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HEADER HYDROLASE (SERINE ESTERASE) 07-OCT-95 1FFB 1FFB 2
COMPND MOL_ID: 1; 1FFB 3
COMPND 2 MOLECULE: CUTINASE; 1FFB 4
COMPND 3 CHAIN: NULL; 1FFB 5
COMPND 4 EC: 3.1.1.3; 1FFB 6
COMPND 5 ENGINEERED: YES; 1FFB 7
COMPND 6 MUTATION: N84D 1FFB 8
SOURCE MOL_ID: 1; 1FFB 9
SOURCE 2 SYNTHETIC: YES; 1FFB 10
SOURCE 3 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI PISI; 1FFB 11
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: SACCHAROMYCES CEREVISIAE PUC 19; 1FFB 12
SOURCE 5 OTHER_DETAILS: ESCHERICHIA COLI CLONING SYSTEM 1FFB 13
EXPDTA X-RAY DIFFRACTION 1FFB 14
AUTHOR C.CAMBILLAU,C.MARTINEZ,A.NICOLAS 1FFB 15
REVDAT 1 08-MAR-96 1FFB 0 1FFB 16
JRNL AUTH A.NICOLAS,M.EGMOND,C.T.VERRIPS,J.DE VLIEG,S.LONGHI, 1FFB 17
JRNL AUTH 2 C.CAMBILLAU,C.MARTINEZ 1FFB 18
JRNL TITL CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO 1FFB 19
JRNL TITL 2 THE STABILIZATION OF THE OXYANION TRANSITION STATE 1FFB 20
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1FFB 21
JRNL REFN 0353 1FFB 22
REMARK 1 1FFB 23
REMARK 1 REFERENCE 1 1FFB 24
REMARK 1 AUTH C.MARTINEZ,A.NICOLAS,H.VAN TILBEURGH,M.-P.EGLOFF, 1FFB 25
REMARK 1 AUTH 2 C.CUDREY,R.VERGER,C.CAMBILLAU 1FFB 26
REMARK 1 TITL CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED 1FFB 27
REMARK 1 TITL 2 OXYANION HOLE 1FFB 28
REMARK 1 REF BIOCHEMISTRY V. 33 83 1994 1FFB 29
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1FFB 30
REMARK 1 REFERENCE 2 1FFB 31
REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,M.LAUWEREYS,G.MATTHYSSENS, 1FFB 32
REMARK 1 AUTH 2 C.CAMBILLAU 1FFB 33
REMARK 1 TITL FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME 1FFB 34
REMARK 1 TITL 2 WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT 1FFB 35
REMARK 1 REF NATURE V. 356 615 1992 1FFB 36
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1FFB 37
REMARK 2 1FFB 38
REMARK 2 RESOLUTION. 1.75 ANGSTROMS. 1FFB 39
REMARK 3 1FFB 40
REMARK 3 REFINEMENT. 1FFB 41
REMARK 3 PROGRAM X-PLOR 1FFB 42
REMARK 3 AUTHORS BRUNGER 1FFB 43
REMARK 3 R VALUE 0.147 1FFB 44
REMARK 3 MEAN B VALUE 37.1 ANGSTROMS**2 1FFB 45
REMARK 3 RMSD BOND DISTANCES 0.008 ANGSTROMS 1FFB 46
REMARK 3 RMSD BOND ANGLES 1.46 DEGREES 1FFB 47
REMARK 3 1FFB 48
REMARK 3 NUMBER OF REFLECTIONS 14687 1FFB 49
REMARK 3 RESOLUTION RANGE 6.0 - 1.75 ANGSTROMS 1FFB 50
REMARK 3 DATA CUTOFF 1. SIGMA(F) 1FFB 51
REMARK 3 1FFB 52
REMARK 3 DATA COLLECTION. 1FFB 53
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 15053 1FFB 54
REMARK 3 COMPLETENESS OF DATA 93.3 % 1FFB 55
REMARK 3 REJECTION CRITERIA 1. SIGMA(I) 1FFB 56
REMARK 3 1FFB 57
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1FFB 58
REMARK 3 NUMBER OF PROTEIN ATOMS 1776 1FFB 59
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1FFB 60
REMARK 3 NUMBER OF HETEROGEN ATOMS 0 1FFB 61
REMARK 3 NUMBER OF SOLVENT ATOMS 230 1FFB 62
REMARK 3 1FFB 63
REMARK 3 STANDARD X-PLOR PARAMETERS 1FFB 64
REMARK 18 1FFB 65
REMARK 18 EXPERIMENTAL DETAILS. 1FFB 66
REMARK 18 DATE OF DATA COLLECTION : 13-OCT-93 1FFB 67
REMARK 18 MONOCHROMATIC (Y/N) : Y 1FFB 68
REMARK 18 LAUE (Y/N) : N 1FFB 69
REMARK 18 WAVELENGTH OR RANGE (A) : 1.5418 1FFB 70
