HEADER TRANSFERASE(AMINOTRANSFERASE) 02-AUG-93 1ARS 1ARS 2 COMPND ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEXED WITH 1ARS 3 COMPND 2 PYRIDOXAL-5'-PHOSPHATE 1ARS 4 SOURCE (ESCHERICHIA COLI) 1ARS 5 AUTHOR A.OKAMOTO,T.HIGUCHI,K.HIROTSU 1ARS 6 REVDAT 1 31-AUG-94 1ARS 0 1ARS 7 JRNL AUTH A.OKAMOTO,T.HIGUCHI,K.HIROTSU,S.KURAMITSU, 1ARS 8 JRNL AUTH 2 H.KAGAMIYAMA 1ARS 9 JRNL TITL X-RAY CRYSTALLOGRAPHIC STUDY OF PYRIDOXAL 1ARS 10 JRNL TITL 2 5'-PHOSPHATE-TYPE ASPARTATE AMINOTRANSFERASES FROM 1ARS 11 JRNL TITL 3 ESCHERICHIA COLI IN OPEN AND CLOSED FORM 1ARS 12 JRNL REF TO BE PUBLISHED 1ARS 13 JRNL REFN 0353 1ARS 14 REMARK 1 1ARS 15 REMARK 1 REFERENCE 1 1ARS 16 REMARK 1 AUTH A.OKAMOTO,K.HIROTSU,T.HIGUCHI,S.KURAMITSU, 1ARS 17 REMARK 1 AUTH 2 H.KAGAMIYAMA 1ARS 18 REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF ASPARTATE 1ARS 19 REMARK 1 TITL 2 AMINOTRANSFERASE FROM ESCHERICHIA COLI 1ARS 20 REMARK 1 EDIT T.FUKUI,H.KAGAMIYAMA,K.SODA,H.WADA 1ARS 21 REMARK 1 REF ENZYMES DEPENDENT ON 107 1991 1ARS 22 REMARK 1 REF 2 PYRIDOXAL PHOSPHATE AND 1ARS 23 REMARK 1 REF 3 OTHER CARBONYL COMPOUNDS 1ARS 24 REMARK 1 REF 4 AS COFACTORS: PROCEEDINGS OF 1ARS 25 REMARK 1 REF 5 THE 8TH INTERNATIONAL 1ARS 26 REMARK 1 REF 6 SYMPOSIUM ON VITAMIN B6 AND 1ARS 27 REMARK 1 REF 7 CARBONYL CATALYSIS 1ARS 28 REMARK 1 PUBL PERGAMON PRESS,OXFORD AND NEW YORK 1ARS 29 REMARK 1 REFN ISBN 0-08-040820-6 2030 1ARS 30 REMARK 2 1ARS 31 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. 1ARS 32 REMARK 3 1ARS 33 REMARK 3 REFINEMENT. 1ARS 34 REMARK 3 PROGRAM X-PLOR 1ARS 35 REMARK 3 AUTHORS BRUNGER 1ARS 36 REMARK 3 R VALUE 0.213 1ARS 37 REMARK 3 RMSD BOND DISTANCES 0.016 ANGSTROMS 1ARS 38 REMARK 3 1ARS 39 REMARK 3 NUMBER OF REFLECTIONS 29267 1ARS 40 REMARK 3 DATA CUTOFF 4.0 SIGMA(F) 1ARS 41 REMARK 3 1ARS 42 REMARK 3 NUMBER OF PROTEIN ATOMS 3069 1ARS 43 REMARK 3 NUMBER OF SOLVENT ATOMS 127 1ARS 44 REMARK 4 1ARS 45 REMARK 4 DIFFRACTION INTENSITY DATA FOR THE REFINEMENT WERE 1ARS 46 REMARK 4 COLLECTED ON A SCREENLESS WEISSENBERG TYPE CAMERA USING 1ARS 47 REMARK 4 SYNCHROTRON RADIATION AT THE PHOTON FACTORY, KEK, JAPAN. 1ARS 48 REMARK 4 THE FUNCTIONAL DIMER CAN BE GENERATED BY APPLYING THE 1ARS 49 REMARK 4 SYMMETRY OPERATOR (X, -Y, -Z) TO THE ATOMIC COORDINATES 1ARS 50 REMARK 4 PRESENTED IN THIS ENTRY. 