HEADER LYASE(CARBON-OXYGEN) 19-SEP-88 1WSY 1WSY 3 COMPND TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) 1WSY 4 SOURCE (SALMONELLA $TYPHIMURIUM, STRAIN /TB$2211(SLASH)$P/STH8$) 1WSY 5 AUTHOR C.HYDE,S.AHMED,E.PADLAN,E.MILES,D.DAVIES 1WSY 6 REVDAT 2 15-JAN-90 1WSYA 1 JRNL 1WSYA 1 REVDAT 1 09-JAN-89 1WSY 0 1WSY 7 JRNL AUTH C.C.HYDE,E.W.MILES 1WSYA 2 JRNL TITL THE TRYPTOPHAN SYNTHASE MULTIENZYME COMPLEX. 1WSYA 3 JRNL TITL 2 EXPLORING STRUCTURE-FUNCTION RELATIONSHIPS WITH 1WSYA 4 JRNL TITL 3 X-RAY CRYSTALLOGRAPHY AND MUTAGENESIS 1WSYA 5 JRNL REF BIO(SLASH)TECHNOLOGY V. 8 27 1990 1WSYA 6 JRNL REFN ASTM BTCHDA US ISSN 0733-222X 844 1WSYA 7 REMARK 1 1WSY 8 REMARK 1 REFERENCE 1 1WSY 9 REMARK 1 AUTH C.C.HYDE,S.A.AHMED,E.A.PADLAN,E.W.MILES,D.R.DAVIES 1WSY 10 REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE TRYPTOPHAN 1WSY 11 REMARK 1 TITL 2 SYNTHASE ALPHA=2=BETA=2= MULTIENZYME COMPLEX FROM 1WSY 12 REMARK 1 TITL 3 SALMONELLA $TYPHIMURIUM 1WSY 13 REMARK 1 REF J.BIOL.CHEM. V. 263 17857 1988 1WSY 14 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1WSY 15 REMARK 1 REFERENCE 2 1WSY 16 REMARK 1 AUTH S.A.AHMED,E.W.MILES,D.R.DAVIES 1WSY 17 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY 1WSY 18 REMARK 1 TITL 2 CRYSTALLOGRAPHIC DATA OF THE TRYPTOPHAN SYNTHASE 1WSY 19 REMARK 1 TITL 3 ALPHA=2=BETA=2= COMPLEX FROM SALMONELLA 1WSY 20 REMARK 1 TITL 4 $TYPHIMURIUM 1WSY 21 REMARK 1 REF J.BIOL.CHEM. V. 260 3716 1985 1WSY 22 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1WSY 23 REMARK 2 1WSY 24 REMARK 2 RESOLUTION. 2.5 ANGSTROMS. 1WSY 25 REMARK 3 1WSY 26 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST SQUARES PROCEDURE OF J. 1WSY 27 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*). THE R 1WSY 28 REMARK 3 VALUE IS 0.253. THE RMS DEVIATION FROM IDEALITY OF THE 1WSY 29 REMARK 3 BOND DISTANCES IS 0.008 ANGSTROMS. THE RMS DEVIATION FROM 1WSY 30 REMARK 3 IDEALITY OF THE BOND ANGLES IS 1.00 DEGREES. 