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HEADER HYDROLASE (SERINE ESTERASE) 07-OCT-95 1FFD 1FFD 2
COMPND MOL_ID: 1; 1FFD 3
COMPND 2 MOLECULE: CUTINASE; 1FFD 4
COMPND 3 CHAIN: NULL; 1FFD 5
COMPND 4 EC: 3.1.1.3; 1FFD 6
COMPND 5 ENGINEERED: YES; 1FFD 7
COMPND 6 MUTATION: N84W 1FFD 8
SOURCE MOL_ID: 1; 1FFD 9
SOURCE 2 SYNTHETIC: YES; 1FFD 10
SOURCE 3 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI PISI; 1FFD 11
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: SACCHAROMYCES CEREVISIAE PUC 19; 1FFD 12
SOURCE 5 OTHER_DETAILS: ESCHERICHIA COLI CLONING SYSTEM 1FFD 13
EXPDTA X-RAY DIFFRACTION 1FFD 14
AUTHOR C.CAMBILLAU,C.MARTINEZ,A.NICOLAS 1FFD 15
REVDAT 1 08-MAR-96 1FFD 0 1FFD 16
JRNL AUTH A.NICOLAS,M.EGMOND,C.T.VERRIPS,J.DE VLIEG,S.LONGHI, 1FFD 17
JRNL AUTH 2 C.CAMBILLAU,C.MARTINEZ 1FFD 18
JRNL TITL CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO 1FFD 19
JRNL TITL 2 THE STABILIZATION OF THE OXYANION TRANSITION STATE 1FFD 20
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1FFD 21
JRNL REFN 0353 1FFD 22
REMARK 1 1FFD 23
REMARK 1 REFERENCE 1 1FFD 24
REMARK 1 AUTH C.MARTINEZ,A.NICOLAS,H.VAN TILBEURGH,M.-P.EGLOFF, 1FFD 25
REMARK 1 AUTH 2 C.CUDREY,R.VERGER,C.CAMBILLAU 1FFD 26
REMARK 1 TITL CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED 1FFD 27
REMARK 1 TITL 2 OXYANION HOLE 1FFD 28
REMARK 1 REF BIOCHEMISTRY V. 33 83 1994 1FFD 29
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1FFD 30
REMARK 1 REFERENCE 2 1FFD 31
REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,M.LAUWEREYS,G.MATTHYSSENS, 1FFD 32
REMARK 1 AUTH 2 C.CAMBILLAU 1FFD 33
REMARK 1 TITL FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME 1FFD 34
REMARK 1 TITL 2 WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT 1FFD 35
REMARK 1 REF NATURE V. 356 615 1992 1FFD 36
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1FFD 37
REMARK 2 1FFD 38
REMARK 2 RESOLUTION. 1.69 ANGSTROMS. 1FFD 39
REMARK 3 1FFD 40
REMARK 3 REFINEMENT. 1FFD 41
REMARK 3 PROGRAM X-PLOR 1FFD 42
REMARK 3 AUTHORS BRUNGER 1FFD 43
REMARK 3 R VALUE 0.144 1FFD 44
REMARK 3 MEAN B VALUE 40.4 ANGSTROMS**2 1FFD 45
REMARK 3 RMSD BOND DISTANCES 0.01 ANGSTROMS 1FFD 46
REMARK 3 RMSD BOND ANGLES 1.47 DEGREES 1FFD 47
REMARK 3 1FFD 48
REMARK 3 NUMBER OF REFLECTIONS 16350 1FFD 49
REMARK 3 RESOLUTION RANGE 6.0 - 1.69 ANGSTROMS 1FFD 50
REMARK 3 DATA CUTOFF 1. SIGMA(F) 1FFD 51
REMARK 3 1FFD 52
REMARK 3 DATA COLLECTION. 1FFD 53
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 17226 1FFD 54
REMARK 3 COMPLETENESS OF DATA 92.9 % 1FFD 55
REMARK 3 REJECTION CRITERIA 1. SIGMA(I) 1FFD 56
REMARK 3 1FFD 57
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1FFD 58
REMARK 3 NUMBER OF PROTEIN ATOMS 1783 1FFD 59
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1FFD 60
REMARK 3 NUMBER OF HETEROGEN ATOMS 0 1FFD 61
REMARK 3 NUMBER OF SOLVENT ATOMS 283 1FFD 62
REMARK 3 1FFD 63
REMARK 3 STANDARD X-PLOR PARAMETERS 1FFD 64
REMARK 4 1FFD 65
REMARK 4 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED 1FFD 66
REMARK 4 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE 1FFD 67
REMARK 4 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL 1FFD 68
REMARK 4 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE 1FFD 69
REMARK 4 NUMBER; I=INSERTION CODE): 1FFD 70
REMARK 4 1FFD 71
REMARK 4 M RES CSSEQI 1FFD 72
REMARK 4 0 HOH 740 DISTANCE = 5.02 ANGSTROMS 1FFD 73