REMARK 18 DETECTOR TYPE : 18CM IMAGE PLATE 1FFB 71
REMARK 18 DETECTOR MANUFACTURER : MARRESEARCH 1FFB 72
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : 3.2 KW / XDS (IP VERSION) 1FFB 73
REMARK 18 DATA REDUNDANCY : 3.4 1FFB 74
REMARK 18 MERGING R VALUE (INTENSITY) : 0.045 1FFB 75
REMARK 19 1FFB 76
REMARK 19 SOLVENT CONTENT (VS) : 32. % 1FFB 77
REMARK 999 1FFB 78
REMARK 999 FOR CHAIN " " - 16 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1FFB 79
REMARK 999 1FFB 80
REMARK 999 FOR CHAIN " " - 1 C-TERMINAL RESIDUES NOT IN ATOMS LIST 1FFB 81
DBREF 1FFB 17 213 SWS P00590 CUTI_FUSSO 33 229 1FFB 82
SEQADV 1FFB ASP 84 SWS P00590 ASN 100 ENGINEERED 1FFB 83
SEQRES 1 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG 1FFB 84
SEQRES 2 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY 1FFB 85
SEQRES 3 214 ASN SER ALA SER CYS ARG ASP VAL ILE PHE ILE TYR ALA 1FFB 86
SEQRES 4 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY 1FFB 87
SEQRES 5 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS 1FFB 88
SEQRES 6 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG 1FFB 89
SEQRES 7 214 ALA THR LEU GLY ASP ASP ALA LEU PRO ARG GLY THR SER 1FFB 90
SEQRES 8 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN 1FFB 91
SEQRES 9 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY 1FFB 92
SEQRES 10 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE 1FFB 93
SEQRES 11 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY 1FFB 94
SEQRES 12 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG 1FFB 95
SEQRES 13 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL 1FFB 96
SEQRES 14 214 PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU 1FFB 97
SEQRES 15 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA 1FFB 98
SEQRES 16 214 ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG 1FFB 99
SEQRES 17 214 ALA VAL ARG GLY SER ALA 1FFB 100
FORMUL 2 HOH *230(H2 O1) 1FFB 101
HELIX 1 1 ASP 22 ASN 25 1 1FFB 102
HELIX 2 2 SER 28 SER 30 5 1FFB 103
HELIX 3 3 GLY 52 PHE 63 1 1FFB 104
HELIX 4 4 ASP 83 ALA 85 5 1FFB 105
HELIX 5 5 SER 92 LYS 108 1 1FFB 106
HELIX 6 6 SER 120 ASP 132 5 1FFB 107
HELIX 7 7 SER 135 LYS 140 1 1FFB 108
HELIX 8 8 ALA 164 ARG 166 5 1FFB 109
HELIX 9 9 LEU 176 THR 179 5 1FFB 110
HELIX 10 10 ALA 186 LEU 189 5 1FFB 111
HELIX 11 11 GLY 192 ARG 196 1 1FFB 112
HELIX 12 12 PRO 198 VAL 210 1 1FFB 113
SHEET 1 A 5 VAL 68 GLY 72 0 1FFB 114
SHEET 2 A 5 VAL 34 ALA 39 1 N VAL 34 O TRP 69 1FFB 115
SHEET 3 A 5 THR 113 TYR 119 1 N THR 113 O ILE 35 1FFB 116
SHEET 4 A 5 ILE 141 PHE 147 1 N ALA 142 O LEU 114 1FFB 117
SHEET 5 A 5 THR 167 PHE 170 1 N LYS 168 O THR 144 1FFB 118
SSBOND 1 CYS 31 CYS 109 1FFB 119
SSBOND 2 CYS 171 CYS 178 1FFB 120
SITE 1 CAT 3 SER 120 HIS 188 ASP 175 1FFB 121
CRYST1 36.950 64.230 37.110 90.00 116.12 90.00 P 21 2 1FFB 122
ORIGX1 1.000000 0.000000 0.000000 0.00000 1FFB 123
ORIGX2 0.000000 1.000000 0.000000 0.00000 1FFB 124
ORIGX3 0.000000 0.000000 1.000000 0.00000 1FFB 125
SCALE1 0.027064 0.000000 0.013270 0.00000 1FFB 126
SCALE2 0.000000 0.015569 0.000000 0.00000 1FFB 127
SCALE3 0.000000 0.000000 0.030012 0.00000 1FFB 128 |