1WSY 31 REMARK 4 1WSY 32 REMARK 4 THE PHYSIOLOGICALLY ACTIVE FORM OF THE ENZYME IS AN 1WSY 33 REMARK 4 ALPHA-2-BETA-2 COMPLEX. THE CRYSTALLOGRAPHIC ASYMMETRIC 1WSY 34 REMARK 4 UNIT COMPRISES ONE ALPHA CHAIN AND ONE BETA CHAIN. THESE 1WSY 35 REMARK 4 CHAINS ARE PRESENTED IN THIS ENTRY WITH CHAIN IDENTIFIERS 1WSY 36 REMARK 4 *A* AND *B*, RESPECTIVELY. THE OTHER ALPHA AND BETA CHAINS 1WSY 37 REMARK 4 CAN BE GENERATED FROM THE CHAINS IN THIS ENTRY BY THE 1WSY 38 REMARK 4 FOLLOWING TRANSFORMATION - 1WSY 39 REMARK 4 1WSY 40 REMARK 4 -1.0 0.0 0.0 184.5 1WSY 41 REMARK 4 0.0 1.0 0.0 0.0 1WSY 42 REMARK 4 0.0 0.0 -1.0 0.0 1WSY 43 REMARK 4 1WSY 44 REMARK 4 IN THE CRYSTAL THE DYAD AXIS RELATING THE TWO ALPHA 1WSY 45 REMARK 4 SUBUNITS AND THE TWO BETA SUBUNITS (THE MOLECULAR Y-AXIS) 1WSY 46 REMARK 4 IS ALONG AN EXACT CRYSTALLOGRAPHIC AXIS (THE CRYSTAL 1WSY 47 REMARK 4 B-AXIS). 1WSY 48 REMARK 5 1WSY 49 REMARK 5 ATOMIC COORDINATES FOR THE FOLLOWING RESIDUES ARE NOT 1WSY 50 REMARK 5 DETERMINED AT PRESENT AND ARE NOT INCLUDED IN THIS ENTRY - 1WSY 51 REMARK 5 ASP A 56 - LEU A 58 1WSY 52 REMARK 5 SER A 178 - LEU A 191 1WSY 53 REMARK 5 SER A 266 - ALA A 268 1WSY 54 REMARK 5 MET B 1 - TYR B 8 1WSY 55 REMARK 5 ARG B 394 - ILE B 397 1WSY 56 REMARK 5 BECAUSE OF THESE MISSING RESIDUES, THE ENDS OF HELICES A6, 1WSY 57 REMARK 5 A8, AND B13 ARE UNCERTAIN. IN ADDITION, THE END OF 1WSY 58 REMARK 5 STRAND 6 OF SHEET S1 IS UNCERTAIN. 1WSY 59 REMARK 6 1WSY 60 REMARK 6 THE SHEET PRESENTED AS * S1* ON SHEET RECORDS BELOW IS 1WSY 61 REMARK 6 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS 1WSY 62 REMARK 6 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND 1WSY 63 REMARK 6 LAST STRANDS ARE IDENTICAL. 1WSY 64 REMARK 7 1WSY 65 REMARK 7 ALL PROLINES ARE IN THE TRANS CONFIGURATION. PRO B 56 MAY 1WSY 66 REMARK 7 BE REINTERPRETED AS A CIS PROLINE IN FURTHER STUDIES. 1WSY 67 REMARK 8 1WSY 68 REMARK 8 PLP FORMS A SCHIFF'S BASE WITH NZ OF LYS B 87. 1WSY 69 REMARK 9 1WSY 70 REMARK 9 THESE COORDINATES SHOULD BE REGARDED AS PRELIMINARY. 1WSY 71 REMARK 9 FURTHER REFINEMENT IS IN PROGRESS. 1WSY 72 REMARK 10 1WSYA 8 REMARK 10 CORRECTION. INSERT NEW PUBLICATION AS JRNL REFERENCE. 1WSYA 9 REMARK 10 15-JAN-90. 