HEADER ISOMERASE(INTRAMOLECULAR OXIDOREDUCTSE) 05-JUL-89 4XIA 4XIAA 1 COMPND D-*XYLOSE ISOMERASE (E.C.5.3.1.5), D-*SORBITOL COMPLEX 4XIA 4 SOURCE (ARTHROBACTER, STRAIN B3728) 4XIA 5 AUTHOR K.HENRICK,C.A.COLLYER,D.M.BLOW 4XIA 6 REVDAT 2 15-JAN-91 4XIAA 1 HEADER 4XIAA 2 REVDAT 1 15-APR-90 4XIA 0 4XIA 7 JRNL AUTH K.HENRICK,C.A.COLLYER,D.M.BLOW 4XIA 8 JRNL TITL STRUCTURES OF D-*XYLOSE ISOMERASE FROM ARTHROBACTER 4XIA 9 JRNL TITL 2 STRAIN B3728 CONTAINING THE INHIBITORS XYLITOL AND 4XIA 10 JRNL TITL 3 D-*SORBITOL AT 2.5 ANGSTROMS AND 2.3 ANGSTROMS 4XIA 11 JRNL TITL 4 RESOLUTION, RESPECTIVELY 4XIA 12 JRNL REF J.MOL.BIOL. V. 208 129 1989 4XIA 13 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 4XIA 14 REMARK 1 4XIA 15 REMARK 1 REFERENCE 1 4XIA 16 REMARK 1 AUTH K.HENRICK,D.M.BLOW,H.L.CARRELL,J.P.GLUSKER 4XIA 17 REMARK 1 TITL COMPARISON OF BACKBONE STRUCTURES OF GLUCOSE 4XIA 18 REMARK 1 TITL 2 ISOMERASE FROM STREPTOMYCES AND ARTHROBACTER 4XIA 19 REMARK 1 REF PROTEIN ENG. V. 1 467 1987 4XIA 20 REMARK 1 REFN ASTM PRENE9 UK ISSN 0269-2139 859 4XIA 21 REMARK 1 REFERENCE 2 4XIA 22 REMARK 1 AUTH J.AKINS,P.BRICK,H.B.JONES,N.HIRAYAMA,P.-*C.SHAW, 4XIA 23 REMARK 1 AUTH 2 D.M.BLOW 4XIA 24 REMARK 1 TITL THE CRYSTALLIZATION OF GLUCOSE ISOMERASE FROM 4XIA 25 REMARK 1 TITL 2 ARTHROBACTER B3728 4XIA 26 REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V. 874 375 1986 4XIA 27 REMARK 1 REFN ASTM BBACAQ NE ISSN 0006-3002 113 4XIA 28 REMARK 2 4XIA 29 REMARK 2 RESOLUTION. 2.3 ANGSTROMS. 4XIA 30 REMARK 3 4XIA 31 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST SQUARES PROCEDURE OF J. 4XIA 32 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*). THE R 4XIA 33 REMARK 3 VALUE IS 0.156 FOR 43615 REFLECTIONS IN THE RESOLUTION 4XIA 34 REMARK 3 RANGE 10.0 TO 2.3 ANGSTROMS. THE R VALUE IS 0.147 FOR 4XIA 35 REMARK 3 41617 REFLECTIONS IN THE RESOLUTION RANGE 6.0 TO 2.3 4XIA 36 REMARK 3 ANGSTROMS. 