1ARS 51 SEQRES 1 396 MET PHE GLU ASN ILE THR ALA ALA PRO ALA ASP PRO ILE 1ARS 52 SEQRES 2 396 LEU GLY LEU ALA ASP LEU PHE ARG ALA ASP GLU ARG PRO 1ARS 53 SEQRES 3 396 GLY LYS ILE ASN LEU GLY ILE GLY VAL TYR LYS ASP GLU 1ARS 54 SEQRES 4 396 THR GLY LYS THR PRO VAL LEU THR SER VAL LYS LYS ALA 1ARS 55 SEQRES 5 396 GLU GLN TYR LEU LEU GLU ASN GLU THR THR LYS ASN TYR 1ARS 56 SEQRES 6 396 LEU GLY ILE ASP GLY ILE PRO GLU PHE GLY ARG CYS THR 1ARS 57 SEQRES 7 396 GLN GLU LEU LEU PHE GLY LYS GLY SER ALA LEU ILE ASN 1ARS 58 SEQRES 8 396 ASP LYS ARG ALA ARG THR ALA GLN THR PRO GLY GLY THR 1ARS 59 SEQRES 9 396 GLY ALA LEU ARG VAL ALA ALA ASP PHE LEU ALA LYS ASN 1ARS 60 SEQRES 10 396 THR SER VAL LYS ARG VAL TRP VAL SER ASN PRO SER TRP 1ARS 61 SEQRES 11 396 PRO ASN HIS LYS SER VAL PHE ASN SER ALA GLY LEU GLU 1ARS 62 SEQRES 12 396 VAL ARG GLU TYR ALA TYR TYR ASP ALA GLU ASN HIS THR 1ARS 63 SEQRES 13 396 LEU ASP PHE ASP ALA LEU ILE ASN SER LEU ASN GLU ALA 1ARS 64 SEQRES 14 396 GLN ALA GLY ASP VAL VAL LEU PHE HIS GLY CYS CYS HIS 1ARS 65 SEQRES 15 396 ASN PRO THR GLY ILE ASP PRO THR LEU GLU GLN TRP GLN 1ARS 66 SEQRES 16 396 THR LEU ALA GLN LEU SER VAL GLU LYS GLY TRP LEU PRO 1ARS 67 SEQRES 17 396 LEU PHE ASP PHE ALA TYR GLN GLY PHE ALA ARG GLY LEU 1ARS 68 SEQRES 18 396 GLU GLU ASP ALA GLU GLY LEU ARG ALA PHE ALA ALA MET 1ARS 69 SEQRES 19 396 HIS LYS GLU LEU ILE VAL ALA SER SER TYR SER LYS ASN 1ARS 70 SEQRES 20 396 PHE GLY LEU TYR ASN GLU ARG VAL GLY ALA CYS THR LEU 1ARS 71 SEQRES 21 396 VAL ALA ALA ASP SER GLU THR VAL ASP ARG ALA PHE SER 1ARS 72 SEQRES 22 396 GLN MET LYS ALA ALA ILE ARG ALA ASN TYR SER ASN PRO 1ARS 73 SEQRES 23 396 PRO ALA HIS GLY ALA SER VAL VAL ALA THR ILE LEU SER 1ARS 74 SEQRES 24 396 ASN ASP ALA LEU ARG ALA ILE TRP GLU GLN GLU LEU THR 1ARS 75 SEQRES 25 396 ASP MET ARG GLN ARG ILE GLN ARG MET ARG GLN LEU PHE 1ARS 76 SEQRES 26 396 VAL ASN THR LEU GLN GLU LYS GLY ALA ASN ARG ASP PHE 1ARS 77 SEQRES 27 396 SER PHE ILE ILE LYS GLN ASN GLY MET PHE SER PHE SER 1ARS 78 SEQRES 28 396 GLY LEU THR LYS GLU GLN VAL LEU ARG LEU ARG GLU GLU 1ARS 79 SEQRES 29 396 PHE GLY VAL TYR ALA VAL ALA SER GLY ARG VAL ASN VAL 1ARS 80 SEQRES 30 396 ALA GLY MET THR PRO ASP ASN MET ALA PRO LEU CYS GLU 1ARS 81 SEQRES 31 396 ALA ILE VAL ALA VAL LEU 1ARS 82 FTNOTE 1 1ARS 83 FTNOTE 1 CIS PROLINE - PRO 138 1ARS 84 FTNOTE 2 1ARS 85 FTNOTE 2 CIS PROLINE - PRO 195 1ARS 86 FTNOTE 3 1ARS 87 FTNOTE 3 RESIDUE PLP 413 IS A PYRIDOXAL-5'-PHOSPHATE, AND AS A 1ARS 88 FTNOTE 3 COFACTOR, MAKES A SCHIFF BASE WITH LYS 258. 