REMARK 4 0 HOH 810 DISTANCE = 5.85 ANGSTROMS 1FFD 74
REMARK 18 1FFD 75
REMARK 18 EXPERIMENTAL DETAILS. 1FFD 76
REMARK 18 DATE OF DATA COLLECTION : 16-NOV-92 1FFD 77
REMARK 18 MONOCHROMATIC (Y/N) : Y 1FFD 78
REMARK 18 LAUE (Y/N) : N 1FFD 79
REMARK 18 WAVELENGTH OR RANGE (A) : 1.5418 1FFD 80
REMARK 18 DETECTOR TYPE : 18CM IMAGE PLATE 1FFD 81
REMARK 18 DETECTOR MANUFACTURER : MARRESEARCH 1FFD 82
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : 3.2 KW / XDS (IP VERSION) 1FFD 83
REMARK 18 DATA REDUNDANCY : 2.3 1FFD 84
REMARK 18 MERGING R VALUE (INTENSITY) : 0.057 1FFD 85
REMARK 19 1FFD 86
REMARK 19 SOLVENT CONTENT (VS) : 38. % 1FFD 87
REMARK 999 1FFD 88
REMARK 999 FOR CHAIN " " - 16 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1FFD 89
REMARK 999 1FFD 90
REMARK 999 FOR CHAIN " " - 1 C-TERMINAL RESIDUES NOT IN ATOMS LIST 1FFD 91
DBREF 1FFD 17 213 SWS P00590 CUTI_FUSSO 33 229 1FFD 92
SEQADV 1FFD TRP 84 SWS P00590 ASN 100 ENGINEERED 1FFD 93
SEQRES 1 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG 1FFD 94
SEQRES 2 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY 1FFD 95
SEQRES 3 214 ASN SER ALA SER CYS ARG ASP VAL ILE PHE ILE TYR ALA 1FFD 96
SEQRES 4 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY 1FFD 97
SEQRES 5 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS 1FFD 98
SEQRES 6 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG 1FFD 99
SEQRES 7 214 ALA THR LEU GLY ASP TRP ALA LEU PRO ARG GLY THR SER 1FFD 100
SEQRES 8 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN 1FFD 101
SEQRES 9 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY 1FFD 102
SEQRES 10 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE 1FFD 103
SEQRES 11 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY 1FFD 104
SEQRES 12 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG 1FFD 105
SEQRES 13 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL 1FFD 106
SEQRES 14 214 PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU 1FFD 107
SEQRES 15 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA 1FFD 108
SEQRES 16 214 ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG 1FFD 109
SEQRES 17 214 ALA VAL ARG GLY SER ALA 1FFD 110
FORMUL 2 HOH *280(H2 O1) 1FFD 111
HELIX 1 1 ASP 22 ASN 25 1 1FFD 112
HELIX 2 2 SER 28 SER 30 5 1FFD 113
HELIX 3 3 GLY 49 PHE 63 1 1FFD 114
HELIX 4 4 LEU 81 ALA 85 5 1FFD 115
HELIX 5 5 SER 92 LYS 108 1 1FFD 116
HELIX 6 6 SER 120 ASP 132 5 1FFD 117
HELIX 7 7 SER 135 LYS 140 1 1FFD 118
HELIX 8 8 ALA 164 ARG 166 5 1FFD 119
HELIX 9 9 LEU 176 THR 179 5 1FFD 120
HELIX 10 10 ALA 186 LEU 189 5 1FFD 121
HELIX 11 11 GLY 192 ARG 196 1 1FFD 122
HELIX 12 12 PRO 198 ARG 211 1 1FFD 123
SHEET 1 A 5 VAL 68 GLY 72 0 1FFD 124
SHEET 2 A 5 VAL 34 ALA 39 1 N VAL 34 O TRP 69 1FFD 125
SHEET 3 A 5 THR 113 TYR 119 1 N THR 113 O ILE 35 1FFD 126
SHEET 4 A 5 THR 144 PHE 147 1 N VAL 145 O ALA 116 1FFD 127
SHEET 5 A 5 THR 167 PHE 170 1 N LYS 168 O THR 144 1FFD 128
SSBOND 1 CYS 31 CYS 109 1FFD 129
SSBOND 2 CYS 171 CYS 178 1FFD 130
SITE 1 CAT 3 SER 120 HIS 188 ASP 175 1FFD 131
CRYST1 35.120 67.360 37.050 90.00 93.90 90.00 P 21 2 1FFD 132
ORIGX1 1.000000 0.000000 0.000000 0.00000 1FFD 133
ORIGX2 0.000000 1.000000 0.000000 0.00000 1FFD 134
ORIGX3 0.000000 0.000000 1.000000 0.00000 1FFD 135
SCALE1 0.028474 0.000000 0.001941 0.00000 1FFD 136
SCALE2 0.000000 0.014846 0.000000 0.00000 1FFD 137
SCALE3 0.000000 0.000000 0.027053 0.00000 1FFD 138 |