4XIA 37 REMARK 3 4XIA 38 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 4XIA 39 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 4XIA 40 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 4XIA 41 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 4XIA 42 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 4XIA 43 REMARK 3 BOND DISTANCE 0.020(0.025) 4XIA 44 REMARK 3 ANGLE DISTANCE 0.046(0.040) 4XIA 45 REMARK 3 PLANAR 1-4 DISTANCE 0.053(0.050) 4XIA 46 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.015(0.020) 4XIA 47 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.150(0.150) 4XIA 48 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 4XIA 49 REMARK 3 SINGLE TORSION CONTACT 0.160(0.200) 4XIA 50 REMARK 3 MULTIPLE TORSION CONTACT 0.220(0.200) 4XIA 51 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 4XIA 52 REMARK 3 STAGGERED 15.7(15.0) 4XIA 53 REMARK 3 TRANSVERSE 33.1(45.0) 4XIA 54 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 4XIA 55 REMARK 3 MAIN-CHAIN BOND 0.91(1.5) 4XIA 56 REMARK 3 MAIN-CHAIN ANGLE 1.46(2.0) 4XIA 57 REMARK 3 SIDE-CHAIN BOND 1.95(2.0) 4XIA 58 REMARK 3 SIDE-CHAIN ANGLE 2.98(3.0) 4XIA 59 REMARK 4 4XIA 60 REMARK 4 THE MOLECULE IS A TETRAMER CONTAINING TWO SUBUNITS IN THE 4XIA 61 REMARK 4 CRYSTALLOGRAPHIC ASYMMETRIC UNIT RELATED BY AN APPROXIMATE 4XIA 62 REMARK 4 TWO-FOLD AXIS. THESE SUBUNITS HAVE BEEN ASSIGNED CHAIN 4XIA 63 REMARK 4 IDENTIFIERS *A* AND *B* IN THIS ENTRY. THE TRANSFORMATION 4XIA 64 REMARK 4 PRESENTED ON THE *MTRIX* RECORDS BELOW WILL YIELD 4XIA 65 REMARK 4 APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO CHAIN 4XIA 66 REMARK 4 *B*. 4XIA 67 REMARK 5 4XIA 68 REMARK 5 THE TWO SHEETS PRESENTED AS *BAA* AND *BAB* ON SHEET 4XIA 69 REMARK 5 RECORDS BELOW ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS. 4XIA 70 REMARK 5 EACH IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE 4XIA 71 REMARK 5 FIRST AND LAST STRANDS ARE IDENTICAL. 4XIA 72 REMARK 6 4XIA 73 REMARK 6 THE WATER MOLECULES ARE NUMBERED FROM 401A AND 401B 4XIA 74 REMARK 6 ONWARDS, ACCORDING TO THE SUBUNIT TO WHICH THEY MOST 4XIA 75 REMARK 6 CLOSELY CORRESPOND. THERE ARE 538 WATER MOLECULES IN THIS 4XIA 76 REMARK 6 ENTRY. THE NUMBERS QUOTED IN THE *JRNL* REFERENCE ABOVE 4XIA 77 REMARK 6 ARE INCORRECT. 4XIA 78 REMARK 7 4XIA 79 REMARK 7 THE CD-NE-CZ ANGLE OF ARG A 158 DEVIATES SIGNIFICANTLY FROM 4XIA 80 REMARK 7 THE EXPECTED VALUE AND IS LIKELY TO BE INCORRECT. 