| content |
HEADER DEHALOGENASE 13-MAY-93 1EDB 1EDB 2
COMPND HALOALKANE DEHALOGENASE (E.C.3.8.1.5) COMPLEX WITH CHLORIDE 1EDB 3
COMPND 2 AT PH 6.2 1EDB 4
SOURCE (XANTHOBACTER AUTOTROPHICUS, STRAIN GJ10) 1EDB 5
AUTHOR K.H.G.VERSCHUEREN,B.W.DIJKSTRA 1EDB 6
REVDAT 1 31-OCT-93 1EDB 0 1EDB 7
JRNL AUTH K.H.G.VERSCHUEREN,J.KINGMA,H.J.ROZEBOOM,K.H.KALK, 1EDB 8
JRNL AUTH 2 D.B.JANSSEN,B.W.DIJKSTRA 1EDB 9
JRNL TITL CRYSTALLOGRAPHIC AND FLUORESCENCE STUDIES OF THE 1EDB 10
JRNL TITL 2 INTERACTION OF HALOALKANE DEHALOGENASE WITH 1EDB 11
JRNL TITL 3 HALIDE IONS: STUDIES WITH HALIDE COMPOUNDS 1EDB 12
JRNL TITL 4 REVEAL A HALIDE BINDING SITE IN THE ACTIVE SITE 1EDB 13
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1EDB 14
JRNL REFN 353 1EDB 15
REMARK 1 1EDB 16
REMARK 1 REFERENCE 1 1EDB 17
REMARK 1 AUTH S.M.FRANKEN,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA 1EDB 18
REMARK 1 TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN 1EDB 19
REMARK 1 TITL 2 ENZYME TO DETOXIFY HALOGENATED ALKANES 1EDB 20
REMARK 1 REF /EMBO$ J. V. 10 1297 1991 1EDB 21
REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 897 1EDB 22
REMARK 1 REFERENCE 2 1EDB 23
REMARK 1 AUTH H.J.ROZEBOOM,J.KINGMA,D.B.JANSSEN,B.W.DIJKSTRA 1EDB 24
REMARK 1 TITL CRYSTALLIZATION OF HALOALKANE DEHALOGENASE FROM 1EDB 25
REMARK 1 TITL 2 XANTHOBACTER AUTOTROPHICUS GJ10 1EDB 26
REMARK 1 REF J.MOL.BIOL. V. 200 611 1988 1EDB 27
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1EDB 28
REMARK 2 1EDB 29
REMARK 2 RESOLUTION. 2.01 ANGSTROMS. 1EDB 30
REMARK 3 1EDB 31
REMARK 3 REFINEMENT. 1EDB 32
REMARK 3 PROGRAM TNT 1EDB 33
REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 1EDB 34
REMARK 3 R VALUE 0.175 1EDB 35
REMARK 3 RMSD BOND ANGLES 3.1 DEGREES 1EDB 36
REMARK 3 1EDB 37
REMARK 3 NUMBER OF REFLECTIONS 16306 1EDB 38
REMARK 3 RESOLUTION RANGE 15. - 2.01 ANGSTROMS 1EDB 39
REMARK 3 DATA CUTOFF 3.0 SIGMA(F) 1EDB 40
REMARK 3 PERCENT COMPLETION 84.8 1EDB 41
REMARK 3 1EDB 42
REMARK 3 NUMBER OF PROTEIN ATOMS 2479 1EDB 43
REMARK 3 NUMBER OF SOLVENT ATOMS 192 1EDB 44
REMARK 3 1EDB 45
REMARK 3 THE STRUCTURE HAS BEEN DETERMINED BY MULTIPLE ISOMORPHOUS 1EDB 46
REMARK 3 REPLACEMENT TECHNIQUES USING THREE HEAVY ATOM DERIVATIVES. 1EDB 47
