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HEADER SERINE ESTERASE 26-MAR-97 1AGY
TITLE THE 1.15 ANGSTROM REFINED STRUCTURE OF FUSARIUM SOLANI PISI
TITLE 2 CUTINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI PISI;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS HYDROLASE, SERINE ESTERASE, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.NICOLAS,C.MARTINEZ,C.CAMBILLAU
REVDAT 1 01-APR-98 1AGY 0
JRNL AUTH A.NICOLAS,C.MARTINEZ,C.CAMBILLAU
JRNL TITL THE 1.15 ANGSTROM REFINED STRUCTURE OF FSP CUTINASE
JRNL TITL 2 COMPARED TO OTHER MEMBERS OF ALPHA/BETA HYDROLASE
JRNL TITL 3 FOLD FAMILY
JRNL REF TO BE PUBLISHED
JRNL REFN 0353
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.LONGHI,M.CZJZEK,V.LAMZIN,A.NICOLAS,C.CAMBILLAU
REMARK 1 TITL ATOMIC RESOLUTION (1.0 A) CRYSTAL STRUCTURE OF
REMARK 1 TITL 2 FUSARIUM SOLANI CUTINASE: STEREOCHEMICAL ANALYSIS
REMARK 1 REF J.MOL.BIOL. V. 268 779 1997
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,M.LAUWEREYS,G.MATTHYSSENS,
REMARK 1 AUTH 2 C.CAMBILLAU
REMARK 1 TITL FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH
REMARK 1 TITL 2 A CATALYTIC SERINE ACCESSIBLE TO SOLVENT
REMARK 1 REF NATURE V. 356 615 1992
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006
REMARK 2
REMARK 2 RESOLUTION. 1.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1.15
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 6.0
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 57662
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.
REMARK 3 FREE R VALUE TEST SET COUNT : 5860
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.00003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.20
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.3
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6378
REMARK 3 BIN R VALUE (WORKING SET) : 0.40
REMARK 3 BIN FREE R VALUE : 0.40
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 623
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.0006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1635
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 271
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : 0.018
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 3.08
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 59.96
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.566
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARALLH22X.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19.PEP
REMARK 3 TOPOLOGY FILE 2 : TOPALLH22X.PRO
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AGY COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JAN-1993
REMARK 200 TEMPERATURE (KELVIN) : 288
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : SILICON CRYSTAL
REMARK 200 OPTICS : NO
REMARK 200
REMARK 200 DETECTOR TYPE : MULTIWIRE
REMARK 200 DETECTOR MANUFACTURER : NICOLET/SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : MARSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60972
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.15
REMARK 200 RESOLUTION RANGE LOW (A) : 20.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.22
REMARK 200 DATA REDUNDANCY : 4.09
REMARK 200 R MERGE (I) : 0.010
REMARK 200 R SYM (I) : 0.010
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.46
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.
REMARK 200 R MERGE FOR SHELL (I) : 0.030
REMARK 200 R SYM FOR SHELL (I) : 0.030
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.21
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RESOLUTION
REMARK 200 EXTENSION
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: CUTINASE STRUCTURE AT 1.6 ANGSTROM
REMARK 200 RESOLUTION
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM
REMARK 280 15 - 20% PEG 6000, 0.1 M HEPES, PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.67911
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG 32 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. SOME OF THESE MAY BE ATOMS
REMARK 500 LOCATED ON SPECIAL POSITIONS IN THE CELL. ATOMS WITH
REMARK 500 NON-BLANK ALTERNATE LOCATION INDICATORS ARE NOT INCLUDED
REMARK 500 IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 1H HOH 587 1HZ LYS 206 1655 1.27
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 0 HOH 640 DISTANCE = 9.65 ANGSTROMS
REMARK 525 0 HOH 646 DISTANCE = 8.30 ANGSTROMS
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: KABSCH AND SANDER
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: KABSCH AND SANDER
REMARK 750
REMARK 750 TURN
REMARK 750 DETERMINATION METHOD: RICHARDSON
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1AGY SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1AGY SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1AGY 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQRES 1 200 LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY ASN
SEQRES 2 200 SER ALA SER CYS ARG ASP VAL ILE PHE ILE TYR ALA ARG
SEQRES 3 200 GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY PRO
SEQRES 4 200 SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS ASP
SEQRES 5 200 GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG ALA
SEQRES 6 200 THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER SER
SEQRES 7 200 ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN ALA
SEQRES 8 200 ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY GLY
SEQRES 9 200 TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE GLU
SEQRES 10 200 ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY THR
SEQRES 11 200 VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG GLY
SEQRES 12 200 ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL PHE
SEQRES 13 200 CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU ILE
SEQRES 14 200 VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA ARG
SEQRES 15 200 GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG ALA
SEQRES 16 200 VAL ARG GLY SER ALA
FORMUL 2 HOH *271(H2 O1)
HELIX 1 A GLY 52 PHE 63 1 12
HELIX 2 B SER 92 LYS 108 1 17
HELIX 3 C GLN 121 ASP 132 1 12
HELIX 4 F TYR 191 ARG 211 1 21
SHEET 1 A 5 VAL 68 GLY 72 0
SHEET 2 A 5 VAL 34 ALA 39 1
SHEET 3 A 5 THR 113 TYR 119 1
SHEET 4 A 5 ALA 142 PHE 147 1
SHEET 5 A 5 ARG 166 PHE 170 1
TURN 1 T1 ASN 27 SER 30
TURN 2 T2 GLY 41 GLU 44
TURN 3 T3 GLY 64 GLY 67
TURN 4 T4 GLY 74 TYR 77
TURN 5 T5 LEU 86 GLY 89
TURN 6 T6 CYS 109 ALA 112
TURN 7 T7 TYR 119 GLY 122
TURN 8 T8 ASP 134 ILE 137
TURN 9 T9 TYR 149 ASN 152
TURN 10 T10 ILE 159 TYR 162
TURN 11 T11 ASN 172 ASP 175
TURN 12 T12 ASP 175 CYS 178
TURN 13 T13 ALA 185 HIS 188
SSBOND 1 CYS 31 CYS 109
SSBOND 2 CYS 171 CYS 178
SITE 1 CAT 3 SER 120 ASP 175 HIS 188
CRYST1 35.120 67.360 37.050 90.00 93.90 90.00 P 1 21 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.028474 0.000000 0.001941 0.00000
SCALE2 0.000000 0.014846 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027053 0.00000 |