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HEADER COMPLEX(SERINE ESTERASE/INHIBITOR) 03-JUN-94 2CUT 2CUT 2
COMPND CUTINASE (E.C.3.1.1.-) COMPLEXED WITH THE INHIBITOR DIETHYL 2CUT 3
COMPND 2 PARA-NITROPHENYL PHOSPHATE 2CUT 4
SOURCE FUNGUS (FUSARIUM SOLANI, SUBSP. PISI) RECOMBINANT FORM 2CUT 5
SOURCE 2 EXPRESSED IN (ESCHERICHIA COLI) 2CUT 6
AUTHOR C.MARTINEZ,C.CAMBILLAU 2CUT 7
REVDAT 1 31-AUG-94 2CUT 0 2CUT 8
JRNL AUTH C.MARTINEZ,A.NICOLAS,H.VAN TILBEURGH,M.-P.EGLOFF, 2CUT 9
JRNL AUTH 2 C.CUDREY,R.VERGER,C.CAMBILLAU 2CUT 10
JRNL TITL CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED 2CUT 11
JRNL TITL 2 OXYANION HOLE 2CUT 12
JRNL REF BIOCHEMISTRY V. 33 83 1994 2CUT 13
JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033 2CUT 14
REMARK 1 2CUT 15
REMARK 2 2CUT 16
REMARK 2 RESOLUTION. 1.9 ANGSTROMS. 2CUT 17
REMARK 3 2CUT 18
REMARK 3 REFINEMENT. 2CUT 19
REMARK 3 PROGRAM X-PLOR 2CUT 20
REMARK 3 AUTHORS BRUNGER 2CUT 21
REMARK 3 R VALUE 0.181 2CUT 22
REMARK 3 RMSD BOND DISTANCES 0.012 ANGSTROMS 2CUT 23
REMARK 3 RMSD BOND ANGLES 2.9 DEGREES 2CUT 24
REMARK 3 2CUT 25
REMARK 3 NUMBER OF REFLECTIONS 12970 2CUT 26
REMARK 3 RESOLUTION RANGE 6.0 - 1.9 ANGSTROMS 2CUT 27
REMARK 3 DATA CUTOFF 1.0 SIGMA(F) 2CUT 28
REMARK 3 PERCENT COMPLETION 87.6 2CUT 29
REMARK 3 2CUT 30
REMARK 3 NUMBER OF PROTEIN ATOMS 1446 2CUT 31
REMARK 3 NUMBER OF SOLVENT ATOMS 119 2CUT 32
REMARK 4 2CUT 33
REMARK 4 SITE *CAT* PRESENTED BELOW REFERS TO THE CATALYTIC TRIAD. 2CUT 34
REMARK 5 2CUT 35
REMARK 5 IN THE CRYSTAL STRUCTURE THE DIETHYL PARA-NITROPHENYL 2CUT 36
REMARK 5 PHOSPHATE INHIBITOR REACTS WITH SER 120 TO PRODUCE A 2CUT 37
REMARK 5 COVALENT ADDUCT WITH THE LEAVING OF THE PARA-NITROPHENYL 2CUT 38
REMARK 5 GROUP. 2CUT 39
REMARK 6 2CUT 40
REMARK 6 CROSS REFERENCE TO SEQUENCE DATABASE 2CUT 41
REMARK 6 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 2CUT 42
REMARK 6 CUTI_FUSSO 2CUT 43
REMARK 6 2CUT 44
REMARK 6 SEQUENCE ADVISORY NOTICE 2CUT 45
REMARK 6 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 2CUT 46
REMARK 6 2CUT 47
REMARK 6 SWISS-PROT ENTRY NAME: CUTI_FUSSO 2CUT 48
REMARK 6 2CUT 49
REMARK 6 SWISS-PROT RESIDUE PDB SEQRES 2CUT 50
REMARK 6 2CUT 51
REMARK 6 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 2CUT 52
REMARK 6 ARG 48 ALA 32 2CUT 53
SEQRES 1 198 LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY ASN 2CUT 54
SEQRES 2 198 SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA ARG 2CUT 55
SEQRES 3 198 GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY PRO 2CUT 56