REMARK 3 CONSULT THE EMBO J. ARTICLE FOR FURTHER DETAILS. 1EDB 48
REMARK 4 1EDB 49
REMARK 4 SEQUENCE ADVISORY NOTICE: 1EDB 50
REMARK 4 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1EDB 51
REMARK 4 1EDB 52
REMARK 4 SWISS-PROT ENTRY NAME: HALO_XANAU 1EDB 53
REMARK 4 1EDB 54
REMARK 4 SWISS-PROT RESIDUE PDB SEQRES 1EDB 55
REMARK 4 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1EDB 56
REMARK 4 ILE 120 LEU 120 1EDB 57
REMARK 5 1EDB 58
REMARK 5 THE DEHALOGENASE HAS BEEN SOAKED IN 5 MM CHLOROACETAMIDE. 1EDB 59
REMARK 5 ONLY THE CHLORINE WAS FOUND, INCLUDED BETWEEN TRP 125 AND 1EDB 60
REMARK 5 TRP 175. 1EDB 61
SEQRES 1 310 MET ILE ASN ALA ILE ARG THR PRO ASP GLN ARG PHE SER 1EDB 62
SEQRES 2 310 ASN LEU ASP GLN TYR PRO PHE SER PRO ASN TYR LEU ASP 1EDB 63
SEQRES 3 310 ASP LEU PRO GLY TYR PRO GLY LEU ARG ALA HIS TYR LEU 1EDB 64
SEQRES 4 310 ASP GLU GLY ASN SER ASP ALA GLU ASP VAL PHE LEU CYS 1EDB 65
SEQRES 5 310 LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG LYS 1EDB 66
SEQRES 6 310 MET ILE PRO VAL PHE ALA GLU SER GLY ALA ARG VAL ILE 1EDB 67
SEQRES 7 310 ALA PRO ASP PHE PHE GLY PHE GLY LYS SER ASP LYS PRO 1EDB 68
SEQRES 8 310 VAL ASP GLU GLU ASP TYR THR PHE GLU PHE HIS ARG ASN 1EDB 69
SEQRES 9 310 PHE LEU LEU ALA LEU ILE GLU ARG LEU ASP LEU ARG ASN 1EDB 70
SEQRES 10 310 ILE THR LEU VAL VAL GLN ASP TRP GLY GLY PHE LEU GLY 1EDB 71
SEQRES 11 310 LEU THR LEU PRO MET ALA ASP PRO SER ARG PHE LYS ARG 1EDB 72
SEQRES 12 310 LEU ILE ILE MET ASN ALA CYS LEU MET THR ASP PRO VAL 1EDB 73
SEQRES 13 310 THR GLN PRO ALA PHE SER ALA PHE VAL THR GLN PRO ALA 1EDB 74
SEQRES 14 310 ASP GLY PHE THR ALA TRP LYS TYR ASP LEU VAL THR PRO 1EDB 75
SEQRES 15 310 SER ASP LEU ARG LEU ASP GLN PHE MET LYS ARG TRP ALA 1EDB 76
SEQRES 16 310 PRO THR LEU THR GLU ALA GLU ALA SER ALA TYR ALA ALA 1EDB 77
SEQRES 17 310 PRO PHE PRO ASP THR SER TYR GLN ALA GLY VAL ARG LYS 1EDB 78
SEQRES 18 310 PHE PRO LYS MET VAL ALA GLN ARG ASP GLN ALA CYS ILE 1EDB 79
SEQRES 19 310 ASP ILE SER THR GLU ALA ILE SER PHE TRP GLN ASN ASP 1EDB 80
SEQRES 20 310 TRP ASN GLY GLN THR PHE MET ALA ILE GLY MET LYS ASP 1EDB 81
SEQRES 21 310 LYS LEU LEU GLY PRO ASP VAL MET TYR PRO MET LYS ALA 1EDB 82
