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HEADER DEHALOGENASE 08-SEP-93 2DHD 2DHD 2
COMPND HALOALKANE DEHALOGENASE (E.C.3.8.1.5) COMPLEXED WITH 2DHD 3
COMPND 2 1,2-DICHLOROETHANE (SOAKED IN 10MM DCE AT PH 5.0 AND 2DHD 4
COMPND 3 AT ROOM TEMPERATURE) 2DHD 5
SOURCE (XANTHOBACTER AUTOTROPHICUS, GJ10) 2DHD 6
AUTHOR K.H.G.VERSCHUEREN,B.W.DIJKSTRA 2DHD 7
REVDAT 1 31-JUL-94 2DHD 0 2DHD 8
JRNL AUTH K.H.G.VERSCHUEREN,F.SELJEE,H.J.ROZEBOOM,K.H.KALK, 2DHD 9
JRNL AUTH 2 B.W.DIJKSTRA 2DHD 10
JRNL TITL CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC 2DHD 11
JRNL TITL 2 MECHANISM OF HALOALKANE DEHALOGENASE 2DHD 12
JRNL REF NATURE V. 363 693 1993 2DHD 13
JRNL REFN ASTM NATUAS UK ISSN 0028-0836 0006 2DHD 14
REMARK 1 2DHD 15
REMARK 1 REFERENCE 1 2DHD 16
REMARK 1 AUTH S.M.FRANKEN,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA 2DHD 17
REMARK 1 TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN 2DHD 18
REMARK 1 TITL 2 ENZYME TO DETOXIFY HALOGENATED ALKANES 2DHD 19
REMARK 1 REF /EMBO$ J. V. 10 1297 1991 2DHD 20
REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 0897 2DHD 21
REMARK 1 REFERENCE 2 2DHD 22
REMARK 1 AUTH H.J.ROZEBOOM,J.KINGMA,D.B.JANSSEN,B.W.DIJKSTRA 2DHD 23
REMARK 1 TITL CRYSTALLIZATION OF HALOALKANE DEHALOGENASE FROM 2DHD 24
REMARK 1 TITL 2 XANTHOBACTER AUTOTROPHICUS GJ10 2DHD 25
REMARK 1 REF J.MOL.BIOL. V. 200 611 1988 2DHD 26
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 2DHD 27
REMARK 2 2DHD 28
REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 2DHD 29
REMARK 3 2DHD 30
REMARK 3 REFINEMENT. 2DHD 31
REMARK 3 PROGRAM TNT 2DHD 32
REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 2DHD 33
REMARK 3 R VALUE 0.189 2DHD 34
REMARK 3 RMSD BOND DISTANCES 0.010 ANGSTROMS 2DHD 35
REMARK 3 RMSD BOND ANGLES 3.0 DEGREES 2DHD 36
REMARK 3 2DHD 37
REMARK 3 NUMBER OF REFLECTIONS 14812 2DHD 38
REMARK 3 RESOLUTION RANGE 15. - 2.13 ANGSTROMS 2DHD 39
REMARK 3 DATA CUTOFF 3.0 SIGMA(F) 2DHD 40
REMARK 3 PERCENT COMPLETION 82. 2DHD 41
REMARK 3 2DHD 42
REMARK 3 NUMBER OF PROTEIN ATOMS 2479 2DHD 43
REMARK 3 NUMBER OF SOLVENT ATOMS 151 2DHD 44
REMARK 4 2DHD 45
REMARK 4 THE CRYSTAL WAS SOAKED IN 10 MM 1,2-DICHLOROETHANE (DCE) 2DHD 46
REMARK 4 AT PH 5.0 AND AT ROOM TEMPERATURE. THE SUBSTRATE IS 2DHD 47
REMARK 4 COVALENTLY BOUND IN THE ACTIVE SITE TO THE NUCLEOPHILIC 2DHD 48
REMARK 4 RESIDUE. 2DHD 49
