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HEADER HYDROLASE (SERINE ESTERASE) 07-OCT-95 1FFC 1FFC 2
COMPND MOL_ID: 1; 1FFC 3
COMPND 2 MOLECULE: CUTINASE; 1FFC 4
COMPND 3 CHAIN: NULL; 1FFC 5
COMPND 4 EC: 3.1.1.3; 1FFC 6
COMPND 5 ENGINEERED: YES; 1FFC 7
COMPND 6 MUTATION: N84L 1FFC 8
SOURCE MOL_ID: 1; 1FFC 9
SOURCE 2 SYNTHETIC: YES; 1FFC 10
SOURCE 3 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI PISI; 1FFC 11
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: SACCHAROMYCES CEREVISIAE PUC 19; 1FFC 12
SOURCE 5 OTHER_DETAILS: ESCHERICHIA COLI CLONING SYSTEM 1FFC 13
EXPDTA X-RAY DIFFRACTION 1FFC 14
AUTHOR C.CAMBILLAU,C.MARTINEZ,A.NICOLAS 1FFC 15
REVDAT 1 08-MAR-96 1FFC 0 1FFC 16
JRNL AUTH A.NICOLAS,M.EGMOND,C.T.VERRIPS,J.DE VLIEG,S.LONGHI, 1FFC 17
JRNL AUTH 2 C.CAMBILLAU,C.MARTINEZ 1FFC 18
JRNL TITL CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO 1FFC 19
JRNL TITL 2 THE STABILIZATION OF THE OXYANION TRANSITION STATE 1FFC 20
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1FFC 21
JRNL REFN 0353 1FFC 22
REMARK 1 1FFC 23
REMARK 1 REFERENCE 1 1FFC 24
REMARK 1 AUTH C.MARTINEZ,A.NICOLAS,H.VAN TILBEURGH,M.-P.EGLOFF, 1FFC 25
REMARK 1 AUTH 2 C.CUDREY,R.VERGER,C.CAMBILLAU 1FFC 26
REMARK 1 TITL CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED 1FFC 27
REMARK 1 TITL 2 OXYANION HOLE 1FFC 28
REMARK 1 REF BIOCHEMISTRY V. 33 83 1994 1FFC 29
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1FFC 30
REMARK 1 REFERENCE 2 1FFC 31
REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,M.LAUWEREYS,G.MATTHYSSENS, 1FFC 32
REMARK 1 AUTH 2 C.CAMBILLAU 1FFC 33
REMARK 1 TITL FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME 1FFC 34
REMARK 1 TITL 2 WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT 1FFC 35
REMARK 1 REF NATURE V. 356 615 1992 1FFC 36
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1FFC 37
REMARK 2 1FFC 38
REMARK 2 RESOLUTION. 1.75 ANGSTROMS. 1FFC 39
REMARK 3 1FFC 40
REMARK 3 REFINEMENT. 1FFC 41
REMARK 3 PROGRAM X-PLOR 1FFC 42
REMARK 3 AUTHORS BRUNGER 1FFC 43
REMARK 3 R VALUE 0.140 1FFC 44
REMARK 3 MEAN B VALUE 39.4 ANGSTROMS**2 1FFC 45
REMARK 3 RMSD BOND DISTANCES 0.009 ANGSTROMS 1FFC 46
REMARK 3 RMSD BOND ANGLES 1.40 DEGREES 1FFC 47
REMARK 3 1FFC 48
REMARK 3 NUMBER OF REFLECTIONS 15276 1FFC 49
REMARK 3 RESOLUTION RANGE 6.0 - 1.75 ANGSTROMS 1FFC 50
REMARK 3 DATA CUTOFF 1. SIGMA(F) 1FFC 51
REMARK 3 1FFC 52
REMARK 3 DATA COLLECTION. 1FFC 53
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 15547 1FFC 54
REMARK 3 COMPLETENESS OF DATA 89.3 % 1FFC 55
REMARK 3 REJECTION CRITERIA 1. SIGMA(I) 1FFC 56
REMARK 3 1FFC 57
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1FFC 58
REMARK 3 NUMBER OF PROTEIN ATOMS 1776 1FFC 59
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1FFC 60
REMARK 3 NUMBER OF HETEROGEN ATOMS 0 1FFC 61
REMARK 3 NUMBER OF SOLVENT ATOMS 325 1FFC 62
REMARK 3 1FFC 63
REMARK 3 STANDARD X-PLOR PARAMETERS 1FFC 64
REMARK 4 1FFC 65
REMARK 4 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED 1FFC 66
REMARK 4 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE 1FFC 67
REMARK 4 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL 1FFC 68
REMARK 4 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE 1FFC 69
REMARK 4 NUMBER; I=INSERTION CODE): 1FFC 70
REMARK 4 1FFC 71
REMARK 4 M RES CSSEQI 1FFC 72
REMARK 4 0 HOH 809 DISTANCE = 5.89 ANGSTROMS 1FFC 73