1WSYA 10 SEQRES 1 A 268 MET GLU ARG TYR GLU ASN LEU PHE ALA GLN LEU ASN ASP 1WSY 73 SEQRES 2 A 268 ARG ARG GLU GLY ALA PHE VAL PRO PHE VAL THR LEU GLY 1WSY 74 SEQRES 3 A 268 ASP PRO GLY ILE GLU GLN SER LEU LYS ILE ILE ASP THR 1WSY 75 SEQRES 4 A 268 LEU ILE ASP ALA GLY ALA ASP ALA LEU GLU LEU GLY VAL 1WSY 76 SEQRES 5 A 268 PRO PHE SER ASP PRO LEU ALA ASP GLY PRO THR ILE GLN 1WSY 77 SEQRES 6 A 268 ASN ALA ASN LEU ARG ALA PHE ALA ALA GLY VAL THR PRO 1WSY 78 SEQRES 7 A 268 ALA GLN CYS PHE GLU MET LEU ALA LEU ILE ARG GLU LYS 1WSY 79 SEQRES 8 A 268 HIS PRO THR ILE PRO ILE GLY LEU LEU MET TYR ALA ASN 1WSY 80 SEQRES 9 A 268 LEU VAL PHE ASN ASN GLY ILE ASP ALA PHE TYR ALA ARG 1WSY 81 SEQRES 10 A 268 CYS GLU GLN VAL GLY VAL ASP SER VAL LEU VAL ALA ASP 1WSY 82 SEQRES 11 A 268 VAL PRO VAL GLU GLU SER ALA PRO PHE ARG GLN ALA ALA 1WSY 83 SEQRES 12 A 268 LEU ARG HIS ASN ILE ALA PRO ILE PHE ILE CYS PRO PRO 1WSY 84 SEQRES 13 A 268 ASN ALA ASP ASP ASP LEU LEU ARG GLN VAL ALA SER TYR 1WSY 85 SEQRES 14 A 268 GLY ARG GLY TYR THR TYR LEU LEU SER ARG SER GLY VAL 1WSY 86 SEQRES 15 A 268 THR GLY ALA GLU ASN ARG GLY ALA LEU PRO LEU HIS HIS 1WSY 87 SEQRES 16 A 268 LEU ILE GLU LYS LEU LYS GLU TYR HIS ALA ALA PRO ALA 1WSY 88 SEQRES 17 A 268 LEU GLN GLY PHE GLY ILE SER SER PRO GLU GLN VAL SER 1WSY 89 SEQRES 18 A 268 ALA ALA VAL ARG ALA GLY ALA ALA GLY ALA ILE SER GLY 1WSY 90 SEQRES 19 A 268 SER ALA ILE VAL LYS ILE ILE GLU LYS ASN LEU ALA SER 1WSY 91 SEQRES 20 A 268 PRO LYS GLN MET LEU ALA GLU LEU ARG SER PHE VAL SER 1WSY 92 SEQRES 21 A 268 ALA MET LYS ALA ALA SER ARG ALA 1WSY 93 SEQRES 1 B 397 MET THR THR LEU LEU ASN PRO TYR PHE GLY GLU PHE GLY 1WSY 94 SEQRES 2 B 397 GLY MET TYR VAL PRO GLN ILE LEU MET PRO ALA LEU ASN 1WSY 95 SEQRES 3 B 397 GLN LEU GLU GLU ALA PHE VAL ARG ALA GLN LYS ASP PRO 1WSY 96 SEQRES 4 B 397 GLU PHE GLN ALA GLN PHE ALA ASP LEU LEU LYS ASN TYR 1WSY 97 SEQRES 5 B 397 ALA GLY ARG PRO THR ALA LEU THR LYS CYS GLN ASN ILE 1WSY 98 SEQRES 6 B 397 THR ALA GLY THR ARG THR THR LEU TYR LEU LYS ARG GLU 1WSY 99 SEQRES 7 B 397 ASP LEU LEU HIS GLY GLY ALA HIS LYS THR ASN GLN VAL 1WSY 100 SEQRES 8 B 397 LEU GLY GLN ALA LEU LEU ALA LYS ARG MET GLY LYS SER 1WSY 101 SEQRES 9 B 397 GLU ILE ILE ALA GLU THR GLY ALA