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HEADER DEHALOGENASE 07-AUG-92 2HAD 2HAD 2
COMPND HALOALKANE DEHALOGENASE ($P*H 6.2) 2HAD 3
SOURCE (XANTHOBACTER $AUTOTROPHICUS /GJ10$) 2HAD 4
AUTHOR K.H.G.VERSCHUEREN,S.M.FRANKEN,B.W.DIJKSTRA 2HAD 5
REVDAT 1 15-JAN-93 2HAD 0 2HAD 6
REMARK 1 2HAD 7
REMARK 1 REFERENCE 1 2HAD 8
REMARK 1 AUTH S.M.FRANKEN,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA 2HAD 9
REMARK 1 TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN 2HAD 10
REMARK 1 TITL 2 ENZYME TO DETOXIFY HALOGENATED ALKANES 2HAD 11
REMARK 1 REF /EMBO$ J. V. 10 1297 1991 2HAD 12
REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 897 2HAD 13
REMARK 1 REFERENCE 2 2HAD 14
REMARK 1 AUTH H.J.ROZEBOOM,J.KINGMA,D.B.JANSSEN,B.W.DIJKSTRA 2HAD 15
REMARK 1 TITL CRYSTALLIZATION OF HALOALKANE DEHALOGENASE FROM 2HAD 16
REMARK 1 TITL 2 XANTHOBACTER $AUTOTROPHICUS /GJ10$ 2HAD 17
REMARK 1 REF J.MOL.BIOL. V. 200 611 1988 2HAD 18
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2HAD 19
REMARK 2 2HAD 20
REMARK 2 RESOLUTION. 1.9 ANGSTROMS. 2HAD 21
REMARK 3 2HAD 22
REMARK 3 REFINEMENT. BY USE OF THE RESTRAINED LEAST-SQUARES PACKAGE 2HAD 23
REMARK 3 (*TNT*) OF L. F. TEN EYCK AND D. E. TRONRUD. THE R-VALUE 2HAD 24
REMARK 3 IS 0.1684 USING ALL 20296 REFLECTIONS IN THE RESOLUTION 2HAD 25
REMARK 3 RANGE 7.0 TO 1.9 ANGSTROMS. 2HAD 26
REMARK 4 2HAD 27
REMARK 4 THE SECONDARY STRUCTURE SPECIFICATIONS BELOW WERE 2HAD 28
REMARK 4 DETERMINED BY USE OF PROGRAM *DSSP* OF W. KABSCH AND 2HAD 29
REMARK 4 C. SANDER. 2HAD 30
SEQRES 1 310 MET ILE ASN ALA ILE ARG THR PRO ASP GLN ARG PHE SER 2HAD 31
SEQRES 2 310 ASN LEU ASP GLN TYR PRO PHE SER PRO ASN TYR LEU ASP 2HAD 32
SEQRES 3 310 ASP LEU PRO GLY TYR PRO GLY LEU ARG ALA HIS TYR LEU 2HAD 33
SEQRES 4 310 ASP GLU GLY ASN SER ASP ALA GLU ASP VAL PHE LEU CYS 2HAD 34
SEQRES 5 310 LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG LYS 2HAD 35
SEQRES 6 310 MET ILE PRO VAL PHE ALA GLU SER GLY ALA ARG VAL ILE 2HAD 36
SEQRES 7 310 ALA PRO ASP PHE PHE GLY PHE GLY LYS SER ASP LYS PRO 2HAD 37
SEQRES 8 310 VAL ASP GLU GLU ASP TYR THR PHE GLU PHE HIS ARG ASN 2HAD 38
SEQRES 9 310 PHE LEU LEU ALA LEU ILE GLU ARG LEU ASP LEU ARG ASN 2HAD 39
SEQRES 10 310 ILE THR LEU VAL VAL GLN ASP TRP GLY GLY PHE LEU GLY 2HAD 40
SEQRES 11 310 LEU THR LEU PRO MET ALA ASP PRO SER ARG PHE LYS ARG 2HAD 41
SEQRES 12 310 LEU ILE ILE MET ASN ALA CYS LEU MET THR ASP PRO VAL 2HAD 42
SEQRES 13 310 THR GLN PRO ALA PHE SER ALA PHE VAL THR GLN PRO ALA 2HAD 43
