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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 |