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HEADER DEHALOGENASE 13-MAY-93 1EDE 1EDE 2
COMPND HALOALKANE DEHALOGENASE (E.C.3.8.1.5) AT PH 8.2 1EDE 3
SOURCE (XANTHOBACTER AUTOTROPHICUS, STRAIN GJ10) 1EDE 4
AUTHOR K.H.G.VERSCHUEREN,B.W.DIJKSTRA 1EDE 5
REVDAT 1 31-OCT-93 1EDE 0 1EDE 6
JRNL AUTH K.H.G.VERSCHUEREN,S.M.FRANKEN,H.J.ROZEBOOM, 1EDE 7
JRNL AUTH 2 K.H.KALK,B.W.DIJKSTRA 1EDE 8
JRNL TITL REFINED X-RAY STRUCTURES OF HALOALKANE 1EDE 9
JRNL TITL 2 DEHALOGENASE AT PH 6.2 AND PH 8.2 AND 1EDE 10
JRNL TITL 3 IMPLICATIONS FOR THE REACTION MECHANISM 1EDE 11
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1EDE 12
JRNL REFN 353 1EDE 13
REMARK 1 1EDE 14
REMARK 1 REFERENCE 1 1EDE 15
REMARK 1 AUTH S.M.FRANKEN,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA 1EDE 16
REMARK 1 TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN 1EDE 17
REMARK 1 TITL 2 ENZYME TO DETOXIFY HALOGENATED ALKANES 1EDE 18
REMARK 1 REF /EMBO$ J. V. 10 1297 1991 1EDE 19
REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 897 1EDE 20
REMARK 1 REFERENCE 2 1EDE 21
REMARK 1 AUTH H.J.ROZEBOOM,J.KINGMA,D.B.JANSSEN,B.W.DIJKSTRA 1EDE 22
REMARK 1 TITL CRYSTALLIZATION OF HALOALKANE DEHALOGENASE FROM 1EDE 23
REMARK 1 TITL 2 XANTHOBACTER AUTOTROPHICUS GJ10 1EDE 24
REMARK 1 REF J.MOL.BIOL. V. 200 611 1988 1EDE 25
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1EDE 26
REMARK 2 1EDE 27
REMARK 2 RESOLUTION. 1.9 ANGSTROMS. 1EDE 28
REMARK 3 1EDE 29
REMARK 3 REFINEMENT. 1EDE 30
REMARK 3 PROGRAM TNT 1EDE 31
REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 1EDE 32
REMARK 3 R VALUE 0.164 1EDE 33
REMARK 3 RMSD BOND DISTANCES 0.008 ANGSTROMS 1EDE 34
REMARK 3 RMSD BOND ANGLES 2.608 DEGREES 1EDE 35
REMARK 3 1EDE 36
REMARK 3 NUMBER OF REFLECTIONS 19853 1EDE 37
REMARK 3 RESOLUTION RANGE 15. - 1.90 ANGSTROMS 1EDE 38
REMARK 3 DATA CUTOFF 3.0 SIGMA(F) 1EDE 39
REMARK 3 PERCENT COMPLETION 85.2 1EDE 40
REMARK 3 1EDE 41
REMARK 3 NUMBER OF PROTEIN ATOMS 2479 1EDE 42
REMARK 3 NUMBER OF SOLVENT ATOMS 206 1EDE 43
REMARK 4 1EDE 44
REMARK 4 SEQUENCE ADVISORY NOTICE: 1EDE 45
REMARK 4 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1EDE 46
REMARK 4 1EDE 47
REMARK 4 SWISS-PROT ENTRY NAME: HALO_XANAU 1EDE 48
REMARK 4 1EDE 49
REMARK 4 SWISS-PROT RESIDUE PDB SEQRES 1EDE 50
REMARK 4 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1EDE 51
REMARK 4 ILE 120 LEU 120 1EDE 52
REMARK 5 1EDE 53
REMARK 5 THERE IS NO H-BOND BETWEEN THE CATALYTIC RESIDUES ASP 124 1EDE 54
REMARK 5 AND HIS 289 AT PH 8.2. 1EDE 55
REMARK 6 1EDE 56
REMARK 6 THE CELL DIMENSIONS ARE SOMEWHAT DIFFERENT FROM THOSE OF 1EDE 57
REMARK 6 THE STRUCTURE AT PH 6. 1EDE 58
SEQRES 1 310 MET ILE ASN ALA ILE ARG THR PRO ASP GLN ARG PHE SER 1EDE 59
SEQRES 2 310 ASN LEU ASP GLN TYR PRO PHE SER PRO ASN TYR LEU ASP 1EDE 60
SEQRES 3 310 ASP LEU PRO GLY TYR PRO GLY LEU ARG ALA HIS TYR LEU 1EDE 61
SEQRES 4 310 ASP GLU GLY ASN SER ASP ALA GLU ASP VAL PHE LEU CYS 1EDE 62
SEQRES 5 310 LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG LYS 1EDE 63
SEQRES 6 310 MET ILE PRO VAL PHE ALA GLU SER GLY ALA ARG VAL ILE 1EDE 64
SEQRES 7 310 ALA PRO ASP PHE PHE GLY PHE GLY LYS SER ASP LYS PRO 1EDE 65
