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HEADER DEHALOGENASE 24-JUN-93 2DHE 2DHE 2
COMPND HALOALKANE DEHALOGENASE (E.C.3.8.1.5) 2DHE 3
COMPND 2 (PH 6, ROOM TEMPERATURE) 2DHE 4
SOURCE (XANTHOBACTER AUTOTROPHICUS, GJ10) 2DHE 5
AUTHOR K.H.G.VERSCHUEREN,B.W.DIJKSTRA 2DHE 6
REVDAT 1 31-AUG-94 2DHE 0 2DHE 7
JRNL AUTH K.H.G.VERSCHUEREN,F.SELJEE,H.J.ROZEBOOM,K.H.KALK, 2DHE 8
JRNL AUTH 2 B.W.DIJKSTRA 2DHE 9
JRNL TITL CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC 2DHE 10
JRNL TITL 2 MECHANISM OF HALOALKANE DEHALOGENASE 2DHE 11
JRNL REF NATURE V. 363 693 1993 2DHE 12
JRNL REFN ASTM NATUAS UK ISSN 0028-0836 0006 2DHE 13
REMARK 1 2DHE 14
REMARK 1 REFERENCE 1 2DHE 15
REMARK 1 AUTH S.M.FRANKEN,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA 2DHE 16
REMARK 1 TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN 2DHE 17
REMARK 1 TITL 2 ENZYME TO DETOXIFY HALOGENATED ALKANES 2DHE 18
REMARK 1 REF EMBO J. V. 10 1297 1991 2DHE 19
REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 0897 2DHE 20
REMARK 1 REFERENCE 2 2DHE 21
REMARK 1 AUTH H.J.ROZEBOOM,J.KINGMA,D.B.JANSSEN,B.W.DIJKSTRA 2DHE 22
REMARK 1 TITL CRYSTALLIZATION OF HALOALKANE DEHALOGENASE FROM 2DHE 23
REMARK 1 TITL 2 XANTHOBACTER AUTOTROPHICUS GJ10 2DHE 24
REMARK 1 REF J.MOL.BIOL. V. 200 611 1988 2DHE 25
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 2DHE 26
REMARK 2 2DHE 27
REMARK 2 RESOLUTION. 2.1 ANGSTROMS. 2DHE 28
REMARK 3 2DHE 29
REMARK 3 REFINEMENT. 2DHE 30
REMARK 3 PROGRAM TNT 2DHE 31
REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 2DHE 32
REMARK 3 R VALUE 0.171 2DHE 33
REMARK 3 RMSD BOND DISTANCES 0.009 ANGSTROMS 2DHE 34
REMARK 3 RMSD BOND ANGLES 2.90 DEGREES 2DHE 35
REMARK 3 2DHE 36
REMARK 3 NUMBER OF REFLECTIONS 14119 2DHE 37
REMARK 3 RESOLUTION RANGE 15.0 - 2.13 ANGSTROMS 2DHE 38
REMARK 3 DATA CUTOFF 3. SIGMA(F) 2DHE 39
REMARK 3 PERCENT COMPLETION 84.7 2DHE 40
REMARK 3 2DHE 41
REMARK 3 NUMBER OF PROTEIN ATOMS 2479 2DHE 42
REMARK 3 NUMBER OF SOLVENT ATOMS 185 2DHE 43
REMARK 4 2DHE 44
REMARK 4 THE ENZYME HAS BEEN SOAKED IN 10 MM SUBSTRATE 1, 2DHE 45
REMARK 4 2-DICHLOROETHANE (DCE) AT PH 6.2 AND AT ROOM TEMPERATURE. 2DHE 46
REMARK 4 THE SUBSTRATE IS DEGRADED AND ONLY THE CHLORIDE PRODUCT IS 2DHE 47