GLY GLN HIS GLY VAL 1WSY 102 SEQRES 10 B 397 ALA SER ALA LEU ALA SER ALA LEU LEU GLY LEU LYS CYS 1WSY 103 SEQRES 11 B 397 ARG ILE TYR MET GLY ALA LYS ASP VAL GLU ARG GLN SER 1WSY 104 SEQRES 12 B 397 PRO ASN VAL PHE ARG MET ARG LEU MET GLY ALA GLU VAL 1WSY 105 SEQRES 13 B 397 ILE PRO VAL HIS SER GLY SER ALA THR LEU LYS ASP ALA 1WSY 106 SEQRES 14 B 397 CYS ASN GLU ALA LEU ARG ASP TRP SER GLY SER TYR GLU 1WSY 107 SEQRES 15 B 397 THR ALA HIS TYR MET LEU GLY THR ALA ALA GLY PRO HIS 1WSY 108 SEQRES 16 B 397 PRO TYR PRO THR ILE VAL ARG GLU PHE GLN ARG MET ILE 1WSY 109 SEQRES 17 B 397 GLY GLU GLU THR LYS ALA GLN ILE LEU ASP LYS GLU GLY 1WSY 110 SEQRES 18 B 397 ARG LEU PRO ASP ALA VAL ILE ALA CYS VAL GLY GLY GLY 1WSY 111 SEQRES 19 B 397 SER ASN ALA ILE GLY MET PHE ALA ASP PHE ILE ASN ASP 1WSY 112 SEQRES 20 B 397 THR SER VAL GLY LEU ILE GLY VAL GLU PRO GLY GLY HIS 1WSY 113 SEQRES 21 B 397 GLY ILE GLU THR GLY GLU HIS GLY ALA PRO LEU LYS HIS 1WSY 114 SEQRES 22 B 397 GLY ARG VAL GLY ILE TYR PHE GLY MET LYS ALA PRO MET 1WSY 115 SEQRES 23 B 397 MET GLN THR ALA ASP GLY GLN ILE GLU GLU SER TYR SER 1WSY 116 SEQRES 24 B 397 ILE SER ALA GLY LEU ASP PHE PRO SER VAL GLY PRO GLN 1WSY 117 SEQRES 25 B 397 HIS ALA TYR LEU ASN SER ILE GLY ARG ALA ASP TYR VAL 1WSY 118 SEQRES 26 B 397 SER ILE THR ASP ASP GLU ALA LEU GLU ALA PHE LYS THR 1WSY 119 SEQRES 27 B 397 LEU CYS ARG HIS GLU GLY ILE ILE PRO ALA LEU GLU SER 1WSY 120 SEQRES 28 B 397 SER HIS ALA LEU ALA HIS ALA LEU LYS MET MET ARG GLU 1WSY 121 SEQRES 29 B 397 GLN PRO GLU LYS GLU GLN LEU LEU VAL VAL ASN LEU SER 1WSY 122 SEQRES 30 B 397 GLY ARG GLY ASP LYS ASP ILE PHE THR VAL HIS ASP ILE 1WSY 123 SEQRES 30 B 397 LEU LYS ALA ARG GLY LEU ILE 1WSY 124 FTNOTE 1 1WSY 125 FTNOTE 1 SEE REMARK 7. 1WSY 126 HET PLP 1 15 PYRIDOXAL 5(PRIME)-PHOSPHATE 1WSY 127 FORMUL 3 PLP C8 H10 N1 O6 P1 1WSY 128 HELIX 1 A0 MET A 1 ASN A 12 1 1WSY 129 HELIX 2 A1 SER A 33 ASP A 42 1 1WSY 130 HELIX 3 A2P THR A 63 ALA A 73 1 1WSY 131 HELIX 4 A2 ALA A 79 ARG A 89 1 1WSY 132 HELIX 5 A3 ILE A 111 GLN A 120 1 1WSY 133 HELIX 6 A4 PRO A 138 ARG A 145 1 1WSY 134 HELIX 7 A5 ASP A 160 SER A 168 1 1WSY 135 