R2B 4 SER B 123 LYS B 129 -1 8ATC 354 SHEET 3 R2B 4 ILE B 134 CYS B 138 -1 8ATC 355 SHEET 4 R2B 4 LYS B 143 SER B 146 -1 8ATC 356 SHEET 1 C1C 5 LYS C 7 ILE C 9 0 8ATC 357 SHEET 2 C1C 5 PRO C 123 ALA C 127 1 8ATC 358 SHEET 3 C1C 5 ALA C 101 HIS C 106 1 8ATC 359 SHEET 4 C1C 5 LYS C 42 PHE C 48 1 8ATC 360 SHEET 5 C1C 5 ALA C 68 SER C 74 1 8ATC 361 SHEET 1 C2C 6 ALA C 208 HIS C 212 0 8ATC 362 SHEET 2 C2C 6 ASN C 182 ALA C 188 1 8ATC 363 SHEET 3 C2C 6 LEU C 155 VAL C 160 1 8ATC 364 SHEET 4 C2C 6 ILE C 224 VAL C 230 1 8ATC 365 SHEET 5 C2C 6 LYS C 262 HIS C 265 1 8ATC 366 SHEET 6 C2C 6 PRO C 281 ALA C 283 1 8ATC 367 SHEET 1 R1D 5 ARG D 41 LEU D 46 0 8ATC 368 SHEET 2 R1D 5 ARG D 55 GLU D 62 -1 8ATC 369 SHEET 3 R1D 5 ARG D 14 ASP D 19 -1 8ATC 370 SHEET 4 R1D 5 THR D 82 ASP D 87 -1 8ATC 371 SHEET 5 R1D 5 GLY D 93 PRO D 97 -1 8ATC 372 SHEET 1 R2D 4 GLU D 101 ASP D 104 0 8ATC 373 SHEET 2 R2D 4 SER D 123 LYS D 129 -1 8ATC 374 SHEET 3 R2D 4 ILE D 134 CYS D 138 -1 8ATC 375 SHEET 4 R2D 4 LYS D 143 SER D 146 -1 8ATC 376 TURN 1 T1A SER A 11 ASP A 14 TYPE III 8ATC 377 TURN 2 T2A ASP A 129 ASN A 132 TYPE I 8ATC 378 TURN 3 T3A PRO A 189 LEU A 192 TYPE I 8ATC 379 TURN 4 T1C SER C 11 ASP C 14 TYPE III 8ATC 380 TURN 5 T2C ASP C 129 ASN C 132 TYPE I 8ATC 381 TURN 6 T3C PRO C 189 LEU C 192 TYPE I 8ATC 382 SITE 1 PAA 9 SER A 52 ARG A 54 THR A 55 SER A 80 8ATC 383 SITE 2 PAA 9 LYS A 84 HIS A 134 ARG A 167 ARG A 229 8ATC 384 SITE 3 PAA 9 GLN A 231 8ATC 385 SITE 1 ZNB 4 CYS B 109 CYS B 114 CYS B 138 CYS B 141 8ATC 386 SITE 1 PAC 9 SER C 52 ARG C 54 THR C 55 SER C 80 8ATC 387 SITE 2 PAC 9 LYS C 84 HIS C 134 ARG C 167 ARG C 229 8ATC 388 SITE 3 PAC 9 GLN C 231 8ATC 389 SITE 1 ZND 4 CYS D 109 CYS D 114 CYS D 138 CYS D 141 8ATC 390 CRYST1 122.110 122.110 156.170 90.00 90.00 120.00 P 3 2 1 2 8ATC 391 ORIGX1 1.000000 0.577350 0.000000 0.00000 8ATC 392 ORIGX2 0.000000 1.154701 0.000000 0.00000 8ATC 393 ORIGX3 0.000000 0.000000 1.000000 0.00000 8ATC 394 SCALE1 0.008189 0.010188 0.000000 0.00000 8ATC 395 SCALE2 0.000000 0.010919 0.000000 0.00000 8ATC 396 SCALE3 0.000000 0.000000 0.006403 0.00000 8ATC 397