REMARK 5 2DHD 50
REMARK 5 CROSS REFERENCE TO SEQUENCE DATA BASE: 2DHD 51
REMARK 5 PIR-ENTRY S15339 2DHD 52
REMARK 6 2DHD 53
REMARK 6 SEQUENCE ADVISORY NOTICE: 2DHD 54
REMARK 6 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 2DHD 55
REMARK 6 2DHD 56
REMARK 6 SWISS-PROT ENTRY NAME: HALO_XANAU 2DHD 57
REMARK 6 2DHD 58
REMARK 6 SWISS-PROT RESIDUE PDB SEQRES 2DHD 59
REMARK 6 2DHD 60
REMARK 6 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 2DHD 61
REMARK 6 ILE 120 LEU 120 2DHD 62
REMARK 6 2DHD 63
REMARK 6 THE SWISS-PROT ENTRY IS IN ERROR AND THE DEPOSITORS HAVE 2DHD 64
REMARK 6 REQUESTED THAT THE SEQUENCE DATA BANKS MAKE THE PROPER 2DHD 65
REMARK 6 CORRECTIONS. 2DHD 66
REMARK 7 2DHD 67
REMARK 7 THE HELIX AND SHEET STRUCTURES ARE SIMILAR TO THOSE IN 2DHD 68
REMARK 7 PROTEIN DATA BANK ENTRY 2HAD. 2DHD 69
SEQRES 1 310 MET ILE ASN ALA ILE ARG THR PRO ASP GLN ARG PHE SER 2DHD 70
SEQRES 2 310 ASN LEU ASP GLN TYR PRO PHE SER PRO ASN TYR LEU ASP 2DHD 71
SEQRES 3 310 ASP LEU PRO GLY TYR PRO GLY LEU ARG ALA HIS TYR LEU 2DHD 72
SEQRES 4 310 ASP GLU GLY ASN SER ASP ALA GLU ASP VAL PHE LEU CYS 2DHD 73
SEQRES 5 310 LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG LYS 2DHD 74
SEQRES 6 310 MET ILE PRO VAL PHE ALA GLU SER GLY ALA ARG VAL ILE 2DHD 75
SEQRES 7 310 ALA PRO ASP PHE PHE GLY PHE GLY LYS SER ASP LYS PRO 2DHD 76
SEQRES 8 310 VAL ASP GLU GLU ASP TYR THR PHE GLU PHE HIS ARG ASN 2DHD 77
SEQRES 9 310 PHE LEU LEU ALA LEU ILE GLU ARG LEU ASP LEU ARG ASN 2DHD 78
SEQRES 10 310 ILE THR LEU VAL VAL GLN ASP TRP GLY GLY PHE LEU GLY 2DHD 79
SEQRES 11 310 LEU THR LEU PRO MET ALA ASP PRO SER ARG PHE LYS ARG 2DHD 80
SEQRES 12 310 LEU ILE ILE MET ASN ALA CYS LEU MET THR ASP PRO VAL 2DHD 81
SEQRES 13 310 THR GLN PRO ALA PHE SER ALA PHE VAL THR GLN PRO ALA 2DHD 82
SEQRES 14 310 ASP GLY PHE THR ALA TRP LYS TYR ASP LEU VAL THR PRO 2DHD 83
SEQRES 15 310 SER ASP LEU ARG LEU ASP GLN PHE MET LYS ARG TRP ALA 2DHD 84
SEQRES 16 310 PRO THR LEU THR GLU ALA GLU ALA SER ALA TYR ALA ALA 2DHD 85
SEQRES 17 310 PRO PHE PRO ASP THR SER TYR GLN ALA GLY VAL ARG LYS 2DHD 86
SEQRES 18 310 PHE PRO LYS MET VAL ALA GLN ARG ASP GLN ALA CYS ILE 2DHD 87
SEQRES 19 310 ASP ILE SER THR GLU ALA ILE SER PHE TRP GLN ASN ASP 2DHD 88
SEQRES 20 310 TRP ASN GLY GLN THR PHE MET ALA ILE GLY MET LYS ASP 2DHD 89
SEQRES 21 310 LYS LEU LEU GLY PRO ASP VAL MET TYR PRO MET LYS ALA 2DHD 90