REMARK 4 PRESENT IN THE ACTIVE SITE CAVITY. THE ELECTRON DENSITY 2DHE 48
REMARK 4 FOR THE HYDROLYTIC WATER MOLECULE (HOH 590) HAS ALMOST 2DHE 49
REMARK 4 COMPLETELY DISAPPEARED. 2DHE 50
REMARK 5 2DHE 51
REMARK 5 THE SECONDARY STRUCTURE SPECIFICATIONS ARE AS IN 2HAD. 2DHE 52
REMARK 6 2DHE 53
REMARK 6 THERE IS A DISCREPANCY BETWEEN THE SEQUENCE OBTAINED FROM 2DHE 54
REMARK 6 THE SWISS-PROT ENTRY AND THE SEQUENCE OBTAINED FOUND IN 2DHE 55
REMARK 6 ENTRY FOR RESIDUE 120 (ILE 120 IN THE SWISS-PROT ENTRY, LEU 2DHE 56
REMARK 6 120 IN THIS ENTRY). THE SWISS-PROT ENTRY IS IN ERROR AND 2DHE 57
REMARK 6 THE DEPOSITORS HAVE REQUESTED THAT THE SEQUENCE DATABANKS 2DHE 58
REMARK 6 MAKE THE PROPER CORRECTIONS. 2DHE 59
SEQRES 1 310 MET ILE ASN ALA ILE ARG THR PRO ASP GLN ARG PHE SER 2DHE 60
SEQRES 2 310 ASN LEU ASP GLN TYR PRO PHE SER PRO ASN TYR LEU ASP 2DHE 61
SEQRES 3 310 ASP LEU PRO GLY TYR PRO GLY LEU ARG ALA HIS TYR LEU 2DHE 62
SEQRES 4 310 ASP GLU GLY ASN SER ASP ALA GLU ASP VAL PHE LEU CYS 2DHE 63
SEQRES 5 310 LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG LYS 2DHE 64
SEQRES 6 310 MET ILE PRO VAL PHE ALA GLU SER GLY ALA ARG VAL ILE 2DHE 65
SEQRES 7 310 ALA PRO ASP PHE PHE GLY PHE GLY LYS SER ASP LYS PRO 2DHE 66
SEQRES 8 310 VAL ASP GLU GLU ASP TYR THR PHE GLU PHE HIS ARG ASN 2DHE 67
SEQRES 9 310 PHE LEU LEU ALA LEU ILE GLU ARG LEU ASP LEU ARG ASN 2DHE 68
SEQRES 10 310 ILE THR LEU VAL VAL GLN ASP TRP GLY GLY PHE LEU GLY 2DHE 69
SEQRES 11 310 LEU THR LEU PRO MET ALA ASP PRO SER ARG PHE LYS ARG 2DHE 70
SEQRES 12 310 LEU ILE ILE MET ASN ALA CYS LEU MET THR ASP PRO VAL 2DHE 71
SEQRES 13 310 THR GLN PRO ALA PHE SER ALA PHE VAL THR GLN PRO ALA 2DHE 72
SEQRES 14 310 ASP GLY PHE THR ALA TRP LYS TYR ASP LEU VAL THR PRO 2DHE 73
SEQRES 15 310 SER ASP LEU ARG LEU ASP GLN PHE MET LYS ARG TRP ALA 2DHE 74
SEQRES 16 310 PRO THR LEU THR GLU ALA GLU ALA SER ALA TYR ALA ALA 2DHE 75
SEQRES 17 310 PRO PHE PRO ASP THR SER TYR GLN ALA GLY VAL ARG LYS 2DHE 76
SEQRES 18 310 PHE PRO LYS MET VAL ALA GLN ARG ASP GLN ALA CYS ILE 2DHE 77
SEQRES 19 310 ASP ILE SER THR GLU ALA ILE SER PHE TRP GLN ASN ASP 2DHE 78
SEQRES 20 310 TRP ASN GLY GLN THR PHE MET ALA ILE GLY MET LYS ASP 2DHE 79
SEQRES 21 310 LYS LEU LEU GLY PRO ASP VAL MET TYR PRO MET LYS ALA 2DHE 80
