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HEADER DEHALOGENASE 31-AUG-93 2EDC 2EDC 2
COMPND HALOALKANE DEHALOGENASE (E.C.3.8.1.5) 2EDC 3
SOURCE (XANTHOBACTER AUTOTROPHICUS, STRAIN GJ10) 2EDC 4
AUTHOR K.H.G.VERSCHUEREN,B.W.DIJKSTRA 2EDC 5
REVDAT 1 31-JAN-94 2EDC 0 2EDC 6
JRNL AUTH K.H.G.VERSCHUEREN,J.KINGMA,H.J.ROZEBOOM,K.H.KALK, 2EDC 7
JRNL AUTH 2 D.B.JANSSEN,B.W.DIJKSTRA 2EDC 8
JRNL TITL CRYSTALLOGRAPHIC AND FLUORESCENCE STUDIES OF THE 2EDC 9
JRNL TITL 2 INTERACTION OF HALOALKANE DEHALOGENASE WITH HALIDE 2EDC 10
JRNL TITL 3 IONS: STUDIES WITH HALIDE COMPOUNDS REVEAL A 2EDC 11
JRNL TITL 4 HALIDE BINDING SITE IN THE ACTIVE SITE 2EDC 12
JRNL REF BIOCHEMISTRY V. 32 9031 1993 2EDC 13
JRNL REFN ASTM BICHAW US ISSN 0006-2960 033 2EDC 14
REMARK 1 2EDC 15
REMARK 1 REFERENCE 1 2EDC 16
REMARK 1 AUTH S.M.FRANKEN,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA 2EDC 17
REMARK 1 TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN 2EDC 18
REMARK 1 TITL 2 ENZYME TO DETOXIFY HALOGENATED ALKANES 2EDC 19
REMARK 1 REF /EMBO$ J. V. 10 1297 1991 2EDC 20
REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 897 2EDC 21
REMARK 1 REFERENCE 2 2EDC 22
REMARK 1 AUTH H.J.ROZEBOOM,J.KINGMA,D.B.JANSSEN,B.W.DIJKSTRA 2EDC 23
REMARK 1 TITL CRYSTALLIZATION OF HALOALKANE DEHALOGENASE FROM 2EDC 24
REMARK 1 TITL 2 XANTHOBACTER AUTOTROPHICUS GJ10 2EDC 25
REMARK 1 REF J.MOL.BIOL. V. 200 611 1988 2EDC 26
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2EDC 27
REMARK 2 2EDC 28
REMARK 2 RESOLUTION. 2.3 ANGSTROMS. 2EDC 29
REMARK 3 2EDC 30
REMARK 3 REFINEMENT. 2EDC 31
REMARK 3 PROGRAM TNT 2EDC 32
REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 2EDC 33
REMARK 3 R VALUE 0.177 2EDC 34
REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS 2EDC 35
REMARK 3 RMSD BOND ANGLES 3.2 DEGREES 2EDC 36
REMARK 3 2EDC 37
REMARK 3 NUMBER OF PROTEIN ATOMS 2479 2EDC 38
REMARK 3 NUMBER OF SOLVENT ATOMS 125 2EDC 39
REMARK 4 2EDC 40
REMARK 4 THE DEHALOGENASE HAS BEEN SOAKED IN 5 MM POTASSIUM IODIDE, 2EDC 41
REMARK 4 THE IODIDE ION WAS FOUND IN THE ACTIVE SITE CAVITY BETWEEN 2EDC 42
REMARK 4 TRP125 AND TRP175 2EDC 43
REMARK 5 2EDC 44
