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