4XIA 81 REMARK 8 4XIA 82 REMARK 8 THERE ARE MAJOR DISCREPANCIES BETWEEN THIS MODEL OF 4XIA 83 REMARK 8 XYLOSE ISOMERASE AND THAT PRESENTED IN PROTEIN DATA BANK 4XIA 84 REMARK 8 ENTRY 3XIA (G.K.FARBER ET AL., BIOCHEMISTRY, V. 28, P. 4XIA 85 REMARK 8 7289 (1989)). THE ALMOST IDENTICAL STRUCTURES OF 4XIA 86 REMARK 8 ARTHROBACTER AND STREPTOMYCES RUBIGINOSUS XYLOSE 4XIA 87 REMARK 8 ISOMERASES (K.HENRICK ET AL., PROTEIN. ENG., V. 1, P. 467 4XIA 88 REMARK 8 (1987)) AND SEQUENCE HOMOLOGIES SUGGEST THAT 3XIA SHOULD BE 4XIA 89 REMARK 8 STRUCTURALLY EQUIVALENT. 4XIA 90 REMARK 9 4XIAA 3 REMARK 9 CORRECTION. STANDARDIZE CLASSIFICATION ON HEADER RECORD. 4XIAA 4 REMARK 9 15-JAN-91. 4XIAA 5 SEQRES 1 A 393 VAL GLN PRO THR PRO ALA ASP HIS PHE THR PHE GLY LEU 4XIA 91 SEQRES 2 A 393 TRP THR VAL GLY TRP THR GLY ALA ASP PRO PHE GLY VAL 4XIA 92 SEQRES 3 A 393 ALA THR ARG ALA ASN LEU ASP PRO VAL GLU ALA VAL HIS 4XIA 93 SEQRES 4 A 393 LYS LEU ALA GLU LEU GLY ALA TYR GLY ILE THR PHE HIS 4XIA 94 SEQRES 5 A 393 ASP ASN ASP LEU ILE PRO PHE ASP ALA THR ALA ALA GLU 4XIA 95 SEQRES 6 A 393 ARG GLU LYS ILE LEU GLY ASP PHE ASN GLN ALA LEU ALA 4XIA 96 SEQRES 7 A 393 ASP THR GLY LEU LYS VAL PRO MET VAL THR THR ASN LEU 4XIA 97 SEQRES 8 A 393 PHE SER HIS PRO VAL PHE LYS ASP GLY GLY PHE THR SER 4XIA 98 SEQRES 9 A 393 ASN ASP ARG SER ILE ARG ARG PHE ALA LEU ALA LYS VAL 4XIA 99 SEQRES 10 A 393 LEU HIS ASN ILE ASP LEU ALA ALA GLU MET GLY ALA GLU 4XIA 100 SEQRES 11 A 393 THR PHE VAL MET TRP GLY GLY ARG GLU GLY SER GLU TYR 4XIA 101 SEQRES 12 A 393 ASP GLY SER LYS ASP LEU ALA ALA ALA LEU ASP ARG MET 4XIA 102 SEQRES 13 A 393 ARG GLU GLY VAL ASP THR ALA ALA GLY TYR ILE LYS ASP 4XIA 103 SEQRES 14 A 393 LYS GLY TYR ASN LEU ARG ILE ALA LEU GLU PRO LYS PRO 4XIA 104 SEQRES 15 A 393 ASN GLU PRO ARG GLY ASP ILE PHE LEU PRO THR VAL GLY 4XIA 105 SEQRES 16 A 393 HIS GLY LEU ALA PHE ILE GLU GLN LEU GLU HIS GLY ASP 4XIA 106 SEQRES 17 A 393 ILE VAL GLY LEU ASN PRO GLU THR GLY HIS GLU GLN MET 4XIA 107 SEQRES 18 A 393 ALA GLY LEU ASN PHE THR HIS GLY ILE ALA GLN ALA LEU 4XIA 108 SEQRES 19 A 393 TRP ALA GLU LYS LEU PHE HIS ILE ASP LEU ASN GLY GLN 4XIA 109 SEQRES 20 A 393 ARG GLY ILE LYS TYR ASP GLN ASP LEU VAL PHE GLY HIS 4XIA 110 SEQRES 21 A 393 GLY ASP