HEADER KETOLISOMERASE 28-NOV-97 1A0E
TITLE XYLOSE ISOMERASE FROM THERMOTOGA NEAPOLITANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XYLOSE ISOMERASE;
COMPND 3 CHAIN: A, D;
COMPND 4 SYNONYM: GLUCOSE ISOMERASE;
COMPND 5 EC: 5.3.1.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA NEAPOLITANA;
SOURCE 3 ORGANISM_TAXID: 2337;
SOURCE 4 STRAIN: 5068;
SOURCE 5 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 6 GENE: XYLA;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PTNE2;
SOURCE 13 EXPRESSION_SYSTEM_GENE: XYLA
KEYWDS KETOLISOMERASE, XYLOSE METABOLISM, GLUCOSE-FRUCTOSE INTERCONVERSION,
KEYWDS 2 HYDRIDE TRANSFER, ALPHA-BETA BARREL, METALLOENZYME, THERMOPHILE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.GALLAY,R.CHOPRA,E.CONTI,P.BRICK,D.BLOW
REVDAT 4 18-APR-18 1A0E 1 REMARK
REVDAT 3 13-JUL-11 1A0E 1 VERSN
REVDAT 2 24-FEB-09 1A0E 1 VERSN
REVDAT 1 03-JUN-98 1A0E 0
JRNL AUTH O.GALLAY,R.CHOPRA,E.CONTI,P.BRICK,R.JACKSON,B.HARTLEY,
JRNL AUTH 2 C.VIEILLE,J.G.ZEIKUS,D.BLOW
JRNL TITL CRYSTAL STRUCTURES OF CLASS II XYLOSE ISOMERASES FROM TWO
JRNL TITL 2 THERMOPHILES AND A HYPERTHERMOPHILE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.E.CHAYEN,E.CONTI,C.VIEILLE,J.G.ZEIKUS
REMARK 1 TITL CRYSTALLIZATION AND INITIAL X-RAY ANALYSIS OF XYLOSE
REMARK 1 TITL 2 ISOMERASE FROM THERMOTOGA NEAPOLITANA
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 53 229 1997
REMARK 1 REFN ISSN 0907-4449
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.VIEILLE,J.M.HESS,R.M.KELLY,J.G.ZEIKUS
REMARK 1 TITL XYLA CLONING AND SEQUENCING AND BIOCHEMICAL CHARACTERIZATION
REMARK 1 TITL 2 OF XYLOSE ISOMERASE FROM THERMOTOGA NEAPOLITANA
REMARK 1 REF APPL.ENVIRON.MICROBIOL. V. 61 1867 1995
REMARK 1 REFN ISSN 0099-2240
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 26119
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : A POSTERIORI
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1265
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2957
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 144
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7012
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 256
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.00
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) : NULL
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.220
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : PARAM.ION
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : TOPH.ION
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED SIDE CHAINS WERE NOT
REMARK 3 INCLUDED IN REFINEMENT.
REMARK 4
REMARK 4 1A0E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170236.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUN-94
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-21
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : DUAL SLIT, COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : ENRAF-NONIUS FAST
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MADNES
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26137
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 12.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.15800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: XYLOSE ISOMERASE FROM THERMOANAEROBACTERIUM
REMARK 200 THERMOSULFURIGENES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 14%
REMARK 280 JEFFAMINE ED 4000, 5 MM MGSO4, 0.5 MM COCL2, 50 MM MOPS, PH 7.0
REMARK 280 (FOR DETAILS SEE REFERENCE 1).
