| content |
HEADER HYDROLASE (SERINE ESTERASE) 07-OCT-95 1FFE 1FFE 2
COMPND MOL_ID: 1; 1FFE 3
COMPND 2 MOLECULE: CUTINASE; 1FFE 4
COMPND 3 CHAIN: NULL; 1FFE 5
COMPND 4 EC: 3.1.1.3; 1FFE 6
COMPND 5 ENGINEERED: YES; 1FFE 7
COMPND 6 MUTATION: S42A 1FFE 8
SOURCE MOL_ID: 1; 1FFE 9
SOURCE 2 SYNTHETIC: YES; 1FFE 10
SOURCE 3 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI PISI; 1FFE 11
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: SACCHAROMYCES CEREVISIAE PUC 19; 1FFE 12
SOURCE 5 OTHER_DETAILS: ESCHERICHIA COLI CLONING SYSTEM 1FFE 13
EXPDTA X-RAY DIFFRACTION 1FFE 14
AUTHOR C.CAMBILLAU,C.MARTINEZ,A.NICOLAS 1FFE 15
REVDAT 1 08-MAR-96 1FFE 0 1FFE 16
JRNL AUTH A.NICOLAS,M.EGMOND,C.T.VERRIPS,J.DE VLIEG,S.LONGHI, 1FFE 17
JRNL AUTH 2 C.CAMBILLAU,C.MARTINEZ 1FFE 18
JRNL TITL CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO 1FFE 19
JRNL TITL 2 THE STABILIZATION OF THE OXYANION TRANSITION STATE 1FFE 20
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1FFE 21
JRNL REFN 0353 1FFE 22
REMARK 1 1FFE 23
REMARK 1 REFERENCE 1 1FFE 24
REMARK 1 AUTH C.MARTINEZ,A.NICOLAS,H.VAN TILBEURGH,M.-P.EGLOFF, 1FFE 25
REMARK 1 AUTH 2 C.CUDREY,R.VERGER,C.CAMBILLAU 1FFE 26
REMARK 1 TITL CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED 1FFE 27
REMARK 1 TITL 2 OXYANION HOLE 1FFE 28
REMARK 1 REF BIOCHEMISTRY V. 33 83 1994 1FFE 29
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1FFE 30
REMARK 1 REFERENCE 2 1FFE 31
REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,M.LAUWEREYS,G.MATTHYSSENS, 1FFE 32
REMARK 1 AUTH 2 C.CAMBILLAU 1FFE 33
REMARK 1 TITL FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME 1FFE 34
REMARK 1 TITL 2 WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT 1FFE 35
REMARK 1 REF NATURE V. 356 615 1992 1FFE 36
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1FFE 37
REMARK 2 1FFE 38
REMARK 2 RESOLUTION. 1.69 ANGSTROMS. 1FFE 39
REMARK 3 1FFE 40
REMARK 3 REFINEMENT. 1FFE 41
REMARK 3 PROGRAM X-PLOR 1FFE 42
REMARK 3 AUTHORS BRUNGER 1FFE 43
REMARK 3 R VALUE 0.135 1FFE 44
REMARK 3 MEAN B VALUE 44.9 ANGSTROMS**2 1FFE 45
REMARK 3 RMSD BOND DISTANCES 0.008 ANGSTROMS 1FFE 46
REMARK 3 RMSD BOND ANGLES 1.40 DEGREES 1FFE 47
REMARK 3 1FFE 48
REMARK 3 NUMBER OF REFLECTIONS 16806 1FFE 49
REMARK 3 RESOLUTION RANGE 6.0 - 1.69 ANGSTROMS 1FFE 50
REMARK 3 DATA CUTOFF 1. SIGMA(F) 1FFE 51
REMARK 3 1FFE 52
REMARK 3 DATA COLLECTION. 1FFE 53
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 17069 1FFE 54
REMARK 3 COMPLETENESS OF DATA 89.9 % 1FFE 55
REMARK 3 REJECTION CRITERIA 1. SIGMA(I) 1FFE 56
REMARK 3 1FFE 57
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1FFE 58
REMARK 3 NUMBER OF PROTEIN ATOMS 1776 1FFE 59
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1FFE 60
REMARK 3 NUMBER OF HETEROGEN ATOMS 0 1FFE 61
REMARK 3 NUMBER OF SOLVENT ATOMS 352 1FFE 62
REMARK 3 1FFE 63
REMARK 3 STANDARD X-PLOR PARAMETERS 1FFE 64
REMARK 4 1FFE 65
REMARK 4 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED 1FFE 66
REMARK 4 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE 1FFE 67
REMARK 4 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL 1FFE 68
REMARK 4 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE 1FFE 69
REMARK 4 NUMBER; I=INSERTION CODE): 1FFE 70
REMARK 4 1FFE 71
REMARK 4 M RES CSSEQI 1FFE 72
REMARK 4 0 HOH 846 DISTANCE = 5.38 ANGSTROMS 1FFE 73
REMARK 18 1FFE 74