LEU THR SER ALA PHE PHE THR VAL ASP LEU LEU 4XIA 111 SEQRES 22 A 393 GLU ASN GLY PHE PRO ASN GLY GLY PRO LYS TYR THR GLY 4XIA 112 SEQRES 23 A 393 PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR ASP GLY 4XIA 113 SEQRES 24 A 393 TYR ASP GLY VAL TRP ASP SER ALA LYS ALA ASN MET SER 4XIA 114 SEQRES 25 A 393 MET TYR LEU LEU LEU LYS GLU ARG ALA LEU ALA PHE ARG 4XIA 115 SEQRES 26 A 393 ALA ASP PRO GLU VAL GLN GLU ALA MET LYS THR SER GLY 4XIA 116 SEQRES 27 A 393 VAL PHE GLU LEU GLY GLU THR THR LEU ASN ALA GLY GLU 4XIA 117 SEQRES 28 A 393 SER ALA ALA ASP LEU MET ASN ASP SER ALA SER PHE ALA 4XIA 118 SEQRES 29 A 393 GLY PHE ASP ALA GLU ALA ALA ALA GLU ARG ASN PHE ALA 4XIA 119 SEQRES 30 A 393 PHE ILE ARG LEU ASN GLN LEU ALA ILE GLU HIS LEU LEU 4XIA 120 SEQRES 31 A 393 GLY SER ARG 4XIA 121 SEQRES 1 B 393 VAL GLN PRO THR PRO ALA ASP HIS PHE THR PHE GLY LEU 4XIA 122 SEQRES 2 B 393 TRP THR VAL GLY TRP THR GLY ALA ASP PRO PHE GLY VAL 4XIA 123 SEQRES 3 B 393 ALA THR ARG ALA ASN LEU ASP PRO VAL GLU ALA VAL HIS 4XIA 124 SEQRES 4 B 393 LYS LEU ALA GLU LEU GLY ALA TYR GLY ILE THR PHE HIS 4XIA 125 SEQRES 5 B 393 ASP ASN ASP LEU ILE PRO PHE ASP ALA THR ALA ALA GLU 4XIA 126 SEQRES 6 B 393 ARG GLU LYS ILE LEU GLY ASP PHE ASN GLN ALA LEU ALA 4XIA 127 SEQRES 7 B 393 ASP THR GLY LEU LYS VAL PRO MET VAL THR THR ASN LEU 4XIA 128 SEQRES 8 B 393 PHE SER HIS PRO VAL PHE LYS ASP GLY GLY PHE THR SER 4XIA 129 SEQRES 9 B 393 ASN ASP ARG SER ILE ARG ARG PHE ALA LEU ALA LYS VAL 4XIA 130 SEQRES 10 B 393 LEU HIS ASN ILE ASP LEU ALA ALA GLU MET GLY ALA GLU 4XIA 131 SEQRES 11 B 393 THR PHE VAL MET TRP GLY GLY ARG GLU GLY SER GLU TYR 4XIA 132 SEQRES 12 B 393 ASP GLY SER LYS ASP LEU ALA ALA ALA LEU ASP ARG MET 4XIA 133 SEQRES 13 B 393 ARG GLU GLY VAL ASP THR ALA ALA GLY TYR ILE LYS ASP 4XIA 134 SEQRES 14 B 393 LYS GLY TYR ASN LEU ARG ILE ALA LEU GLU PRO LYS PRO 4XIA 135 SEQRES 15 B 393 ASN GLU PRO ARG GLY ASP ILE PHE LEU PRO THR VAL GLY 4XIA 136 SEQRES 16 B 393 HIS GLY LEU ALA PHE ILE GLU GLN LEU GLU HIS GLY ASP 4XIA 137 SEQRES 17 B 393 ILE VAL GLY LEU ASN PRO GLU THR GLY HIS GLU GLN MET 4XIA 138 SEQRES 18 B 393 ALA GLY LEU ASN PHE THR HIS GLY ILE ALA GLN ALA LEU 4XIA 139 SEQRES 19 B 393 TRP ALA