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HEADER HYDROLASE (SERINE ESTERASE) 07-OCT-95 1FFA 1FFA 2
COMPND MOL_ID: 1; 1FFA 3
COMPND 2 MOLECULE: CUTINASE; 1FFA 4
COMPND 3 CHAIN: NULL; 1FFA 5
COMPND 4 EC: 3.1.1.3; 1FFA 6
COMPND 5 ENGINEERED: YES; 1FFA 7
COMPND 6 MUTATION: N84A 1FFA 8
SOURCE MOL_ID: 1; 1FFA 9
SOURCE 2 SYNTHETIC: YES; 1FFA 10
SOURCE 3 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI PISI; 1FFA 11
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: SACCHAROMYCES CEREVISIAE PUC 19; 1FFA 12
SOURCE 5 OTHER_DETAILS: ESCHERICHIA COLI CLONING SYSTEM 1FFA 13
EXPDTA X-RAY DIFFRACTION 1FFA 14
AUTHOR C.CAMBILLAU,C.MARTINEZ,A.NICOLAS 1FFA 15
REVDAT 1 08-MAR-96 1FFA 0 1FFA 16
JRNL AUTH A.NICOLAS,M.EGMOND,C.T.VERRIPS,J.DE VLIEG,S.LONGHI, 1FFA 17
JRNL AUTH 2 C.CAMBILLAU,C.MARTINEZ 1FFA 18
JRNL TITL CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO 1FFA 19
JRNL TITL 2 THE STABILIZATION OF THE OXYANION TRANSITION STATE 1FFA 20
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1FFA 21
JRNL REFN 0353 1FFA 22
REMARK 1 1FFA 23
REMARK 1 REFERENCE 1 1FFA 24
REMARK 1 AUTH C.MARTINEZ,A.NICOLAS,H.VAN TILBEURGH,M.-P.EGLOFF, 1FFA 25
REMARK 1 AUTH 2 C.CUDREY,R.VERGER,C.CAMBILLAU 1FFA 26
REMARK 1 TITL CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED 1FFA 27
REMARK 1 TITL 2 OXYANION HOLE 1FFA 28
REMARK 1 REF BIOCHEMISTRY V. 33 83 1994 1FFA 29
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1FFA 30
REMARK 1 REFERENCE 2 1FFA 31
REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,M.LAUWEREYS,G.MATTHYSSENS, 1FFA 32
REMARK 1 AUTH 2 C.CAMBILLAU 1FFA 33
REMARK 1 TITL FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME 1FFA 34
REMARK 1 TITL 2 WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT 1FFA 35
REMARK 1 REF NATURE V. 356 615 1992 1FFA 36
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1FFA 37
REMARK 2 1FFA 38
REMARK 2 RESOLUTION. 1.69 ANGSTROMS. 1FFA 39
REMARK 3 1FFA 40
REMARK 3 REFINEMENT. 1FFA 41
REMARK 3 PROGRAM X-PLOR 1FFA 42
REMARK 3 AUTHORS BRUNGER 1FFA 43
REMARK 3 R VALUE 0.137 1FFA 44
REMARK 3 MEAN B VALUE 38.4 ANGSTROMS**2 1FFA 45
REMARK 3 RMSD BOND DISTANCES 0.009 ANGSTROMS 1FFA 46
REMARK 3 RMSD BOND ANGLES 1.43 DEGREES 1FFA 47
REMARK 3 1FFA 48
REMARK 3 NUMBER OF REFLECTIONS 17888 1FFA 49
REMARK 3 RESOLUTION RANGE 6.0 - 1.69 ANGSTROMS 1FFA 50
REMARK 3 DATA CUTOFF 1. SIGMA(F) 1FFA 51
REMARK 3 1FFA 52
REMARK 3 DATA COLLECTION. 1FFA 53
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 18092 1FFA 54
REMARK 3 COMPLETENESS OF DATA 95.3 % 1FFA 55
REMARK 3 REJECTION CRITERIA 1. SIGMA(I) 1FFA 56
REMARK 3 1FFA 57
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1FFA 58
REMARK 3 NUMBER OF PROTEIN ATOMS 1773 1FFA 59
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1FFA 60
REMARK 3 NUMBER OF HETEROGEN ATOMS 0 1FFA 61
REMARK 3 NUMBER OF SOLVENT ATOMS 309 1FFA 62
REMARK 3 1FFA 63
REMARK 3 STANDARD X-PLOR PARAMETERS 1FFA 64
REMARK 4 1FFA 65
REMARK 4 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED 1FFA 66
REMARK 4 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE 1FFA 67
REMARK 4 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL 1FFA 68
REMARK 4 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE 1FFA 69
REMARK 4 NUMBER; I=INSERTION CODE): 1FFA 70
REMARK 4 1FFA 71
REMARK 4 M RES CSSEQI 1FFA 72
REMARK 4 0 HOH 914 DISTANCE = 6.08 ANGSTROMS 1FFA 73
