| content |
HEADER DEHALOGENASE 13-MAY-93 1EDD 1EDD 2
COMPND HALOALKANE DEHALOGENASE (E.C.3.8.1.5) COMPLEX WITH CHLORIDE 1EDD 3
COMPND 2 AT PH 8 1EDD 4
SOURCE (XANTHOBACTER AUTOTROPHICUS, STRAIN GJ10) 1EDD 5
AUTHOR K.H.G.VERSCHUEREN,B.W.DIJKSTRA 1EDD 6
REVDAT 1 31-OCT-93 1EDD 0 1EDD 7
JRNL AUTH K.H.G.VERSCHUEREN,J.KINGMA,H.J.ROZEBOOM,K.H.KALK, 1EDD 8
JRNL AUTH 2 D.B.JANSSEN,B.W.DIJKSTRA 1EDD 9
JRNL TITL CRYSTALLOGRAPHIC AND FLUORESCENCE STUDIES OF THE 1EDD 10
JRNL TITL 2 INTERACTION OF HALOALKANE DEHALOGENASE WITH 1EDD 11
JRNL TITL 3 HALIDE IONS: STUDIES WITH HALIDE COMPOUNDS 1EDD 12
JRNL TITL 4 REVEAL A HALIDE BINDING SITE IN THE ACTIVE SITE 1EDD 13
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1EDD 14
JRNL REFN 353 1EDD 15
REMARK 1 1EDD 16
REMARK 1 REFERENCE 1 1EDD 17
REMARK 1 AUTH S.M.FRANKEN,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA 1EDD 18
REMARK 1 TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN 1EDD 19
REMARK 1 TITL 2 ENZYME TO DETOXIFY HALOGENATED ALKANES 1EDD 20
REMARK 1 REF /EMBO$ J. V. 10 1297 1991 1EDD 21
REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 897 1EDD 22
REMARK 1 REFERENCE 2 1EDD 23
REMARK 1 AUTH H.J.ROZEBOOM,J.KINGMA,D.B.JANSSEN,B.W.DIJKSTRA 1EDD 24
REMARK 1 TITL CRYSTALLIZATION OF HALOALKANE DEHALOGENASE FROM 1EDD 25
REMARK 1 TITL 2 XANTHOBACTER AUTOTROPHICUS GJ10 1EDD 26
REMARK 1 REF J.MOL.BIOL. V. 200 611 1988 1EDD 27
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1EDD 28
REMARK 2 1EDD 29
REMARK 2 RESOLUTION. 2.10 ANGSTROMS. 1EDD 30
REMARK 3 1EDD 31
REMARK 3 REFINEMENT. 1EDD 32
REMARK 3 PROGRAM TNT 1EDD 33
REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 1EDD 34
REMARK 3 R VALUE 0.181 1EDD 35
REMARK 3 RMSD BOND DISTANCES 0.013 ANGSTROMS 1EDD 36
REMARK 3 RMSD BOND ANGLES 3.4 DEGREES 1EDD 37
REMARK 3 1EDD 38
REMARK 3 NUMBER OF REFLECTIONS 12376 1EDD 39
REMARK 3 RESOLUTION RANGE 15. - 2.19 ANGSTROMS 1EDD 40
REMARK 3 DATA CUTOFF 3.0 SIGMA(F) 1EDD 41
REMARK 3 PERCENT COMPLETION 81.2 1EDD 42
REMARK 3 1EDD 43
REMARK 3 NUMBER OF PROTEIN ATOMS 2479 1EDD 44
REMARK 3 NUMBER OF SOLVENT ATOMS 172 1EDD 45
REMARK 4 1EDD 46
REMARK 4 SEQUENCE ADVISORY NOTICE: 1EDD 47