GLU LYS LEU PHE HIS ILE ASP LEU ASN GLY GLN 4XIA 140 SEQRES 20 B 393 ARG GLY ILE LYS TYR ASP GLN ASP LEU VAL PHE GLY HIS 4XIA 141 SEQRES 21 B 393 GLY ASP LEU THR SER ALA PHE PHE THR VAL ASP LEU LEU 4XIA 142 SEQRES 22 B 393 GLU ASN GLY PHE PRO ASN GLY GLY PRO LYS TYR THR GLY 4XIA 143 SEQRES 23 B 393 PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR ASP GLY 4XIA 144 SEQRES 24 B 393 TYR ASP GLY VAL TRP ASP SER ALA LYS ALA ASN MET SER 4XIA 145 SEQRES 25 B 393 MET TYR LEU LEU LEU LYS GLU ARG ALA LEU ALA PHE ARG 4XIA 146 SEQRES 26 B 393 ALA ASP PRO GLU VAL GLN GLU ALA MET LYS THR SER GLY 4XIA 147 SEQRES 27 B 393 VAL PHE GLU LEU GLY GLU THR THR LEU ASN ALA GLY GLU 4XIA 148 SEQRES 28 B 393 SER ALA ALA ASP LEU MET ASN ASP SER ALA SER PHE ALA 4XIA 149 SEQRES 29 B 393 GLY PHE ASP ALA GLU ALA ALA ALA GLU ARG ASN PHE ALA 4XIA 150 SEQRES 30 B 393 PHE ILE ARG LEU ASN GLN LEU ALA ILE GLU HIS LEU LEU 4XIA 151 SEQRES 31 B 393 GLY SER ARG 4XIA 152 FTNOTE 1 4XIA 153 FTNOTE 1 RESIDUES PRO A 186 AND PRO B 186 ARE CIS PROLINES. 4XIA 154 FTNOTE 2 4XIA 155 FTNOTE 2 THE CD-NE-CZ ANGLE OF ARG A 158 DEVIATES SIGNIFICANTLY FROM 4XIA 156 FTNOTE 2 THE EXPECTED VALUE AND IS LIKELY TO BE INCORRECT. 4XIA 157 HET MG A 399 1 MAGNESIUM ++ CATION 4XIA 158 HET SOR A 400 12 D-SORBITOL 4XIA 159 HET MG B 399 1 MAGNESIUM ++ CATION 4XIA 160 HET SOR B 400 12 D-SORBITOL 4XIA 161 FORMUL 3 MG 2(MG1 ++) 4XIA 162 FORMUL 4 SOR 2(C6 H14 O6) 4XIA 163 FORMUL 5 HOH *538(H2 O1) 4XIA 164 HELIX 1 A0 LEU A 14 VAL A 17 5 4XIA 165 HELIX 2 A1 PRO A 35 LEU A 45 1 4XIA 166 HELIX 3 A2A ASP A 54 ILE A 58 5 4XIA 167 HELIX 4 A2 ALA A 64 THR A 81 1 KINKED 4XIA 168 HELIX 5 A3 ARG A 108 MET A 128 1 KINKED 4XIA 169 HELIX 6 A4 LEU A 150 LYS A 171 1 4XIA 170 HELIX 7 A5 VAL A 195 GLN A 204 1 4XIA 171 HELIX 8 A6A THR A 217 GLU A 220 1 TURN 4XIA 172 HELIX 9 A6B HIS A 219 GLY A 224 5 4XIA 173 HELIX 10 A6 PHE A 227 TRP A 236 1 4XIA 174 HELIX 11 A7 LEU A 264 ASN A 276 1 4XIA 175 HELIX 12 A8 TYR A 301 ALA A 327 1 KINKED 4XIA 176 HELIX 13 A9 PRO A 329 SER A 338 1 4XIA 177 HELIX 14 A10 VAL A 340 GLY A 344 5 4XIA 178 HELIX 15 A11 ALA A 354 ASN A 359 5 4XIA 179 HELIX 16 A12 ALA A 369 GLU A 374 1 TURN 4XIA 180 HELIX 17 A13 PHE A 379 LEU