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HEADER HALOPEROXIDASE 27-MAR-98 1A8Q
TITLE BROMOPEROXIDASE A1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMOPEROXIDASE A1;
COMPND 3 CHAIN: NULL;
COMPND 4 SYNONYM: CHLOROPEROXIDASE A1, HALOPEROXIDASE A1;
COMPND 5 EC: 1.11.1.10;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AUREOFACIENS;
SOURCE 3 COLLECTION: ATCC 10762;
SOURCE 4 GENE: BPOA1;
SOURCE 5 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TK64;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PIJ486;
SOURCE 9 EXPRESSION_SYSTEM_GENE: BPOA1
KEYWDS HALOPEROXIDASE, OXIDOREDUCTASE
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 1A8Q 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. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 31158
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.
REMARK 3 FREE R VALUE TEST SET COUNT : 1566
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.158
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.169
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1566
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 31158
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2143
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 207
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.02
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) : 0.06
REMARK 3 LOW RESOLUTION CUTOFF (A) : 9.0
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.014 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.027 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.034 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.021 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.137 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.176 ; 0.30
REMARK 3 MULTIPLE TORSION (A) : 0.252 ; 0.30
REMARK 3 H-BOND (X...Y) (A) : 0.135 ; 0.30
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) : 4.3 ; 7.00
REMARK 3 STAGGERED (DEGREES) : 14.3 ; 15.00
REMARK 3 TRANSVERSE (DEGREES) : 29.8 ; 20.00
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.41 ; 2.00
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.03 ; 3.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.20 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.41 ; 3.00
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A8Q 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 : JUL-1996
REMARK 200 TEMPERATURE (KELVIN) : 283
REMARK 200 PH : 8.0
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 : 31158
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.75
REMARK 200 RESOLUTION RANGE LOW (A) : 23.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 200 DATA REDUNDANCY : 2.8
REMARK 200 R MERGE (I) : 0.065
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.8
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.5
REMARK 200 R MERGE FOR SHELL (I) : 0.147
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.4
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1BRO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE 50MM
REMARK 280 TRIS/HCL PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 Y-X,-X,Z
REMARK 290 4555 -X,-Y,1/2+Z
REMARK 290 5555 Y,Y-X,1/2+Z
REMARK 290 6555 X-Y,X,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 -0.500000 -0.866004 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866046 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866004 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866046 -0.500000 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 45.93477
REMARK 290 SMTRY1 5 0.500000 0.866004 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866046 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 45.93477
REMARK 290 SMTRY1 6 0.500000 -0.866004 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866046 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.93477
REMARK 290
REMARK 290 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: NUL
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
DBREF 1A8Q 1 274 SWS P33912 BPA1_STRAU 1 274
SEQRES 1 274 PRO ILE CYS THR THR ARG ASP GLY VAL GLU ILE PHE TYR
SEQRES 2 274 LYS ASP TRP GLY GLN GLY ARG PRO VAL VAL PHE ILE HIS
SEQRES 3 274 GLY TRP PRO LEU ASN GLY ASP ALA TRP GLN ASP GLN LEU
SEQRES 4 274 LYS ALA VAL VAL ASP ALA GLY TYR ARG GLY ILE ALA HIS
SEQRES 5 274 ASP ARG ARG GLY HIS GLY HIS SER THR PRO VAL TRP ASP
SEQRES 6 274 GLY TYR ASP PHE ASP THR PHE ALA ASP ASP LEU ASN ASP
SEQRES 7 274 LEU LEU THR ASP LEU ASP LEU ARG ASP VAL THR LEU VAL
SEQRES 8 274 ALA HIS SER MET GLY GLY GLY GLU LEU ALA ARG TYR VAL
SEQRES 9 274 GLY ARG HIS GLY THR GLY ARG LEU ARG SER ALA VAL LEU
SEQRES 10 274 LEU SER ALA ILE PRO PRO VAL MET ILE LYS SER ASP LYS
SEQRES 11 274 ASN PRO ASP GLY VAL PRO ASP GLU VAL PHE ASP ALA LEU
SEQRES 12 274 LYS ASN GLY VAL LEU THR GLU ARG SER GLN PHE TRP LYS
SEQRES 13 274 ASP THR ALA GLU GLY PHE PHE SER ALA ASN ARG PRO GLY
SEQRES 14 274 ASN LYS VAL THR GLN GLY ASN LYS ASP ALA PHE TRP TYR
SEQRES 15 274 MET ALA MET ALA GLN THR ILE GLU GLY GLY VAL ARG CYS
SEQRES 16 274 VAL ASP ALA PHE GLY TYR THR ASP PHE THR GLU ASP LEU
SEQRES 17 274 LYS LYS PHE ASP ILE PRO THR LEU VAL VAL HIS GLY ASP
SEQRES 18 274 ASP ASP GLN VAL VAL PRO ILE ASP ALA THR GLY ARG LYS
SEQRES 19 274 SER ALA GLN ILE ILE PRO ASN ALA GLU LEU LYS VAL TYR
SEQRES 20 274 GLU GLY SER SER HIS GLY ILE ALA MET VAL PRO GLY ASP
SEQRES 21 274 LYS GLU LYS PHE ASN ARG ASP LEU LEU GLU PHE LEU ASN
SEQRES 22 274 LYS
FORMUL 2 HOH *207(H2 O1)
HELIX 1 1 GLY 32 ASP 44 5 13
HELIX 2 2 PHE 69 ASP 82 1 14
HELIX 3 3 SER 94 HIS 107 5 14
HELIX 4 4 ASP 137 PHE 162 1 26
HELIX 5 5 GLN 174 ALA 186 1 13
HELIX 6 6 ILE 189 TYR 201 1 13
HELIX 7 7 THR 205 LYS 210 1 6
HELIX 8 8 ILE 228 ALA 230 5 3
HELIX 9 9 GLY 232 ILE 238 1 7
HELIX 10 10 ASP 260 LEU 272 1 13
SHEET 1 A 2 ILE 2 THR 4 0
SHEET 2 A 2 GLU 10 PHE 12 -1 N ILE 11 O CYS 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 ILE 25 1 N VAL 22 O ARG 48
SHEET 4 B 7 VAL 88 HIS 93 1 N THR 89 O VAL 23
SHEET 5 B 7 LEU 112 LEU 118 1 N ARG 113 O VAL 88
SHEET 6 B 7 PRO 214 GLY 220 1 N PRO 214 O ALA 115
SHEET 7 B 7 GLU 243 TYR 247 1 N GLU 243 O VAL 217
CISPEP 1 TRP 28 PRO 29 0 -9.76
CISPEP 2 PRO 122 PRO 123 0 3.64
SITE 1 NUL 3 SER 94 ASP 223 HIS 252
CRYST1 80.770 80.770 91.870 90.00 90.00 120.00 P 63 6
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 0.012381 0.007148 0.000000 0.00000
SCALE2 0.000000 0.014296 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010885 0.00000 |