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HEADER HALOPEROXIDASE 27-MAR-98 1A8S
TITLE CHLOROPEROXIDASE F/PROPIONATE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHLOROPEROXIDASE F;
COMPND 3 CHAIN: NULL;
COMPND 4 SYNONYM: HALOPEROXIDASE F;
COMPND 5 EC: 1.11.1.10;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS FLUORESCENS;
SOURCE 3 STRAIN: BL914;
SOURCE 4 GENE: CPOF;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PSK12;
SOURCE 8 EXPRESSION_SYSTEM_GENE: CPOF
KEYWDS HALOPEROXIDASE, OXIDOREDUCTASE, PROPIONATE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.HOFMANN,S.TOELZER,I.PELLETIER,J.ALTENBUCHNER,K.-H.VAN PEE,
AUTHOR 2 H.-J.HECHT
REVDAT 1 17-JUN-98 1A8S 0
JRNL AUTH B.HOFMANN,S.TOELZER,I.PELLETIER,J.ALTENBUCHNER,
JRNL AUTH 2 K.H.VAN PEE,H.J.HECHT
JRNL TITL STRUCTURAL INVESTIGATION OF THE COFACTOR-FREE
JRNL TITL 2 CHLOROPEROXIDASES
JRNL REF J.MOL.BIOL. V. 279 889 1998
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 0070
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 3 NUMBER OF REFLECTIONS : 33363
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.
REMARK 3 FREE R VALUE TEST SET COUNT : 1668
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.173
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.176
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1668
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 33363
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2085
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 335
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.38
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.57
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) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.4
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.017 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.031 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.037 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.024 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.154 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.173 ; 0.30
REMARK 3 MULTIPLE TORSION (A) : 0.195 ; 0.30
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : 0.0 ; 15.0
REMARK 3 PLANAR (DEGREES) : 4.0 ; 7.00
REMARK 3 STAGGERED (DEGREES) : 14.9 ; 15.00
REMARK 3 TRANSVERSE (DEGREES) : 33.8 ; 20.00
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.52 ; 2.00
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.88 ; 3.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.05 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.92 ; 3.00
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A8S 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 : OCT-1997
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33363
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 35.5
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 200 DATA REDUNDANCY : 2.0
REMARK 200 R MERGE (I) : 0.069
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.7
REMARK 200 R MERGE FOR SHELL (I) : 0.197
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.9
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: REFINED COORDINATES OF CHLOROPEROXIDASE L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.1
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM SULFATE 50MM
REMARK 280 CITRATE/PHOSPHATE BUFFER PH 6.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: NUL
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 850
REMARK 850 CORRECTION BEFORE RELEASE
REMARK 850 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE
REMARK 850 DATE REVISED: 09-APR-1998 TRACKING NUMBER: T14782
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1A8S GB 2623869 1 - 1 NOT IN ATOMS LIST
DBREF 1A8S 1 273 GB 2623869 AF031153 2 274
SEQRES 1 273 THR THR PHE THR THR ARG ASP GLY THR GLN ILE TYR TYR
SEQRES 2 273 LYS ASP TRP GLY SER GLY GLN PRO ILE VAL PHE SER HIS
SEQRES 3 273 GLY TRP PRO LEU ASN ALA ASP SER TRP GLU SER GLN MET
SEQRES 4 273 ILE PHE LEU ALA ALA GLN GLY TYR ARG VAL ILE ALA HIS
SEQRES 5 273 ASP ARG ARG GLY HIS GLY ARG SER SER GLN PRO TRP SER
SEQRES 6 273 GLY ASN ASP MET ASP THR TYR ALA ASP ASP LEU ALA GLN
SEQRES 7 273 LEU ILE GLU HIS LEU ASP LEU ARG ASP ALA VAL LEU PHE
SEQRES 8 273 GLY PHE SER THR GLY GLY GLY GLU VAL ALA ARG TYR ILE
SEQRES 9 273 GLY ARG HIS GLY THR ALA ARG VAL ALA LYS ALA GLY LEU
SEQRES 10 273 ILE SER ALA VAL PRO PRO LEU MET LEU LYS THR GLU ALA
SEQRES 11 273 ASN PRO GLY GLY LEU PRO MET GLU VAL PHE ASP GLY ILE
SEQRES 12 273 ARG GLN ALA SER LEU ALA ASP ARG SER GLN LEU TYR LYS
SEQRES 13 273 ASP LEU ALA SER GLY PRO PHE PHE GLY PHE ASN GLN PRO
SEQRES 14 273 GLY ALA LYS SER SER ALA GLY MET VAL ASP TRP PHE TRP
SEQRES 15 273 LEU GLN GLY MET ALA ALA GLY HIS LYS ASN ALA TYR ASP
SEQRES 16 273 CYS ILE LYS ALA PHE SER GLU THR ASP PHE THR GLU ASP
SEQRES 17 273 LEU LYS LYS ILE ASP VAL PRO THR LEU VAL VAL HIS GLY
SEQRES 18 273 ASP ALA ASP GLN VAL VAL PRO ILE GLU ALA SER GLY ILE
SEQRES 19 273 ALA SER ALA ALA LEU VAL LYS GLY SER THR LEU LYS ILE
SEQRES 20 273 TYR SER GLY ALA PRO HIS GLY LEU THR ASP THR HIS LYS
SEQRES 21 273 ASP GLN LEU ASN ALA ASP LEU LEU ALA PHE ILE LYS GLY
HET PPI 1 5
HET SO4 1 5
HET SO4 2 5
HET SO4 3 5
HET SO4 4 5
HETNAM PPI PROPANOIC ACID
HETNAM SO4 SULFATE ION
FORMUL 2 PPI C3 H6 O2
FORMUL 3 SO4 4(O4 S1 2-)
FORMUL 4 HOH *335(H2 O1)
HELIX 1 1 ALA 32 GLN 45 5 14
HELIX 2 2 MET 69 HIS 82 1 14
HELIX 3 3 SER 94 HIS 107 5 14
HELIX 4 4 MET 137 SER 160 1 24
HELIX 5 5 ALA 175 ALA 187 1 13
HELIX 6 6 HIS 190 GLU 202 1 13
HELIX 7 7 THR 206 LYS 211 1 6
HELIX 8 8 GLY 233 LEU 239 1 7
HELIX 9 9 LEU 255 THR 258 1 4
HELIX 10 10 LYS 260 ILE 271 1 12
SHEET 1 A 2 THR 2 THR 4 0
SHEET 2 A 2 GLN 10 TYR 12 -1 N ILE 11 O PHE 3
SHEET 1 B 7 TYR 13 TRP 16 0
SHEET 2 B 7 ARG 48 HIS 52 -1 N ALA 51 O LYS 14
SHEET 3 B 7 PRO 21 SER 25 1 N ILE 22 O ARG 48
SHEET 4 B 7 ALA 88 PHE 93 1 N VAL 89 O VAL 23
SHEET 5 B 7 VAL 112 ILE 118 1 N ALA 113 O ALA 88
SHEET 6 B 7 PRO 215 GLY 221 1 N PRO 215 O ALA 115
SHEET 7 B 7 THR 244 TYR 248 1 N THR 244 O VAL 218
CISPEP 1 TRP 28 PRO 29 0 -12.02
CISPEP 2 PRO 122 PRO 123 0 1.90
SITE 1 NUL 3 SER 94 ASP 224 HIS 253
CRYST1 106.470 106.470 106.470 90.00 90.00 90.00 P 2 3 12
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 0.009392 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009392 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009392 0.00000 |