A 391 1 4XIA 181 HELIX 18 B0 LEU B 14 VAL B 17 5 4XIA 182 HELIX 19 B1 PRO B 35 LEU B 45 1 4XIA 183 HELIX 20 B2A ASP B 54 ILE B 58 5 4XIA 184 HELIX 21 B2 ALA B 64 THR B 81 1 KINKED 4XIA 185 HELIX 22 B3 ARG B 108 MET B 128 1 KINKED 4XIA 186 HELIX 23 B4 LEU B 150 LYS B 171 1 4XIA 187 HELIX 24 B5 VAL B 195 GLN B 204 1 4XIA 188 HELIX 25 B6A THR B 217 GLU B 220 1 TURN 4XIA 189 HELIX 26 B6B HIS B 219 GLY B 224 5 4XIA 190 HELIX 27 B6 PHE B 227 TRP B 236 1 4XIA 191 HELIX 28 B7 LEU B 264 ASN B 276 1 4XIA 192 HELIX 29 B8 TYR B 301 ALA B 327 1 KINKED 4XIA 193 HELIX 30 B9 PRO B 329 SER B 338 1 4XIA 194 HELIX 31 B10 VAL B 340 GLY B 344 5 4XIA 195 HELIX 32 B11 ALA B 354 ASN B 359 5 4XIA 196 HELIX 33 B12 ALA B 369 GLU B 374 1 TURN 4XIA 197 HELIX 34 B13 PHE B 379 LEU B 391 1 4XIA 198 SHEET 1 BAA 9 HIS A 9 LEU A 14 0 4XIA 199 SHEET 2 BAA 9 TYR A 48 THR A 51 1 4XIA 200 SHEET 3 BAA 9 LYS A 84 VAL A 88 1 4XIA 201 SHEET 4 BAA 9 GLU A 131 MET A 135 1 4XIA 202 SHEET 5 BAA 9 ARG A 176 GLU A 180 1 4XIA 203 SHEET 6 BAA 9 ILE A 210 THR A 217 1 4XIA 204 SHEET 7 BAA 9 PHE A 241 LEU A 245 1 4XIA 205 SHEET 8 BAA 9 ARG A 289 ASP A 292 1 4XIA 206 SHEET 9 BAA 9 HIS A 9 LEU A 14 1 4XIA 207 SHEET 1 BAB 9 HIS B 9 LEU B 14 0 4XIA 208 SHEET 2 BAB 9 TYR B 48 THR B 51 1 4XIA 209 SHEET 3 BAB 9 LYS B 84 VAL B 88 1 4XIA 210 SHEET 4 BAB 9 GLU B 131 MET B 135 1 4XIA 211 SHEET 5 BAB 9 ARG B 176 GLU B 180 1 4XIA 212 SHEET 6 BAB 9 ILE B 210 THR B 217 1 4XIA 213 SHEET 7 BAB 9 PHE B 241 LEU B 245 1 4XIA 214 SHEET 8 BAB 9 ARG B 289 ASP B 292 1 4XIA 215 SHEET 9 BAB 9 HIS B 9 LEU B 14 1 4XIA 216 TURN 1 T1A ASP A 23 GLY A 26 4XIA 217 TURN 2 T1B ASP B 23 GLY B 26 4XIA 218 CRYST1 105.800 105.800 153.400 90.00 90.00 120.00 P 31 2 1 12 4XIA 219 ORIGX1 1.000000 0.000000 0.000000 0.00000 4XIA 220 ORIGX2 0.000000 1.000000 0.000000 0.00000 4XIA 221 ORIGX3 0.000000 0.000000 1.000000 0.00000 4XIA 222 SCALE1 0.009452 0.005457 0.000000 0.00000 4XIA 223 SCALE2 0.000000 0.010914 0.000000 0.00000 4XIA 224 SCALE3 0.000000 0.000000 0.006519 0.00000 4XIA 225 MTRIX1 1 -0.883900 -0.064800 0.463200 66.28000 1 4XIA 226 MTRIX2 1 -0.070600 -0.960500 -0.269000 115.10000 1 4XIA 227 MTRIX3 1 0.462400 -0.270500 0.844400 0.16000 1 4XIA 228