REMARK 5 SEQUENCE ADVISORY NOTICE: 2EDC 45
REMARK 5 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 2EDC 46
REMARK 5 2EDC 47
REMARK 5 SWISS-PROT ENTRY NAME: HALO_XANAU 2EDC 48
REMARK 5 2EDC 49
REMARK 5 SWISS-PROT RESIDUE PDB SEQRES 2EDC 50
REMARK 5 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 2EDC 51
REMARK 5 ILE 120 LEU 120 2EDC 52
REMARK 5 2EDC 53
REMARK 5 THE SWISS-PROT ENTRY IS IN ERROR AND THE DEPOSITORS HAVE 2EDC 54
REMARK 5 REQUESTED THAT THE SEQUENCE DATABANKS MAKE THE PROPER 2EDC 55
REMARK 5 CORRECTIONS. 2EDC 56
SEQRES 1 310 MET ILE ASN ALA ILE ARG THR PRO ASP GLN ARG PHE SER 2EDC 57
SEQRES 2 310 ASN LEU ASP GLN TYR PRO PHE SER PRO ASN TYR LEU ASP 2EDC 58
SEQRES 3 310 ASP LEU PRO GLY TYR PRO GLY LEU ARG ALA HIS TYR LEU 2EDC 59
SEQRES 4 310 ASP GLU GLY ASN SER ASP ALA GLU ASP VAL PHE LEU CYS 2EDC 60
SEQRES 5 310 LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG LYS 2EDC 61
SEQRES 6 310 MET ILE PRO VAL PHE ALA GLU SER GLY ALA ARG VAL ILE 2EDC 62
SEQRES 7 310 ALA PRO ASP PHE PHE GLY PHE GLY LYS SER ASP LYS PRO 2EDC 63
SEQRES 8 310 VAL ASP GLU GLU ASP TYR THR PHE GLU PHE HIS ARG ASN 2EDC 64
SEQRES 9 310 PHE LEU LEU ALA LEU ILE GLU ARG LEU ASP LEU ARG ASN 2EDC 65
SEQRES 10 310 ILE THR LEU VAL VAL GLN ASP TRP GLY GLY PHE LEU GLY 2EDC 66
SEQRES 11 310 LEU THR LEU PRO MET ALA ASP PRO SER ARG PHE LYS ARG 2EDC 67
SEQRES 12 310 LEU ILE ILE MET ASN ALA CYS LEU MET THR ASP PRO VAL 2EDC 68
SEQRES 13 310 THR GLN PRO ALA PHE SER ALA PHE VAL THR GLN PRO ALA 2EDC 69
SEQRES 14 310 ASP GLY PHE THR ALA TRP LYS TYR ASP LEU VAL THR PRO 2EDC 70
SEQRES 15 310 SER ASP LEU ARG LEU ASP GLN PHE MET LYS ARG TRP ALA 2EDC 71
SEQRES 16 310 PRO THR LEU THR GLU ALA GLU ALA SER ALA TYR ALA ALA 2EDC 72
SEQRES 17 310 PRO PHE PRO ASP THR SER TYR GLN ALA GLY VAL ARG LYS 2EDC 73
SEQRES 18 310 PHE PRO LYS MET VAL ALA GLN ARG ASP GLN ALA CYS ILE 2EDC 74
SEQRES 19 310 ASP ILE SER THR GLU ALA ILE SER PHE TRP GLN ASN ASP 2EDC 75
SEQRES 20 310 TRP ASN GLY GLN THR PHE MET ALA ILE GLY MET LYS ASP 2EDC 76
SEQRES 21 310 LYS LEU LEU GLY PRO ASP VAL MET TYR PRO MET LYS ALA 2EDC 77
SEQRES 22 310 LEU ILE ASN GLY CYS PRO GLU PRO LEU GLU ILE ALA ASP 2EDC 78