REMARK 18 1FFC 74
REMARK 18 EXPERIMENTAL DETAILS. 1FFC 75
REMARK 18 DATE OF DATA COLLECTION : 27-JAN-94 1FFC 76
REMARK 18 MONOCHROMATIC (Y/N) : Y 1FFC 77
REMARK 18 LAUE (Y/N) : N 1FFC 78
REMARK 18 WAVELENGTH OR RANGE (A) : 1.5418 1FFC 79
REMARK 18 DETECTOR TYPE : 18CM IMAGE PLATE 1FFC 80
REMARK 18 DETECTOR MANUFACTURER : MARRESEARCH 1FFC 81
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : 3.2 KW / XDS (IP VERSION) 1FFC 82
REMARK 18 DATA REDUNDANCY : 3.6 1FFC 83
REMARK 18 MERGING R VALUE (INTENSITY) : 0.042 1FFC 84
REMARK 19 1FFC 85
REMARK 19 SOLVENT CONTENT (VS) : 38. % 1FFC 86
REMARK 999 1FFC 87
REMARK 999 FOR CHAIN " " - 16 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1FFC 88
REMARK 999 1FFC 89
REMARK 999 FOR CHAIN " " - 1 C-TERMINAL RESIDUES NOT IN ATOMS LIST 1FFC 90
DBREF 1FFC 17 213 SWS P00590 CUTI_FUSSO 33 229 1FFC 91
SEQADV 1FFC LEU 84 SWS P00590 ASN 100 ENGINEERED 1FFC 92
SEQRES 1 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG 1FFC 93
SEQRES 2 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY 1FFC 94
SEQRES 3 214 ASN SER ALA SER CYS ARG ASP VAL ILE PHE ILE TYR ALA 1FFC 95
SEQRES 4 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY 1FFC 96
SEQRES 5 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS 1FFC 97
SEQRES 6 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG 1FFC 98
SEQRES 7 214 ALA THR LEU GLY ASP LEU ALA LEU PRO ARG GLY THR SER 1FFC 99
SEQRES 8 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN 1FFC 100
SEQRES 9 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY 1FFC 101
SEQRES 10 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE 1FFC 102
SEQRES 11 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY 1FFC 103
SEQRES 12 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG 1FFC 104
SEQRES 13 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL 1FFC 105
SEQRES 14 214 PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU 1FFC 106
SEQRES 15 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA 1FFC 107
SEQRES 16 214 ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG 1FFC 108
SEQRES 17 214 ALA VAL ARG GLY SER ALA 1FFC 109
FORMUL 2 HOH *325(H2 O1) 1FFC 110
HELIX 1 1 ASP 22 ASN 25 1 1FFC 111
HELIX 2 2 SER 28 SER 30 5 1FFC 112
HELIX 3 3 GLY 49 PHE 63 1 1FFC 113
HELIX 4 4 LEU 81 ALA 85 5 1FFC 114
HELIX 5 5 SER 92 LYS 108 1 1FFC 115
HELIX 6 6 SER 120 ASP 132 5 1FFC 116
HELIX 7 7 SER 135 LYS 140 1 1FFC 117
HELIX 8 8 ALA 164 ARG 166 5 1FFC 118
HELIX 9 9 LEU 176 THR 179 5 1FFC 119
HELIX 10 10 ALA 186 LEU 189 5 1FFC 120
HELIX 11 11 GLY 192 ARG 196 1 1FFC 121
HELIX 12 12 PRO 198 ARG 211 1 1FFC 122
SHEET 1 A 5 VAL 68 GLY 72 0 1FFC 123
SHEET 2 A 5 VAL 34 ALA 39 1 N VAL 34 O TRP 69 1FFC 124
SHEET 3 A 5 THR 113 TYR 119 1 N THR 113 O ILE 35 1FFC 125
SHEET 4 A 5 ILE 141 PHE 147 1 N ALA 142 O LEU 114 1FFC 126
SHEET 5 A 5 THR 167 PHE 170 1 N LYS 168 O THR 144 1FFC 127
SSBOND 1 CYS 31 CYS 109 1FFC 128
SSBOND 2 CYS 171 CYS 178 1FFC 129
SITE 1 CAT 3 SER 120 HIS 188 ASP 175 1FFC 130
CRYST1 35.120 67.360 37.050 90.00 93.90 90.00 P 21 2 1FFC 131
ORIGX1 1.000000 0.000000 0.000000 0.00000 1FFC 132
ORIGX2 0.000000 1.000000 0.000000 0.00000 1FFC 133
ORIGX3 0.000000 0.000000 1.000000 0.00000 1FFC 134
SCALE1 0.028474 0.000000 0.001941 0.00000 1FFC 135
SCALE2 0.000000 0.014846 0.000000 0.00000 1FFC 136
SCALE3 0.000000 0.000000 0.027053 0.00000 1FFC 137 |