REMARK 18 EXPERIMENTAL DETAILS. 1FFE 75
REMARK 18 DATE OF DATA COLLECTION : 31-DEC-93 1FFE 76
REMARK 18 MONOCHROMATIC (Y/N) : Y 1FFE 77
REMARK 18 LAUE (Y/N) : N 1FFE 78
REMARK 18 WAVELENGTH OR RANGE (A) : 1.5418 1FFE 79
REMARK 18 DETECTOR TYPE : 18CM IMAGE PLATE 1FFE 80
REMARK 18 DETECTOR MANUFACTURER : MARRESEARCH 1FFE 81
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : 3.2 KW / XDS (IP VERSION) 1FFE 82
REMARK 18 DATA REDUNDANCY : 3.3 1FFE 83
REMARK 18 MERGING R VALUE (INTENSITY) : 0.039 1FFE 84
REMARK 19 1FFE 85
REMARK 19 SOLVENT CONTENT (VS) : 38. % 1FFE 86
REMARK 999 1FFE 87
REMARK 999 FOR CHAIN " " - 16 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1FFE 88
REMARK 999 1FFE 89
REMARK 999 FOR CHAIN " " - 1 C-TERMINAL RESIDUES NOT IN ATOMS LIST 1FFE 90
DBREF 1FFE 17 213 SWS P00590 CUTI_FUSSO 33 229 1FFE 91
SEQADV 1FFE ALA 42 SWS P00590 SER 58 ENGINEERED 1FFE 92
SEQRES 1 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG 1FFE 93
SEQRES 2 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY 1FFE 94
SEQRES 3 214 ASN SER ALA SER CYS ARG ASP VAL ILE PHE ILE TYR ALA 1FFE 95
SEQRES 4 214 ARG GLY ALA THR GLU THR GLY ASN LEU GLY THR LEU GLY 1FFE 96
SEQRES 5 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS 1FFE 97
SEQRES 6 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG 1FFE 98
SEQRES 7 214 ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER 1FFE 99
SEQRES 8 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN 1FFE 100
SEQRES 9 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY 1FFE 101
SEQRES 10 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE 1FFE 102
SEQRES 11 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY 1FFE 103
SEQRES 12 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG 1FFE 104
SEQRES 13 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL 1FFE 105
SEQRES 14 214 PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU 1FFE 106
SEQRES 15 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA 1FFE 107
SEQRES 16 214 ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG 1FFE 108
SEQRES 17 214 ALA VAL ARG GLY SER ALA 1FFE 109
FORMUL 2 HOH *350(H2 O1) 1FFE 110
HELIX 1 1 ASP 22 ASN 25 1 1FFE 111
HELIX 2 2 SER 28 SER 30 5 1FFE 112
HELIX 3 3 GLY 49 PHE 63 1 1FFE 113
HELIX 4 4 LEU 81 ALA 85 5 1FFE 114
HELIX 5 5 SER 92 LYS 108 1 1FFE 115
HELIX 6 6 SER 120 ASP 132 5 1FFE 116
HELIX 7 7 SER 135 LYS 140 1 1FFE 117
HELIX 8 8 ALA 164 ARG 166 5 1FFE 118
HELIX 9 9 LEU 176 THR 179 5 1FFE 119
HELIX 10 10 ALA 186 LEU 189 5 1FFE 120
HELIX 11 11 GLY 192 ARG 196 1 1FFE 121
HELIX 12 12 PRO 198 ARG 211 1 1FFE 122
SHEET 1 A 5 VAL 68 GLY 72 0 1FFE 123
SHEET 2 A 5 VAL 34 ALA 39 1 N VAL 34 O TRP 69 1FFE 124
SHEET 3 A 5 THR 113 TYR 119 1 N THR 113 O ILE 35 1FFE 125
SHEET 4 A 5 ILE 141 PHE 147 1 N ALA 142 O LEU 114 1FFE 126
SHEET 5 A 5 THR 167 PHE 170 1 N LYS 168 O THR 144 1FFE 127
SSBOND 1 CYS 31 CYS 109 1FFE 128
SSBOND 2 CYS 171 CYS 178 1FFE 129
SITE 1 CAT 3 SER 120 HIS 188 ASP 175 1FFE 130
CRYST1 35.120 67.360 37.050 90.00 93.90 90.00 P 21 2 1FFE 131
ORIGX1 1.000000 0.000000 0.000000 0.00000 1FFE 132
ORIGX2 0.000000 1.000000 0.000000 0.00000 1FFE 133
ORIGX3 0.000000 0.000000 1.000000 0.00000 1FFE 134
SCALE1 0.028474 0.000000 0.001941 0.00000 1FFE 135
SCALE2 0.000000 0.014846 0.000000 0.00000 1FFE 136
SCALE3 0.000000 0.000000 0.027053 0.00000 1FFE 137 |