REMARK 18 1FFA 74
REMARK 18 EXPERIMENTAL DETAILS. 1FFA 75
REMARK 18 DATE OF DATA COLLECTION : 15-JAN-94 1FFA 76
REMARK 18 MONOCHROMATIC (Y/N) : Y 1FFA 77
REMARK 18 LAUE (Y/N) : N 1FFA 78
REMARK 18 WAVELENGTH OR RANGE (A) : 1.5418 1FFA 79
REMARK 18 DETECTOR TYPE : 18CM IMAGE PLATE 1FFA 80
REMARK 18 DETECTOR MANUFACTURER : MARRESEARCH 1FFA 81
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : 3.2 KW / XDS (IP VERSION) 1FFA 82
REMARK 18 DATA REDUNDANCY : 3.3 1FFA 83
REMARK 18 MERGING R VALUE (INTENSITY) : 0.029 1FFA 84
REMARK 19 1FFA 85
REMARK 19 SOLVENT CONTENT (VS) : 38. % 1FFA 86
REMARK 999 1FFA 87
REMARK 999 FOR CHAIN " " - 16 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1FFA 88
REMARK 999 1FFA 89
REMARK 999 FOR CHAIN " " - 1 C-TERMINAL RESIDUES NOT IN ATOMS LIST 1FFA 90
DBREF 1FFA 17 213 SWS P00590 CUTI_FUSSO 33 229 1FFA 91
SEQADV 1FFA ALA 84 SWS P00590 ASN 100 ENGINEERED 1FFA 92
SEQRES 1 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG 1FFA 93
SEQRES 2 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY 1FFA 94
SEQRES 3 214 ASN SER ALA SER CYS ARG ASP VAL ILE PHE ILE TYR ALA 1FFA 95
SEQRES 4 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY 1FFA 96
SEQRES 5 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS 1FFA 97
SEQRES 6 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG 1FFA 98
SEQRES 7 214 ALA THR LEU GLY ASP ALA ALA LEU PRO ARG GLY THR SER 1FFA 99
SEQRES 8 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN 1FFA 100
SEQRES 9 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY 1FFA 101
SEQRES 10 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE 1FFA 102
SEQRES 11 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY 1FFA 103
SEQRES 12 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG 1FFA 104
SEQRES 13 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL 1FFA 105
SEQRES 14 214 PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU 1FFA 106
SEQRES 15 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA 1FFA 107
SEQRES 16 214 ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG 1FFA 108
SEQRES 17 214 ALA VAL ARG GLY SER ALA 1FFA 109
FORMUL 2 HOH *310(H2 O1) 1FFA 110
HELIX 1 1 ASP 22 ASN 25 1 1FFA 111
HELIX 2 2 SER 28 SER 30 5 1FFA 112
HELIX 3 3 GLY 49 PHE 63 1 1FFA 113
HELIX 4 4 LEU 81 ALA 85 5 1FFA 114
HELIX 5 5 SER 92 LYS 108 1 1FFA 115
HELIX 6 6 SER 120 ASP 132 5 1FFA 116
HELIX 7 7 SER 135 LYS 140 1 1FFA 117
HELIX 8 8 ALA 164 ARG 166 5 1FFA 118
HELIX 9 9 LEU 176 THR 179 5 1FFA 119
HELIX 10 10 ALA 186 LEU 189 5 1FFA 120
HELIX 11 11 GLY 192 ARG 196 1 1FFA 121
HELIX 12 12 PRO 198 ARG 211 1 1FFA 122
SHEET 1 A 5 VAL 68 GLY 72 0 1FFA 123
SHEET 2 A 5 VAL 34 ALA 39 1 N VAL 34 O TRP 69 1FFA 124
SHEET 3 A 5 THR 113 TYR 119 1 N THR 113 O ILE 35 1FFA 125
SHEET 4 A 5 ILE 141 PHE 147 1 N ALA 142 O LEU 114 1FFA 126
SHEET 5 A 5 THR 167 PHE 170 1 N LYS 168 O THR 144 1FFA 127
SSBOND 1 CYS 31 CYS 109 1FFA 128
SSBOND 2 CYS 171 CYS 178 1FFA 129
SITE 1 CAT 3 SER 120 HIS 188 ASP 175 1FFA 130
CRYST1 35.120 67.360 37.050 90.00 93.90 90.00 P 21 2 1FFA 131
ORIGX1 1.000000 0.000000 0.000000 0.00000 1FFA 132
ORIGX2 0.000000 1.000000 0.000000 0.00000 1FFA 133
ORIGX3 0.000000 0.000000 1.000000 0.00000 1FFA 134
SCALE1 0.028474 0.000000 0.001941 0.00000 1FFA 135
SCALE2 0.000000 0.014846 0.000000 0.00000 1FFA 136
SCALE3 0.000000 0.000000 0.027053 0.00000 1FFA 137 |