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.43000
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 49.43000
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 1.000000 0.000000 0.000000 80.89500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.93500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 80.89500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.93500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.43000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 80.89500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 60.93500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 49.43000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 80.89500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 60.93500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 30610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -287.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
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 LYS A 109 CG CD CE NZ
REMARK 470 LYS A 120 CG CD CE NZ
REMARK 470 GLU A 123 CG CD OE1 OE2
REMARK 470 ARG A 128 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 130 CG CD CE NZ
REMARK 470 ASP A 131 CG OD1 OD2
REMARK 470 ASN A 133 CG OD1 ND2
REMARK 470 ARG A 221 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 384 CG CD OE1 OE2
REMARK 470 ARG A 390 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 395 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 399 CG CD OE1 OE2
REMARK 470 LYS A 401 CG CD CE NZ
REMARK 470 LYS A 406 CG CD CE NZ
REMARK 470 GLU A 409 CG CD OE1 OE2
REMARK 470 ILE A 412 CG1 CG2 CD1
REMARK 470 LYS A 414 CG CD CE NZ
REMARK 470 GLU A 415 CG CD OE1 OE2
REMARK 470 GLU A 418 CG CD OE1 OE2
REMARK 470 ARG A 443 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 109 CG CD CE NZ
REMARK 470 LYS D 120 CG CD CE NZ
REMARK 470 GLU D 123 CG CD OE1 OE2
REMARK 470 ARG D 128 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 130 CG CD CE NZ
REMARK 470 ASP D 131 CG OD1 OD2
REMARK 470 ASN D 133 CG OD1 ND2
REMARK 470 ARG D 221 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 384 CG CD OE1 OE2
REMARK 470 ARG D 390 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 395 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 399 CG CD OE1 OE2
REMARK 470 LYS D 401 CG CD CE NZ
REMARK 470 LYS D 406 CG CD CE NZ
REMARK 470 GLU D 409 CG CD OE1 OE2
REMARK 470 ILE D 412 CG1 CG2 CD1
REMARK 470 LYS D 414 CG CD CE NZ
REMARK 470 GLU D 415 CG CD OE1 OE2
REMARK 470 GLU D 418 CG CD OE1 OE2
REMARK 470 ARG D 443 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. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED 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 CO CO A 493 CO CO A 493 3655 0.32
REMARK 500 CG GLU D 2 CO CO D 493 3555 1.42
REMARK 500 CB GLU D 2 OE2 GLU D 2 3555 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 4 67.86 -116.44
REMARK 500 TRP A 68 1.36 -62.03
REMARK 500 SER A 132 -165.24 -115.86
REMARK 500 PHE A 144 -25.06 -144.67
REMARK 500 ALA A 153 -85.31 -107.41
REMARK 500 LYS A 235 -176.60 -176.00
REMARK 500 GLU A 236 112.91 62.94
REMARK 500 THR A 331 -87.34 -114.25
REMARK 500 LYS A 332 55.65 -103.82
REMARK 500 ILE A 412 -37.71 -39.54
REMARK 500 PHE D 4 67.87 -116.43
REMARK 500 TRP D 68 1.34 -62.01
REMARK 500 SER D 132 -165.27 -115.86
REMARK 500 PHE D 144 -25.10 -144.65
REMARK 500 ALA D 153 -85.29 -107.45
REMARK 500 LYS D 235 -176.58 -175.95
REMARK 500 GLU D 236 112.89 62.90
REMARK 500 THR D 331 -87.29 -114.22
REMARK 500 LYS D 332 55.60 -103.86
REMARK 500 ILE D 412 -37.69 -39.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 491 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 231 OE2
REMARK 620 2 GLU A 267 OE1 89.6
REMARK 620 3 ASP A 295 OD2 84.8 88.6
REMARK 620 4 ASP A 338 OD2 172.5 82.9 94.8
REMARK 620 5 HOH A 613 O 94.4 73.4 162.0 83.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 492 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 267 OE2
REMARK 620 2 HIS A 270 NE2 79.6
REMARK 620 3 HOH A 613 O 94.8 78.9
REMARK 620 4 HOH A 615 O 97.5 151.8 73.4
REMARK 620 5 HOH A 616 O 84.0 96.5 175.3 111.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 493 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 2 OE2
REMARK 620 2 GLU A 2 OE2 135.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO D 491 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 231 OE2
REMARK 620 2 GLU D 267 OE1 89.6
REMARK 620 3 ASP D 295 OD2 84.8 88.6
REMARK 620 4 ASP D 338 OD2 172.5 82.9 94.8
REMARK 620 5 HOH D 618 O 94.4 73.4 162.0 83.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO D 492 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 267 OE2
REMARK 620 2 HIS D 270 NE2 79.6
REMARK 620 3 HOH D 620 O 97.5 151.7
REMARK 620 4 HOH D 621 O 84.0 96.5 111.3
REMARK 620 5 HOH D 618 O 94.8 78.8 73.4 175.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO D 493 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 2 OE2
REMARK 620 2 GLU D 2 OE2 111.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CO1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 1 OF MOLECULE A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CO2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 2 OF MOLECULE A (HOH629 WAS
REMARK 800 ADDED AFTER LAST REFINEMENT RESULTED IN A NEW FO-FC PEAK AT THIS
REMARK 800 SITE).