1ARS 89 HET PLP 413 15 PYRIDOXAL-5'-PHOSPHATE 1ARS 90 FORMUL 2 PLP C8 H10 N1 O6 P1 1ARS 91 FORMUL 3 HOH *127(H2 O1) 1ARS 92 HELIX 1 HA LEU 18 PHE 24 1 1ARS 93 HELIX 2 HB THR 51 ASN 63 1 1ARS 94 HELIX 3 HC PRO 77 PHE 88 1 1ARS 95 HELIX 4 HD ALA 93 ASN 96 1 1ARS 96 HELIX 5 HE GLY 108 ASN 122 1 1ARS 97 HELIX 6 HF HIS 143 ALA 150 1 1ARS 98 HELIX 7 HG PHE 170 LEU 177 1 1ARS 99 HELIX 8 HH LEU 202 LYS 215 1 1ARS 100 HELIX 9 HI LEU 233 MET 246 1 1ARS 101 HELIX 10 HJ SER 257 ASN 259 1 1ARS 102 HELIX 11 HK SER 277 ARG 292 1 1ARS 103 HELIX 12 HL ALA 300 SER 311 1 1ARS 104 HELIX 13 HM ASP 313 LYS 344 1 1ARS 105 HELIX 14 HN SER 351 LYS 355 5 1ARS 106 HELIX 15 HO LYS 367 GLU 376 1 1ARS 107 HELIX 16 HP MET 397 LEU 409 1 1ARS 108 SHEET 1 S1 2 ILE 33 LEU 35 0 1ARS 109 SHEET 2 S1 2 GLY 378 TYR 380 1 1ARS 110 SHEET 1 S2 7 ARG 99 THR 105 0 1ARS 111 SHEET 2 S2 7 VAL 267 ALA 274 -1 1ARS 112 SHEET 3 S2 7 LEU 250 SER 255 -1 1ARS 113 SHEET 4 S2 7 LEU 218 PHE 223 1 1ARS 114 SHEET 5 S2 7 ASP 184 GLY 190 1 1ARS 115 SHEET 6 S2 7 ARG 129 ASN 137 1 1ARS 116 SHEET 7 S2 7 GLU 154 TYR 158 1 1ARS 117 SHEET 1 S3 2 MET 359 SER 363 0 1ARS 118 SHEET 2 S3 2 ARG 386 VAL 389 -1 1ARS 119 TURN 1 T1 PHE 6 ILE 9 TYPE I 1ARS 120 TURN 2 T2 ARG 29 LYS 32 TYPE I 1ARS 121 TURN 3 T3 ASP 42 GLY 45 TYPE I 1ARS 122 TURN 4 T4 GLY 72 GLY 75 TYPE I 1ARS 123 TURN 5 T5 GLY 89 SER 92 TYPE I 1ARS 124 TURN 6 T6 ILE 95 LYS 98 TYPE I 1ARS 125 TURN 7 T7 TRP 140 HIS 143 TYPE I 1ARS 126 TURN 8 T8 ASN 148 GLY 151 TYPE I 1ARS 127 TURN 9 T9 GLN 181 ASP 184 TYPE II 1ARS 128 TURN 10 T10 VAL 213 GLY 216 TYPE I 1ARS 129 TURN 11 T11 TYR 225 PHE 228 TYPE II 1ARS 130 TURN 12 T12 GLU 235 GLU 238 TYPE I 1ARS 131 TURN 13 T13 ILE 309 ASN 312 TYPE I 1ARS 132 TURN 14 T14 ASN 312 LEU 315 TYPE III 1ARS 133 TURN 15 T15 ILE 353 GLN 356 TYPE I 1ARS 134 TURN 16 T16 VAL 382 GLY 385 TYPE I 1ARS 135 TURN 17 T17 THR 393 ASN 396 TYPE III 1ARS 136 CRYST1 155.420 87.130 79.400 90.00 90.00 90.00 C 2 2 21 8 1ARS 137 ORIGX1 1.000000 0.000000 0.000000 0.00000 1ARS 138 ORIGX2 0.000000 1.000000 0.000000 0.00000 1ARS 139 ORIGX3 0.000000 0.000000 1.000000 0.00000 1ARS 140 SCALE1 0.006434 0.000000 0.000000 0.00000 1ARS 141 SCALE2 0.000000 0.011477 0.000000 0.00000 1ARS 142 SCALE3 0.000000 0.000000 0.012594 0.00000 1ARS 143