SEQRES 23 310 ALA GLY HIS PHE VAL GLN GLU PHE GLY GLU GLN VAL ALA 2EDC 79
SEQRES 24 310 ARG GLU ALA LEU LYS HIS PHE ALA GLU THR GLU 2EDC 80
FTNOTE 1 2EDC 81
FTNOTE 1 RESIDUES PRO 57 AND PRO 168 ARE CIS PROLINES. 2EDC 82
HET IOD 600 1 IODIDE ION 2EDC 83
FORMUL 2 IOD I1 - 2EDC 84
FORMUL 3 HOH *125(H2 O1) 2EDC 85
HELIX 1 A1 SER 60 GLU 72 1 2EDC 86
HELIX 2 A2 PHE 99 ARG 112 1 2EDC 87
HELIX 3 A3 ASP 124 GLY 130 1 2EDC 88
HELIX 4 A4 PRO 159 PHE 164 1 2EDC 89
HELIX 5 A5 PHE 172 VAL 180 1 2EDC 90
HELIX 6 A6 LEU 187 TRP 194 1 2EDC 91
HELIX 7 A7 GLU 200 ALA 207 1 2EDC 92
HELIX 8 A8 THR 213 ALA 227 1 2EDC 93
HELIX 9 A9 GLN 231 ASN 246 1 2EDC 94
HELIX 10 A10 PRO 265 LEU 274 1 2EDC 95
HELIX 11 A11 VAL 291 HIS 305 1 2EDC 96
SHEET 1 S1 8 SER 21 LEU 25 0 2EDC 97
SHEET 2 S1 8 ALA 36 GLU 41 -1 2EDC 98
SHEET 3 S1 8 ARG 76 PRO 80 -1 2EDC 99
SHEET 4 S1 8 VAL 49 HIS 54 1 2EDC 100
SHEET 5 S1 8 ILE 118 VAL 122 1 2EDC 101
SHEET 6 S1 8 PHE 141 MET 147 1 2EDC 102
SHEET 7 S1 8 GLN 251 GLY 257 1 2EDC 103
SHEET 8 S1 8 GLU 280 ILE 284 1 2EDC 104
TURN 1 T1 ASP 9 PHE 12 NEAR 3/10 TURN 2EDC 105
TURN 2 T2 LEU 28 TYR 31 REVERSE TURN II 2EDC 106
TURN 3 T3 ASN 43 ALA 46 NEAR REVERSE TURN I 2EDC 107
TURN 4 T4 GLY 55 THR 58 NEAR CIS-PROLINE TURN (VI/B) 2EDC 108
TURN 5 T5 PHE 82 PHE 85 NEAR REVERSE TURN II 2EDC 109
TURN 6 T6 PHE 85 SER 88 NEAR REVERSE TURN II' 2EDC 110
TURN 7 T7 ASP 93 ASP 96 3/10 TURN 2EDC 111
TURN 8 T8 GLN 123 TRP 125 "NUCLEOPHILE ELBOW" 2EDC 112
TURN 9 T9 PRO 138 PHE 141 NEAR 310 TURN 2EDC 113
TURN 10 T10 ASP 154 THR 157 OPEN TURN III 2EDC 114
TURN 11 T11 THR 166 ALA 169 OPEN CIS-PROLINE TURN (VI/B) 2EDC 115
TURN 12 T12 THR 213 GLN 216 REVERSE TURN I 2EDC 116
TURN 13 T13 ILE 275 CYS 278 REVERSE TURN II 2EDC 117
TURN 14 T14 ILE 284 ALA 287 NEAR REVERSE TURN I 2EDC 118
CRYST1 94.900 73.100 41.500 90.00 90.00 90.00 P 21 21 2 4 2EDC 119
ORIGX1 1.000000 0.000000 0.000000 0.00000 2EDC 120
ORIGX2 0.000000 1.000000 0.000000 0.00000 2EDC 121
ORIGX3 0.000000 0.000000 1.000000 0.00000 2EDC 122
SCALE1 0.010537 0.000000 0.000000 0.00000 2EDC 123
SCALE2 0.000000 0.013680 0.000000 0.00000 2EDC 124
SCALE3 0.000000 0.000000 0.024096 0.00000 2EDC 125 |