REMARK 4 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1EDD 48
REMARK 4 1EDD 49
REMARK 4 SWISS-PROT ENTRY NAME: HALO_XANAU 1EDD 50
REMARK 4 1EDD 51
REMARK 4 SWISS-PROT RESIDUE PDB SEQRES 1EDD 52
REMARK 4 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1EDD 53
REMARK 4 ILE 120 LEU 120 1EDD 54
REMARK 5 1EDD 55
REMARK 5 THE DEHALOGENASE HAS BEEN SOAKED IN 10 MM SODIUM CHLORIDE. 1EDD 56
REMARK 5 THE CHLORIDE ION WAS FOUND IN THE ACTIVE SITE CAVITY 1EDD 57
REMARK 5 BETWEEN TRP 125 AND TRP 175. 1EDD 58
SEQRES 1 310 MET ILE ASN ALA ILE ARG THR PRO ASP GLN ARG PHE SER 1EDD 59
SEQRES 2 310 ASN LEU ASP GLN TYR PRO PHE SER PRO ASN TYR LEU ASP 1EDD 60
SEQRES 3 310 ASP LEU PRO GLY TYR PRO GLY LEU ARG ALA HIS TYR LEU 1EDD 61
SEQRES 4 310 ASP GLU GLY ASN SER ASP ALA GLU ASP VAL PHE LEU CYS 1EDD 62
SEQRES 5 310 LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG LYS 1EDD 63
SEQRES 6 310 MET ILE PRO VAL PHE ALA GLU SER GLY ALA ARG VAL ILE 1EDD 64
SEQRES 7 310 ALA PRO ASP PHE PHE GLY PHE GLY LYS SER ASP LYS PRO 1EDD 65
SEQRES 8 310 VAL ASP GLU GLU ASP TYR THR PHE GLU PHE HIS ARG ASN 1EDD 66
SEQRES 9 310 PHE LEU LEU ALA LEU ILE GLU ARG LEU ASP LEU ARG ASN 1EDD 67
SEQRES 10 310 ILE THR LEU VAL VAL GLN ASP TRP GLY GLY PHE LEU GLY 1EDD 68
SEQRES 11 310 LEU THR LEU PRO MET ALA ASP PRO SER ARG PHE LYS ARG 1EDD 69
SEQRES 12 310 LEU ILE ILE MET ASN ALA CYS LEU MET THR ASP PRO VAL 1EDD 70
SEQRES 13 310 THR GLN PRO ALA PHE SER ALA PHE VAL THR GLN PRO ALA 1EDD 71
SEQRES 14 310 ASP GLY PHE THR ALA TRP LYS TYR ASP LEU VAL THR PRO 1EDD 72
SEQRES 15 310 SER ASP LEU ARG LEU ASP GLN PHE MET LYS ARG TRP ALA 1EDD 73
SEQRES 16 310 PRO THR LEU THR GLU ALA GLU ALA SER ALA TYR ALA ALA 1EDD 74
SEQRES 17 310 PRO PHE PRO ASP THR SER TYR GLN ALA GLY VAL ARG LYS 1EDD 75
SEQRES 18 310 PHE PRO LYS MET VAL ALA GLN ARG ASP GLN ALA CYS ILE 1EDD 76
SEQRES 19 310 ASP ILE SER THR GLU ALA ILE SER PHE TRP GLN ASN ASP 1EDD 77
SEQRES 20 310 TRP ASN GLY GLN THR PHE MET ALA ILE GLY MET LYS ASP 1EDD 78
SEQRES 21 310 LYS LEU LEU GLY PRO ASP VAL MET TYR PRO MET LYS ALA 1EDD 79
SEQRES 22 310 LEU ILE ASN GLY CYS PRO GLU PRO LEU GLU ILE ALA ASP 1EDD 80
