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HEADER HALOPEROXIDASE 30-MAR-98 1BRT
TITLE BROMOPEROXIDASE A2 MUTANT M99T
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMOPEROXIDASE A2;
COMPND 3 CHAIN: NULL;
COMPND 4 SYNONYM: HALOPEROXIDASE A2, CHLOROPEROXIDASE A2;
COMPND 5 EC: 1.11.1.10;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: M99T
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AUREOFACIENS;
SOURCE 3 COLLECTION: ATCC 10762;
SOURCE 4 GENE: BPOA2;
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: BPOA2
KEYWDS HALOPEROXIDASE, OXIDOREDUCTASE, PEROXIDASE, ALPHA/BETA
KEYWDS 2 HYDROLASE FOLD, MUTANT M99T
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 1BRT 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. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 90.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 45133
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) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.164
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.
REMARK 3 FREE R VALUE TEST SET COUNT : 2283
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.140
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.147
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2283
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 45133
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2146
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 246
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.22
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) : 0.02
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.8
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.020 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.034 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.038 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.025 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.171 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.165 ; 0.30
REMARK 3 MULTIPLE TORSION (A) : 0.262 ; 0.30
REMARK 3 H-BOND (X...Y) (A) : 0.143 ; 0.30
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 4.5 ; 7.00
REMARK 3 STAGGERED (DEGREES) : 14.2 ; 15.00
REMARK 3 TRANSVERSE (DEGREES) : 30.2 ; 20.00
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.55 ; 2.00
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.24 ; 3.0
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.84 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.0 ; 3.00
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BRT 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 : MAR-1995
REMARK 200 TEMPERATURE (KELVIN) : 283
REMARK 200 PH : 8.5
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 : 45113
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.5
REMARK 200 RESOLUTION RANGE LOW (A) : 27.2
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 6.0
REMARK 200 R MERGE (I) : 0.040
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.5
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.5
REMARK 200 R MERGE FOR SHELL (I) : 0.133
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1BRO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE 0.1 M
REMARK 280 TRIS/HCL, PH 8.5.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 13555 1/2+X,1/2+Y,1/2+Z
REMARK 290 14555 1/2-X,1/2-Y,1/2+Z
REMARK 290 15555 1/2-X,1/2+Y,1/2-Z
REMARK 290 16555 1/2+X,1/2-Y,1/2-Z
REMARK 290 17555 1/2+Z,1/2+X,1/2+Y
REMARK 290 18555 1/2+Z,1/2-X,1/2-Y
REMARK 290 19555 1/2-Z,1/2-X,1/2+Y
REMARK 290 20555 1/2-Z,1/2+X,1/2-Y
REMARK 290 21555 1/2+Y,1/2+Z,1/2+X
REMARK 290 22555 1/2-Y,1/2+Z,1/2-X
REMARK 290 23555 1/2+Y,1/2-Z,1/2-X
REMARK 290 24555 1/2-Y,1/2-Z,1/2+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 SMTRY1 13 1.000000 0.000000 0.000000 60.85686
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 60.85686
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 60.85686
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 60.85686
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 60.85686
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 60.85686
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 60.85686
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 60.85686
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 60.85686
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 60.85686
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 60.85686
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 60.85686
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 60.85686
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 60.85686
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 60.85686
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 60.85686
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 60.85686
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 60.85686
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 60.85686
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 60.85686
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 60.85686
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 60.85686
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 60.85686
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 60.85686
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 60.85686
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 60.85686
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 60.85686
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 60.85686
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 60.85686
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 60.85686
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 60.85686
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 60.85686
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 60.85686
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 60.85686
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 60.85686
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 60.85686
REMARK 290
REMARK 290 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: TAKEN FROM RELEASED PDB ENTRY 1BRO
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: TAKEN FROM RELEASED PDB ENTRY 1BRO
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: NUL
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 800
REMARK 800 SITE_IDENTIFIER: NUL
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
DBREF 1BRT 1 277 SWS P29715 BPA2_STRAU 1 277
SEQADV 1BRT THR 99 SWS P29715 MET 99 ENGINEERED
SEQRES 1 277 PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER ILE
SEQRES 2 277 ASP LEU TYR TYR GLU ASP HIS GLY THR GLY GLN PRO VAL
SEQRES 3 277 VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER TRP
SEQRES 4 277 GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR ARG
SEQRES 5 277 VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER SER
SEQRES 6 277 GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA ALA
SEQRES 7 277 ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN ASP
SEQRES 8 277 ALA VAL LEU VAL GLY PHE SER THR GLY THR GLY GLU VAL
SEQRES 9 277 ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE ALA
SEQRES 10 277 LYS VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU LEU
SEQRES 11 277 LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN GLU
SEQRES 12 277 PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP ARG
SEQRES 13 277 TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR ASN
SEQRES 14 277 LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU ALA
SEQRES 15 277 VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY PHE
SEQRES 16 277 PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR ASP
SEQRES 17 277 PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA LEU
SEQRES 18 277 ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE GLU
SEQRES 19 277 ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER ALA
SEQRES 20 277 GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU LEU
SEQRES 21 277 TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU ALA
SEQRES 22 277 PHE LEU ALA LYS
HET CL 1 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL1 1-
FORMUL 3 HOH *246(H2 O1)
HELIX 1 1 GLY 36 ASP 48 5 13
HELIX 2 2 TYR 73 LEU 87 1 15
HELIX 3 3 SER 98 TYR 111 5 14
HELIX 4 4 GLN 142 ALA 154 1 13
HELIX 5 5 ARG 156 PHE 167 1 12
HELIX 6 6 LEU 170 ASN 173 1 4
HELIX 7 7 GLU 180 SER 192 1 13
HELIX 8 8 PHE 195 THR 204 1 10
HELIX 9 9 ARG 210 ARG 215 1 6
HELIX 10 10 ILE 233 ASN 235 5 3
HELIX 11 11 ALA 237 ALA 243 1 7
HELIX 12 12 LEU 259 THR 262 1 4
HELIX 13 13 ALA 264 LEU 275 1 12
SHEET 1 A 7 TYR 17 GLY 21 0
SHEET 2 A 7 ARG 52 TYR 56 -1 N THR 55 O GLU 18
SHEET 3 A 7 PRO 25 ILE 29 1 N VAL 26 O ARG 52
SHEET 4 A 7 ALA 92 PHE 97 1 N VAL 93 O VAL 27
SHEET 5 A 7 ILE 116 LEU 122 1 N ALA 117 O ALA 92
SHEET 6 A 7 PRO 219 GLY 225 1 N PRO 219 O VAL 119
SHEET 7 A 7 GLU 248 VAL 252 1 N GLU 248 O ILE 222
SHEET 1 B 2 PHE 2 GLU 8 0
SHEET 2 B 2 THR 11 TYR 16 -1 N LEU 15 O ILE 3
CISPEP 1 PHE 32 PRO 33 0 -10.37
CISPEP 2 GLU 126 PRO 127 0 3.73
SITE 1 NUL 3 SER 98 ASP 228 HIS 257
CRYST1 121.720 121.720 121.720 90.00 90.00 90.00 I 2 3 24
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 0.008216 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008216 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008216 0.00000 |