SEQRES 4 198 SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS ASP 2CUT 57
SEQRES 5 198 GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG ALA 2CUT 58
SEQRES 6 198 THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER SER 2CUT 59
SEQRES 7 198 ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN ALA 2CUT 60
SEQRES 8 198 ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY GLY 2CUT 61
SEQRES 9 198 TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE GLU 2CUT 62
SEQRES 10 198 ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY THR 2CUT 63
SEQRES 11 198 VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG GLY 2CUT 64
SEQRES 12 198 ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL PHE 2CUT 65
SEQRES 13 198 CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU ILE 2CUT 66
SEQRES 14 198 VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA ARG 2CUT 67
SEQRES 15 198 GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG ALA 2CUT 68
SEQRES 16 198 VAL ARG GLY 2CUT 69
HET DEP 401 8 DIETHYL PHOSPHONO GROUP 2CUT 70
FORMUL 2 DEP C4 H10 O3 P1 2CUT 71
FORMUL 3 HOH *119(H2 O1) 2CUT 72
HELIX 1 A LEU 51 PHE 63 1 2CUT 73
HELIX 2 B SER 91 LYS 108 1 2CUT 74
HELIX 3 C SER 120 LEU 133 1 2CUT 75
HELIX 4 D LYS 151 GLY 157 1 2CUT 76
HELIX 5 E TYR 191 ALA 209 1 2CUT 77
SHEET 1 A 5 VAL 34 GLY 41 0 2CUT 78
SHEET 2 A 5 VAL 68 GLY 72 1 2CUT 79
SHEET 3 A 5 ALA 112 TYR 119 1 2CUT 80
SHEET 4 A 5 GLY 143 PHE 147 1 2CUT 81
SHEET 5 A 5 THR 167 CYS 171 1 2CUT 82
SHEET 1 B 1 ILE 183 ALA 185 0 2CUT 83
TURN 1 T1 GLY 64 GLY 67 2CUT 84
TURN 2 T2 GLY 74 TYR 77 2CUT 85
TURN 3 T3 LEU 86 GLY 89 2CUT 86
TURN 4 T4 CYS 109 ALA 112 2CUT 87
TURN 5 T5 TYR 119 GLY 122 2CUT 88
TURN 6 T6 ASP 134 ILE 137 2CUT 89
TURN 7 T7 ARG 138 ILE 141 2CUT 90
TURN 8 T8 TYR 149 ASN 152 2CUT 91
TURN 9 T9 LEU 153 ARG 156 2CUT 92
TURN 10 T10 ILE 159 TYR 162 2CUT 93
TURN 11 T11 PRO 163 ARG 166 2CUT 94
TURN 12 T12 ASN 172 ASP 175 2CUT 95
TURN 13 T13 ASP 175 CYS 178 2CUT 96
TURN 14 T14 ALA 185 HIS 188 2CUT 97
TURN 15 T15 PRO 187 ALA 190 2CUT 98
SSBOND 1 CYS 31 CYS 109 2CUT 99
SSBOND 2 CYS 171 CYS 178 2CUT 100
SITE 1 CAT 3 SER 120 ASP 175 HIS 188 2CUT 101
CRYST1 40.300 61.100 72.700 90.00 90.00 90.00 P 21 21 21 4 2CUT 102
ORIGX1 1.000000 0.000000 0.000000 0.00000 2CUT 103
ORIGX2 0.000000 1.000000 0.000000 0.00000 2CUT 104
ORIGX3 0.000000 0.000000 1.000000 0.00000 2CUT 105
SCALE1 0.024814 0.000000 0.000000 0.00000 2CUT 106
SCALE2 0.000000 0.016367 0.000000 0.00000 2CUT 107
SCALE3 0.000000 0.000000 0.013755 0.00000 2CUT 108 |