SEQRES 22 310 LEU ILE ASN GLY CYS PRO GLU PRO LEU GLU ILE ALA ASP 1EDB 83
SEQRES 23 310 ALA GLY HIS PHE VAL GLN GLU PHE GLY GLU GLN VAL ALA 1EDB 84
SEQRES 24 310 ARG GLU ALA LEU LYS HIS PHE ALA GLU THR GLU 1EDB 85
FTNOTE 1 1EDB 86
FTNOTE 1 RESIDUES 57 AND 168 ARE CIS PROLINES. 1EDB 87
HET CL 600 1 CHLORIDE ION 1EDB 88
FORMUL 2 CL CL1 - 1EDB 89
FORMUL 3 HOH *191(H2 O1) 1EDB 90
HELIX 1 A1 SER 60 GLU 72 1 1EDB 91
HELIX 2 A2 PHE 99 ARG 112 1 1EDB 92
HELIX 3 A3 ASP 124 GLY 130 1 1EDB 93
HELIX 4 A4 PRO 159 PHE 164 1 1EDB 94
HELIX 5 A5 PHE 172 VAL 180 1 1EDB 95
HELIX 6 A6 LEU 187 TRP 194 1 1EDB 96
HELIX 7 A7 GLU 200 ALA 207 1 1EDB 97
HELIX 8 A8 THR 213 ALA 227 1 1EDB 98
HELIX 9 A9 GLN 231 ASN 246 1 1EDB 99
HELIX 10 A10 PRO 265 LEU 274 1 1EDB 100
HELIX 11 A11 VAL 291 HIS 305 1 1EDB 101
SHEET 1 S1 8 SER 21 LEU 25 0 1EDB 102
SHEET 2 S1 8 ALA 36 GLU 41 -1 1EDB 103
SHEET 3 S1 8 ARG 76 PRO 80 -1 1EDB 104
SHEET 4 S1 8 VAL 49 HIS 54 1 1EDB 105
SHEET 5 S1 8 ILE 118 VAL 122 1 1EDB 106
SHEET 6 S1 8 PHE 141 MET 147 1 1EDB 107
SHEET 7 S1 8 GLN 251 GLY 257 1 1EDB 108
SHEET 8 S1 8 GLU 280 ILE 284 1 1EDB 109
TURN 1 T1 ASP 9 PHE 12 NEAR 3/10 TURN 1EDB 110
TURN 2 T2 LEU 28 TYR 31 REVERSE TURN II 1EDB 111
TURN 3 T3 ASN 43 ALA 46 NEAR REVERSE TURN I 1EDB 112
TURN 4 T4 GLY 55 THR 58 NEAR CIS-PROLINE TURN (VI/B) 1EDB 113
TURN 5 T5 PHE 82 PHE 85 NEAR REVERSE TURN II 1EDB 114
TURN 6 T6 PHE 85 SER 88 NEAR REVERSE TURN II' 1EDB 115
TURN 7 T7 ASP 93 ASP 96 3/10 TURN 1EDB 116
TURN 8 T8 GLN 123 TRP 125 "NUCLEOPHILE ELBOW" 1EDB 117
TURN 9 T9 PRO 138 PHE 141 NEAR 310 TURN 1EDB 118
TURN 10 T10 ASP 154 THR 157 OPEN TURN III 1EDB 119
TURN 11 T11 THR 166 ALA 169 OPEN CIS-PROLINE TURN (VI/B) 1EDB 120
TURN 12 T12 THR 213 GLN 216 REVERSE TURN I 1EDB 121
TURN 13 T13 ILE 275 CYS 278 REVERSE TURN II 1EDB 122
TURN 14 T14 ILE 284 ALA 287 NEAR REVERSE TURN I 1EDB 123
CRYST1 95.400 72.900 41.400 90.00 90.00 90.00 P 21 21 2 4 1EDB 124
ORIGX1 1.000000 0.000000 0.000000 0.00000 1EDB 125
ORIGX2 0.000000 1.000000 0.000000 0.00000 1EDB 126
ORIGX3 0.000000 0.000000 1.000000 0.00000 1EDB 127
SCALE1 0.010482 0.000000 0.000000 0.00000 1EDB 128
SCALE2 0.000000 0.013717 0.000000 0.00000 1EDB 129
SCALE3 0.000000 0.000000 0.024155 0.00000 1EDB 130 |