SEQRES 22 310 LEU ILE ASN GLY CYS PRO GLU PRO LEU GLU ILE ALA ASP 2DHD 91
SEQRES 23 310 ALA GLY HIS PHE VAL GLN GLU PHE GLY GLU GLN VAL ALA 2DHD 92
SEQRES 24 310 ARG GLU ALA LEU LYS HIS PHE ALA GLU THR GLU 2DHD 93
FTNOTE 1 2DHD 94
FTNOTE 1 CIS PROLINE - PRO 57 2DHD 95
FTNOTE 2 2DHD 96
FTNOTE 2 CIS PROLINE - PRO 168 2DHD 97
HET MCE 124 3 CHLOROETHANE BOUND TO ASP 124 2DHD 98
HET CL 552 1 CHLORIDE ION 2DHD 99
FORMUL 2 MCE C2 H4 CL1 2DHD 100
FORMUL 3 CL CL1 - 2DHD 101
FORMUL 4 HOH *151(H2 O1) 2DHD 102
HELIX 1 A1 SER 60 GLU 72 1 2DHD 103
HELIX 2 A2 PHE 99 ARG 112 1 2DHD 104
HELIX 3 A3 ASP 124 GLY 130 1 2DHD 105
HELIX 4 A4 PRO 159 PHE 164 1 2DHD 106
HELIX 5 A5 PHE 172 VAL 180 1 2DHD 107
HELIX 6 A6 LEU 187 TRP 194 1 2DHD 108
HELIX 7 A7 GLU 200 ALA 207 1 2DHD 109
HELIX 8 A8 THR 213 ALA 227 1 2DHD 110
HELIX 9 A9 GLN 231 ASN 246 1 2DHD 111
HELIX 10 A10 PRO 265 LEU 274 1 2DHD 112
HELIX 11 A11 VAL 291 HIS 305 1 2DHD 113
SHEET 1 S1 8 SER 21 LEU 25 0 2DHD 114
SHEET 2 S1 8 ALA 36 GLU 41 -1 2DHD 115
SHEET 3 S1 8 ARG 76 PRO 80 -1 2DHD 116
SHEET 4 S1 8 VAL 49 HIS 54 1 2DHD 117
SHEET 5 S1 8 ILE 118 VAL 122 1 2DHD 118
SHEET 6 S1 8 PHE 141 MET 147 1 2DHD 119
SHEET 7 S1 8 GLN 251 GLY 257 1 2DHD 120
SHEET 8 S1 8 GLU 280 ILE 284 1 2DHD 121
TURN 1 T1 ASP 9 PHE 12 NEAR 3/10 TURN 2DHD 122
TURN 2 T2 LEU 28 TYR 31 REVERSE TURN II 2DHD 123
TURN 3 T3 ASN 43 ALA 46 NEAR REVERSE TURN I 2DHD 124
TURN 4 T4 GLY 55 THR 58 NEAR CIS-PROLINE TURN (VI/B) 2DHD 125
TURN 5 T5 PHE 82 PHE 85 NEAR REVERSE TURN II 2DHD 126
TURN 6 T6 PHE 85 SER 88 NEAR REVERSE TURN II' 2DHD 127
TURN 7 T7 ASP 93 ASP 96 3/10 TURN 2DHD 128
TURN 8 T8 GLN 123 TRP 125 "NUCLEOPHILE ELBOW" 2DHD 129
TURN 9 T9 PRO 138 PHE 141 NEAR 310 TURN 2DHD 130
TURN 10 T10 ASP 154 THR 157 OPEN TURN III 2DHD 131
TURN 11 T11 THR 166 ALA 169 OPEN CIS-PROLINE TURN (VI/B) 2DHD 132
TURN 12 T12 THR 213 GLN 216 REVERSE TURN I 2DHD 133
TURN 13 T13 ILE 275 CYS 278 REVERSE TURN II 2DHD 134
TURN 14 T14 ILE 284 ALA 287 NEAR REVERSE TURN I 2DHD 135
CRYST1 94.800 72.800 41.400 90.00 90.00 90.00 P 21 21 2 4 2DHD 136
ORIGX1 1.000000 0.000000 0.000000 0.00000 2DHD 137
ORIGX2 0.000000 1.000000 0.000000 0.00000 2DHD 138
ORIGX3 0.000000 0.000000 1.000000 0.00000 2DHD 139
SCALE1 0.010549 0.000000 0.000000 0.00000 2DHD 140
SCALE2 0.000000 0.013736 0.000000 0.00000 2DHD 141
SCALE3 0.000000 0.000000 0.024155 0.00000 2DHD 142 |