HEADER HYDROLASE(SERINE ESTERASE) 06-APR-94 1CUS 1CUS 2 COMPND CUTINASE (E.C.3.1.1.-) 1CUS 3 SOURCE FUNGUS (FUSARIUM SOLANI, SUBSP. PISI) RECOMBINANT FORM 1CUS 4 SOURCE 2 EXPRESSED IN (ESCHERICHIA COLI) 1CUS 5 AUTHOR C.MARTINEZ,C.CAMBILLAU 1CUS 6 REVDAT 1 31-JUL-94 1CUS 0 1CUS 7 REMARK 1 1CUS 8 REMARK 1 REFERENCE 1 1CUS 9 REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,M.LAUWEREYS,G.MATTHYSSENS, 1CUS 10 REMARK 1 AUTH 2 C.CAMBILLAU 1CUS 11 REMARK 1 TITL FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH 1CUS 12 REMARK 1 TITL 2 A CATALYTIC SERINE ACCESSIBLE TO SOLVENT 1CUS 13 REMARK 1 REF NATURE V. 356 615 1992 1CUS 14 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1CUS 15 REMARK 1 REFERENCE 2 1CUS 16 REMARK 1 AUTH C.MARTINEZ,A.NICOLAS,H.VAN TILBEURGH,M.-P.EGLOFF, 1CUS 17 REMARK 1 AUTH 2 C.CUDREY,R.VERGER,C.CAMBILLAU 1CUS 18 REMARK 1 TITL CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED 1CUS 19 REMARK 1 TITL 2 OXYANION HOLE 1CUS 20 REMARK 1 REF BIOCHEMISTRY V. 33 83 1994 1CUS 21 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1CUS 22 REMARK 1 REFERENCE 3 1CUS 23 REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,P.STANSSENS,M.LAUWEREYS, 1CUS 24 REMARK 1 AUTH 2 C.CAMBILLAU 1CUS 25 REMARK 1 TITL ENGINEERING CYSTEINE MUTANTS TO OBTAIN 1CUS 26 REMARK 1 TITL 2 CRYSTALLOGRAPHIC PHASES WITH A CUTINASE FROM 1CUS 27 REMARK 1 TITL 3 FUSARIUM SOLANI PISI 1CUS 28 REMARK 1 REF PROTEIN ENG. V. 6 157 1993 1CUS 29 REMARK 1 REFN ASTM PRENE9 UK ISSN 0269-2139 0859 1CUS 30 REMARK 1 REFERENCE 4 1CUS 31 REMARK 1 AUTH C.ABERGEL,C.MARTINEZ,J.FONTECILLA-CAMPS,C.CAMBILLAU 1CUS 32 REMARK 1 AUTH 2 ,P.DE GEUS,M.LAUWEREYS 1CUS 33 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STUDY OF A 1CUS 34 REMARK 1 TITL 2 RECOMBINANT CUTINASE FROM FUSARIUM SOLANI PISI 1CUS 35 REMARK 1 REF J.MOL.BIOL. V. 215 215 1990 1CUS 36 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1CUS 37 REMARK 2 1CUS 38 REMARK 2 RESOLUTION. 1.25 ANGSTROMS. 1CUS 39 REMARK 3 1CUS 40 REMARK 3 REFINEMENT. 1CUS 41 REMARK 3 PROGRAM X-PLOR 1CUS 42 REMARK 3 AUTHORS BRUNGER 1CUS 43 REMARK 3 R VALUE 0.158 1CUS 44 REMARK 3 RMSD BOND DISTANCES 0.009 ANGSTROMS 1CUS 45 REMARK 3 RMSD BOND ANGLES 2.08 DEGREES 1CUS 46 REMARK 3 1CUS 47 REMARK 3 RESOLUTION RANGE 6.0 - 1.25 ANGSTROMS 1CUS 48 REMARK 4 1CUS 49 REMARK 4 SITE *CAT* PRESENTED BELOW REFERS TO THE CATALYTIC TRIAD. 1CUS 50 REMARK 5 1CUS 51 REMARK 5 CROSS REFERENCE TO SEQUENCE DATABASE 1CUS 52 REMARK 5 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1CUS 53 REMARK 6 CUTI_FUSSO 1CUS 54 REMARK 7 1CUS 55 REMARK 7 SEQUENCE ADVISORY NOTICE: 1CUS 56 REMARK 7 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1CUS 57 REMARK 7 1CUS 58 REMARK 7 SWISS-PROT ENTRY NAME: CUTI_FUSSO 1CUS 59 REMARK 7 1CUS 60 REMARK 7 SWISS-PROT RESIDUE PDB SEQRES 1CUS 61 