SEQRES 23 310 ALA GLY HIS PHE VAL GLN GLU PHE GLY GLU GLN VAL ALA 1EDD 81
SEQRES 24 310 ARG GLU ALA LEU LYS HIS PHE ALA GLU THR GLU 1EDD 82
FTNOTE 1 1EDD 83
FTNOTE 1 RESIDUES 57 AND 168 ARE CIS PROLINES. 1EDD 84
HET CL 600 1 CHLORIDE ION 1EDD 85
FORMUL 2 CL CL1 - 1EDD 86
FORMUL 3 HOH *172(H2 O1) 1EDD 87
HELIX 1 A1 SER 60 GLU 72 1 1EDD 88
HELIX 2 A2 PHE 99 ARG 112 1 1EDD 89
HELIX 3 A3 ASP 124 GLY 130 1 1EDD 90
HELIX 4 A4 PRO 159 PHE 164 1 1EDD 91
HELIX 5 A5 PHE 172 VAL 180 1 1EDD 92
HELIX 6 A6 LEU 187 TRP 194 1 1EDD 93
HELIX 7 A7 GLU 200 ALA 207 1 1EDD 94
HELIX 8 A8 THR 213 ALA 227 1 1EDD 95
HELIX 9 A9 GLN 231 ASN 246 1 1EDD 96
HELIX 10 A10 PRO 265 LEU 274 1 1EDD 97
HELIX 11 A11 VAL 291 HIS 305 1 1EDD 98
SHEET 1 S1 8 SER 21 LEU 25 0 1EDD 99
SHEET 2 S1 8 ALA 36 GLU 41 -1 1EDD 100
SHEET 3 S1 8 ARG 76 PRO 80 -1 1EDD 101
SHEET 4 S1 8 VAL 49 HIS 54 1 1EDD 102
SHEET 5 S1 8 ILE 118 VAL 122 1 1EDD 103
SHEET 6 S1 8 PHE 141 MET 147 1 1EDD 104
SHEET 7 S1 8 GLN 251 GLY 257 1 1EDD 105
SHEET 8 S1 8 GLU 280 ILE 284 1 1EDD 106
TURN 1 T1 ASP 9 PHE 12 NEAR 3/10 TURN 1EDD 107
TURN 2 T2 LEU 28 TYR 31 REVERSE TURN II 1EDD 108
TURN 3 T3 ASN 43 ALA 46 NEAR REVERSE TURN I 1EDD 109
TURN 4 T4 GLY 55 THR 58 NEAR CIS-PROLINE TURN (VI/B) 1EDD 110
TURN 5 T5 PHE 82 PHE 85 NEAR REVERSE TURN II 1EDD 111
TURN 6 T6 PHE 85 SER 88 NEAR REVERSE TURN II' 1EDD 112
TURN 7 T7 ASP 93 ASP 96 3/10 TURN 1EDD 113
TURN 8 T8 GLN 123 TRP 125 "NUCLEOPHILE ELBOW" 1EDD 114
TURN 9 T9 PRO 138 PHE 141 NEAR 310 TURN 1EDD 115
TURN 10 T10 ASP 154 THR 157 OPEN TURN III 1EDD 116
TURN 11 T11 THR 166 ALA 169 OPEN CIS-PROLINE TURN (VI/B) 1EDD 117
TURN 12 T12 THR 213 GLN 216 REVERSE TURN I 1EDD 118
TURN 13 T13 ILE 275 CYS 278 REVERSE TURN II 1EDD 119
TURN 14 T14 ILE 284 ALA 287 NEAR REVERSE TURN I 1EDD 120
CRYST1 94.400 72.500 41.300 90.00 90.00 90.00 P 21 21 2 4 1EDD 121
ORIGX1 1.000000 0.000000 0.000000 0.00000 1EDD 122
ORIGX2 0.000000 1.000000 0.000000 0.00000 1EDD 123
ORIGX3 0.000000 0.000000 1.000000 0.00000 1EDD 124
SCALE1 0.010593 0.000000 0.000000 0.00000 1EDD 125
SCALE2 0.000000 0.013793 0.000000 0.00000 1EDD 126
SCALE3 0.000000 0.000000 0.024213 0.00000 1EDD 127 |