HELIX 8 A6 PRO A 192 GLU A 202 1 RESIDUES 178-191 NOT LOCATED 1WSY 136 HELIX 9 A7 PRO A 217 ARG A 225 1 1WSY 137 HELIX 10 A8P SER A 235 GLU A 242 1 1WSY 138 HELIX 11 A8 PRO A 248 ALA A 265 1 RESIDUES 267-268 NOT LOCATED 1WSY 139 HELIX 12 B1 ALA B 24 LYS B 37 1 1WSY 140 HELIX 13 B2 GLU B 40 ASN B 51 1 1WSY 141 HELIX 14 B3 LYS B 87 LEU B 97 1 1WSY 142 HELIX 15 B4 HIS B 115 ALA B 124 1 1WSY 143 HELIX 16 B5 ASN B 145 ARG B 150 1 1WSY 144 HELIX 17 B6 LEU B 166 TRP B 177 1 1WSY 145 HELIX 18 B7 PRO B 198 GLU B 203 1 1WSY 146 HELIX 19 B8 ARG B 206 GLU B 220 1 1WSY 147 HELIX 20 B9 SER B 235 PHE B 244 1 1WSY 148 HELIX 21 B10 PRO B 311 ILE B 319 1 1WSY 149 HELIX 22 B11 ASP B 329 ARG B 341 1 1WSY 150 HELIX 23 B12 LEU B 349 GLU B 364 1 1WSY 151 HELIX 24 B13 ASP B 383 ALA B 393 1 RESIDUES 394-397 NOT LOCATED 1WSY 152 SHEET 1 S1 9 ARG A 15 THR A 24 0 1WSY 153 SHEET 2 S1 9 ALA A 47 VAL A 52 1 1WSY 154 SHEET 3 S1 9 ILE A 95 TYR A 102 1 1WSY 155 SHEET 4 S1 9 ASP A 124 VAL A 128 1 1WSY 156 SHEET 5 S1 9 ILE A 148 CYS A 154 1 1WSY 157 SHEET 6 S1 9 TYR A 173 LEU A 177 1 1WSY 158 SHEET 7 S1 9 ALA A 208 PHE A 212 1 1WSY 159 SHEET 8 S1 9 ALA A 229 ILE A 232 1 1WSY 160 SHEET 9 S1 9 ARG A 15 THR A 24 1 1WSY 161 SHEET 1 S2 4 ALA B 154 VAL B 159 0 1WSY 162 SHEET 2 S2 4 LEU B 128 MET B 134 1 1WSY 163 SHEET 3 S2 4 SER B 104 THR B 110 1 1WSY 164 SHEET 4 S2 4 ALA B 184 LEU B 188 1 1WSY 165 SHEET 1 S3 6 ALA B 58 CYS B 62 0 1WSY 166 SHEET 2 S3 6 THR B 71 ARG B 77 -1 1WSY 167 SHEET 3 S3 6 GLU B 369 ASN B 375 1 1WSY 168 SHEET 4 S3 6 ASP B 225 VAL B 231 1 1WSY 169 SHEET 5 S3 6 VAL B 250 GLU B 256 1 1WSY 170 SHEET 6 S3 6 ALA B 322 ILE B 327 1 1WSY 171 CRYST1 184.500 61.100 67.700 90.00 94.67 90.00 C 2 4 1WSY 172 ORIGX1 1.000000 0.000000 0.000000 0.00000 1WSY 173 ORIGX2 0.000000 1.000000 0.000000 0.00000 1WSY 174 ORIGX3 0.000000 0.000000 1.000000 0.00000 1WSY 175 SCALE1 0.005420 0.000000 0.000443 0.00000 1WSY 176 SCALE2 0.000000 0.016367 0.000000 0.00000 1WSY 177 SCALE3 0.000000 0.000000 0.014820 0.00000 1WSY 178 ATOM 1 N MET A 1 39.833 22.986 30.477 1.00 27.84 1WSY 179 ATOM 2 CA MET A 1 38.949 22.042 29.784 1.00 28.44 1WSY 180 A