SEQRES 14 310 ASP GLY PHE THR ALA TRP LYS TYR ASP LEU VAL THR PRO 2HAD 44
SEQRES 15 310 SER ASP LEU ARG LEU ASP GLN PHE MET LYS ARG TRP ALA 2HAD 45
SEQRES 16 310 PRO THR LEU THR GLU ALA GLU ALA SER ALA TYR ALA ALA 2HAD 46
SEQRES 17 310 PRO PHE PRO ASP THR SER TYR GLN ALA GLY VAL ARG LYS 2HAD 47
SEQRES 18 310 PHE PRO LYS MET VAL ALA GLN ARG ASP GLN ALA CYS ILE 2HAD 48
SEQRES 19 310 ASP ILE SER THR GLU ALA ILE SER PHE TRP GLN ASN ASP 2HAD 49
SEQRES 20 310 TRP ASN GLY GLN THR PHE MET ALA ILE GLY MET LYS ASP 2HAD 50
SEQRES 21 310 LYS LEU LEU GLY PRO ASP VAL MET TYR PRO MET LYS ALA 2HAD 51
SEQRES 22 310 LEU ILE ASN GLY CYS PRO GLU PRO LEU GLU ILE ALA ASP 2HAD 52
SEQRES 23 310 ALA GLY HIS PHE VAL GLN GLU PHE GLY GLU GLN VAL ALA 2HAD 53
SEQRES 24 310 ARG GLU ALA LEU LYS HIS PHE ALA GLU THR GLU 2HAD 54
FTNOTE 1 2HAD 55
FTNOTE 1 RESIDUES PRO 57 AND PRO 168 ARE CIS PROLINES. 2HAD 56
FORMUL 2 HOH *258(H2 O1) 2HAD 57
HELIX 1 A1 SER 60 GLU 72 1 2HAD 58
HELIX 2 A2 PHE 99 ARG 112 1 2HAD 59
HELIX 3 A3 ASP 124 GLY 130 1 2HAD 60
HELIX 4 A4 PRO 159 PHE 164 1 2HAD 61
HELIX 5 A5 PHE 172 VAL 180 1 2HAD 62
HELIX 6 A6 LEU 187 TRP 194 1 2HAD 63
HELIX 7 A7 GLU 200 ALA 207 1 2HAD 64
HELIX 8 A8 THR 213 ALA 227 1 2HAD 65
HELIX 9 A9 GLN 231 ASN 246 1 2HAD 66
HELIX 10 A10 PRO 265 LEU 274 1 2HAD 67
HELIX 11 A11 VAL 291 HIS 305 1 2HAD 68
SHEET 1 S1 8 SER 21 LEU 25 0 2HAD 69
SHEET 2 S1 8 ALA 36 GLU 41 -1 2HAD 70
SHEET 3 S1 8 ARG 76 PRO 80 -1 2HAD 71
SHEET 4 S1 8 VAL 49 HIS 54 1 2HAD 72
SHEET 5 S1 8 ILE 118 VAL 122 1 2HAD 73
SHEET 6 S1 8 PHE 141 MET 147 1 2HAD 74
SHEET 7 S1 8 GLN 251 GLY 257 1 2HAD 75
SHEET 8 S1 8 GLU 280 ILE 284 1 2HAD 76
CRYST1 94.800 72.800 41.400 90.00 90.00 90.00 P 21 21 2 4 2HAD 77
ORIGX1 1.000000 0.000000 0.000000 0.00000 2HAD 78
ORIGX2 0.000000 1.000000 0.000000 0.00000 2HAD 79
ORIGX3 0.000000 0.000000 1.000000 0.00000 2HAD 80
SCALE1 0.010549 0.000000 0.000000 0.00000 2HAD 81
SCALE2 0.000000 0.013736 0.000000 0.00000 2HAD 82
SCALE3 0.000000 0.000000 0.024155 0.00000 2HAD 83
MTRIX1 1 1.000000 0.000000 0.000000 0.50000 2HAD 84
MTRIX2 1 0.000000 -1.000000 0.000000 0.50000 2HAD 85
MTRIX3 1 0.000000 0.000000 -1.000000 0.00000 2HAD 86
MTRIX1 2 -1.000000 0.000000 0.000000 0.50000 2HAD 87
MTRIX2 2 0.000000 1.000000 0.000000 0.50000 2HAD 88
MTRIX3 2 0.000000 0.000000 -1.000000 0.00000 2HAD 89
MTRIX1 3 -1.000000 0.000000 0.000000 0.00000 2HAD 90
MTRIX2 3 0.000000 -1.000000 0.000000 0.00000 2HAD 91
MTRIX3 3 0.000000 0.000000 1.000000 0.00000 2HAD 92 |