SEQRES 22 310 LEU ILE ASN GLY CYS PRO GLU PRO LEU GLU ILE ALA ASP 2DHE 81
SEQRES 23 310 ALA GLY HIS PHE VAL GLN GLU PHE GLY GLU GLN VAL ALA 2DHE 82
SEQRES 24 310 ARG GLU ALA LEU LYS HIS PHE ALA GLU THR GLU 2DHE 83
FTNOTE 1 2DHE 84
FTNOTE 1 CIS PROLINE - PRO 57 2DHE 85
FTNOTE 2 2DHE 86
FTNOTE 2 CIS PROLINE - PRO 168 2DHE 87
HET CL 600 1 CHLORIDE ION 2DHE 88
FORMUL 2 CL CL1 - 2DHE 89
FORMUL 3 HOH *185(H2 O1) 2DHE 90
HELIX 1 A1 SER 60 GLU 72 1 2DHE 91
HELIX 2 A2 PHE 99 ARG 112 1 2DHE 92
HELIX 3 A3 ASP 124 GLY 130 1 2DHE 93
HELIX 4 A4 PRO 159 PHE 164 1 2DHE 94
HELIX 5 A5 PHE 172 VAL 180 1 2DHE 95
HELIX 6 A6 LEU 187 TRP 194 1 2DHE 96
HELIX 7 A7 GLU 200 ALA 207 1 2DHE 97
HELIX 8 A8 THR 213 ALA 227 1 2DHE 98
HELIX 9 A9 GLN 231 ASN 246 1 2DHE 99
HELIX 10 A10 PRO 265 LEU 274 1 2DHE 100
HELIX 11 A11 VAL 291 HIS 305 1 2DHE 101
SHEET 1 S1 8 SER 21 LEU 25 0 2DHE 102
SHEET 2 S1 8 ALA 36 GLU 41 -1 2DHE 103
SHEET 3 S1 8 ARG 76 PRO 80 -1 2DHE 104
SHEET 4 S1 8 VAL 49 HIS 54 1 2DHE 105
SHEET 5 S1 8 ILE 118 VAL 122 1 2DHE 106
SHEET 6 S1 8 PHE 141 MET 147 1 2DHE 107
SHEET 7 S1 8 GLN 251 GLY 257 1 2DHE 108
SHEET 8 S1 8 GLU 280 ILE 284 1 2DHE 109
TURN 1 T1 ASP 9 PHE 12 NEAR 3/10 TURN 2DHE 110
TURN 2 T2 LEU 28 TYR 31 REVERSE TURN II 2DHE 111
TURN 3 T3 ASN 43 ALA 46 NEAR REVERSE TURN I 2DHE 112
TURN 4 T4 GLY 55 THR 58 NEAR CIS-PROLINE TURN (VI/B) 2DHE 113
TURN 5 T5 PHE 82 PHE 85 NEAR REVERSE TURN II 2DHE 114
TURN 6 T6 PHE 85 SER 88 NEAR REVERSE TURN II' 2DHE 115
TURN 7 T7 ASP 93 ASP 96 3/10 TURN 2DHE 116
TURN 8 T8 GLN 123 TRP 125 "NUCLEOPHILE ELBOW" 2DHE 117
TURN 9 T9 PRO 138 PHE 141 NEAR 3/10 TURN 2DHE 118
TURN 10 T10 ASP 154 THR 157 OPEN TURN III 2DHE 119
TURN 11 T11 THR 166 ALA 169 OPEN CIS-PROLINE TURN (VI/B) 2DHE 120
TURN 12 T12 THR 213 GLN 216 REVERSE TURN I 2DHE 121
TURN 13 T13 ILE 275 CYS 278 REVERSE TURN II 2DHE 122
TURN 14 T14 ILE 284 ALA 287 NEAR REVERSE TURN I 2DHE 123
CRYST1 95.000 72.600 41.500 90.00 90.00 90.00 P 21 21 2 4 2DHE 124
ORIGX1 1.000000 0.000000 0.000000 0.00000 2DHE 125
ORIGX2 0.000000 1.000000 0.000000 0.00000 2DHE 126
ORIGX3 0.000000 0.000000 1.000000 0.00000 2DHE 127
SCALE1 0.010526 0.000000 0.000000 0.00000 2DHE 128
SCALE2 0.000000 0.013774 0.000000 0.00000 2DHE 129
SCALE3 0.000000 0.000000 0.024096 0.00000 2DHE 130 |