SEQRES 8 310 VAL ASP GLU GLU ASP TYR THR PHE GLU PHE HIS ARG ASN 1EDE 66
SEQRES 9 310 PHE LEU LEU ALA LEU ILE GLU ARG LEU ASP LEU ARG ASN 1EDE 67
SEQRES 10 310 ILE THR LEU VAL VAL GLN ASP TRP GLY GLY PHE LEU GLY 1EDE 68
SEQRES 11 310 LEU THR LEU PRO MET ALA ASP PRO SER ARG PHE LYS ARG 1EDE 69
SEQRES 12 310 LEU ILE ILE MET ASN ALA CYS LEU MET THR ASP PRO VAL 1EDE 70
SEQRES 13 310 THR GLN PRO ALA PHE SER ALA PHE VAL THR GLN PRO ALA 1EDE 71
SEQRES 14 310 ASP GLY PHE THR ALA TRP LYS TYR ASP LEU VAL THR PRO 1EDE 72
SEQRES 15 310 SER ASP LEU ARG LEU ASP GLN PHE MET LYS ARG TRP ALA 1EDE 73
SEQRES 16 310 PRO THR LEU THR GLU ALA GLU ALA SER ALA TYR ALA ALA 1EDE 74
SEQRES 17 310 PRO PHE PRO ASP THR SER TYR GLN ALA GLY VAL ARG LYS 1EDE 75
SEQRES 18 310 PHE PRO LYS MET VAL ALA GLN ARG ASP GLN ALA CYS ILE 1EDE 76
SEQRES 19 310 ASP ILE SER THR GLU ALA ILE SER PHE TRP GLN ASN ASP 1EDE 77
SEQRES 20 310 TRP ASN GLY GLN THR PHE MET ALA ILE GLY MET LYS ASP 1EDE 78
SEQRES 21 310 LYS LEU LEU GLY PRO ASP VAL MET TYR PRO MET LYS ALA 1EDE 79
SEQRES 22 310 LEU ILE ASN GLY CYS PRO GLU PRO LEU GLU ILE ALA ASP 1EDE 80
SEQRES 23 310 ALA GLY HIS PHE VAL GLN GLU PHE GLY GLU GLN VAL ALA 1EDE 81
SEQRES 24 310 ARG GLU ALA LEU LYS HIS PHE ALA GLU THR GLU 1EDE 82
FTNOTE 1 1EDE 83
FTNOTE 1 RESIDUES 57 AND 168 ARE CIS PROLINES. 1EDE 84
FORMUL 2 HOH *204(H2 O1) 1EDE 85
HELIX 1 A1 SER 60 GLU 72 1 1EDE 86
HELIX 2 A2 PHE 99 ARG 112 1 1EDE 87
HELIX 3 A3 ASP 124 GLY 130 1 1EDE 88
HELIX 4 A4 PRO 159 PHE 164 1 1EDE 89
HELIX 5 A5 PHE 172 VAL 180 1 1EDE 90
HELIX 6 A6 LEU 187 TRP 194 1 1EDE 91
HELIX 7 A7 GLU 200 ALA 207 1 1EDE 92
HELIX 8 A8 THR 213 ALA 227 1 1EDE 93
HELIX 9 A9 GLN 231 ASN 246 1 1EDE 94
HELIX 10 A10 PRO 265 LEU 274 1 1EDE 95
HELIX 11 A11 VAL 291 HIS 305 1 1EDE 96
SHEET 1 S1 8 SER 21 LEU 25 0 1EDE 97
SHEET 2 S1 8 ALA 36 GLU 41 -1 1EDE 98
SHEET 3 S1 8 ARG 76 PRO 80 -1 1EDE 99
SHEET 4 S1 8 VAL 49 HIS 54 1 1EDE 100
SHEET 5 S1 8 ILE 118 VAL 122 1 1EDE 101
SHEET 6 S1 8 PHE 141 MET 147 1 1EDE 102
SHEET 7 S1 8 GLN 251 GLY 257 1 1EDE 103
SHEET 8 S1 8 GLU 280 ILE 284 1 1EDE 104
TURN 1 T1 ASP 9 PHE 12 NEAR 3/10 TURN 1EDE 105
TURN 2 T2 LEU 28 TYR 31 REVERSE TURN II 1EDE 106
TURN 3 T3 ASN 43 ALA 46 NEAR REVERSE TURN I 1EDE 107
TURN 4 T4 GLY 55 THR 58 NEAR CIS-PROLINE TURN (VI/B) 1EDE 108
TURN 5 T5 PHE 82 PHE 85 NEAR REVERSE TURN II 1EDE 109
TURN 6 T6 PHE 85 SER 88 NEAR REVERSE TURN II' 1EDE 110
TURN 7 T7 ASP 93 ASP 96 3/10 TURN 1EDE 111
TURN 8 T8 GLN 123 TRP 125 "NUCLEOPHILE ELBOW" 1EDE 112
TURN 9 T9 PRO 138 PHE 141 NEAR 310 TURN 1EDE 113
TURN 10 T10 ASP 154 THR 157 OPEN TURN III 1EDE 114
TURN 11 T11 THR 166 ALA 169 OPEN CIS-PROLINE TURN (VI/B) 1EDE 115
TURN 12 T12 THR 213 GLN 216 REVERSE TURN I 1EDE 116
TURN 13 T13 ILE 275 CYS 278 REVERSE TURN II 1EDE 117
TURN 14 T14 ILE 284 ALA 287 NEAR REVERSE TURN I 1EDE 118
CRYST1 94.400 72.900 41.400 90.00 90.00 90.00 P 21 21 2 4 1EDE 119
ORIGX1 1.000000 0.000000 0.000000 0.00000 1EDE 120
ORIGX2 0.000000 1.000000 0.000000 0.00000 1EDE 121
ORIGX3 0.000000 0.000000 1.000000 0.00000 1EDE 122
SCALE1 0.010593 0.000000 0.000000 0.00000 1EDE 123
SCALE2 0.000000 0.013717 0.000000 0.00000 1EDE 124
SCALE3 0.000000 0.000000 0.024155 0.00000 1EDE 125 |