REMARK 7 1CUS 62 REMARK 7 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1CUS 63 REMARK 7 ARG 48 ALA 32 1CUS 64 SEQRES 1 200 LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY ASN 1CUS 65 SEQRES 2 200 SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA ARG 1CUS 66 SEQRES 3 200 GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY PRO 1CUS 67 SEQRES 4 200 SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS ASP 1CUS 68 SEQRES 5 200 GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG ALA 1CUS 69 SEQRES 6 200 THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER SER 1CUS 70 SEQRES 7 200 ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN ALA 1CUS 71 SEQRES 8 200 ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY GLY 1CUS 72 SEQRES 9 200 TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE GLU 1CUS 73 SEQRES 10 200 ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY THR 1CUS 74 SEQRES 11 200 VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG GLY 1CUS 75 SEQRES 12 200 ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL PHE 1CUS 76 SEQRES 13 200 CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU ILE 1CUS 77 SEQRES 14 200 VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA ARG 1CUS 78 SEQRES 15 200 GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG ALA 1CUS 79 SEQRES 16 200 VAL ARG GLY SER ALA 1CUS 80 FORMUL 2 HOH *216(H2 O1) 1CUS 81 HELIX 1 A LEU 51 PHE 63 1 1CUS 82 HELIX 2 B SER 91 LYS 108 1 1CUS 83 HELIX 3 C SER 120 LEU 133 1 1CUS 84 HELIX 4 D LYS 151 GLY 157 1 1CUS 85 HELIX 5 E TYR 191 ALA 209 1 1CUS 86 SHEET 1 A 5 VAL 34 GLY 41 0 1CUS 87 SHEET 2 A 5 VAL 68 GLY 72 1 1CUS 88 SHEET 3 A 5 ALA 112 TYR 119 1 1CUS 89 SHEET 4 A 5 GLY 143 PHE 147 1 1CUS 90 SHEET 5 A 5 THR 167 CYS 171 1 1CUS 91 SHEET 1 B 1 ILE 183 ALA 185 0 1CUS 92 TURN 1 T1 GLY 64 GLY 67 1CUS 93 TURN 2 T2 GLY 74 TYR 77 1CUS 94 TURN 3 T3 LEU 86 GLY 89 1CUS 95 TURN 4 T4 CYS 109 ALA 112 1CUS 96 TURN 5 T5 TYR 119 GLY 122 1CUS 97 TURN 6 T6 ASP 134 ILE 137 1CUS 98 TURN 7 T7 ARG 138 ILE 141 1CUS 99 TURN 8 T8 TYR 149 ASN 152 1CUS 100 TURN 9 T9 LEU 153 ARG 156 1CUS 101 TURN 10 T10 ILE 159 TYR 162 1CUS 102 TURN 11 T11 PRO 163 ARG 166 1CUS 103 TURN 12 T12 ASN 172 ASP 175 1CUS 104 TURN 13 T13 ASP 175 CYS 178 1CUS 105 TURN 14 T14 ALA 185 HIS 188 1CUS 106 TURN 15 T15 PRO 187 ALA 190 1CUS 107 SSBOND 1 CYS 31 CYS 109 1CUS 108 SSBOND 2 CYS 171 CYS 178 1CUS 109 SITE 1 CAT 3 SER 120 ASP 175 HIS 188 1CUS 110 CRYST1 35.120 67.300 37.050 90.00 93.90 90.00 P 21 2 1CUS 111 ORIGX1 1.000000 0.000000 0.000000 0.00000 1CUS 112 ORIGX2 0.000000 1.000000 0.000000 0.00000 1CUS 113 ORIGX3 0.000000 0.000000 1.000000 0.00000 1CUS 114 SCALE1 0.028474 0.000000 0.001941 0.00000 1CUS 115 SCALE2 0.000000 0.014859 0.000000 0.00000 1CUS 116 SCALE3 0.000000 0.000000 0.027053 0.00000 1CUS 117