REMARK 800
REMARK 800 SITE_IDENTIFIER: CO3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 3 OF MOLECULE A (SITE CO3 IS ON
REMARK 800 A CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AXIS: INTERPRETATION OF THE
REMARK 800 OBSERVED DENSITY PEAK AS A CO CATION WAS PRAGMATIC RATHER THAN
REMARK 800 RIGOROUS, AS THIS SITE IS CLEARLY NOT A FEATURE OF THE PROTEIN
REMARK 800 IN SOLUTION).
REMARK 800
REMARK 800 SITE_IDENTIFIER: CO4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 1 OF MOLECULE D
REMARK 800
REMARK 800 SITE_IDENTIFIER: CO5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 2 OF MOLECULE D (HOH629 WAS
REMARK 800 ADDED AFTER LAST REFINEMENT RESULTED IN A NEW FO-FC PEAK AT THIS
REMARK 800 SITE).
REMARK 800
REMARK 800 SITE_IDENTIFIER: CO6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CO BINDING SITE 3 OF MOLECULE D (SITE CO3 IS ON
REMARK 800 A CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AXIS: INTERPRETATION OF THE
REMARK 800 OBSERVED DENSITY PEAK AS A CO CATION WAS PRAGMATIC RATHER THAN
REMARK 800 RIGOROUS, AS THIS SITE IS CLEARLY NOT A FEATURE OF THE PROTEIN
REMARK 800 IN SOLUTION).
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 493
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO D 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO D 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO D 493
DBREF 1A0E A 1 443 UNP P45687 XYLA_THENE 2 444
DBREF 1A0E D 1 443 UNP P45687 XYLA_THENE 2 444
SEQRES 1 A 443 ALA GLU PHE PHE PRO GLU ILE PRO LYS VAL GLN PHE GLU
SEQRES 2 A 443 GLY LYS GLU SER THR ASN PRO LEU ALA PHE LYS PHE TYR
SEQRES 3 A 443 ASP PRO GLU GLU ILE ILE ASP GLY LYS PRO LEU LYS ASP
SEQRES 4 A 443 HIS LEU LYS PHE SER VAL ALA PHE TRP HIS THR PHE VAL
SEQRES 5 A 443 ASN GLU GLY ARG ASP PRO PHE GLY ASP PRO THR ALA ASP
SEQRES 6 A 443 ARG PRO TRP ASN ARG TYR THR ASP PRO MET ASP LYS ALA
SEQRES 7 A 443 PHE ALA ARG VAL ASP ALA LEU PHE GLU PHE CYS GLU LYS
SEQRES 8 A 443 LEU ASN ILE GLU TYR PHE CYS PHE HIS ASP ARG ASP ILE
SEQRES 9 A 443 ALA PRO GLU GLY LYS THR LEU ARG GLU THR ASN LYS ILE
SEQRES 10 A 443 LEU ASP LYS VAL VAL GLU ARG ILE LYS GLU ARG MET LYS
SEQRES 11 A 443 ASP SER ASN VAL LYS LEU LEU TRP GLY THR ALA ASN LEU
SEQRES 12 A 443 PHE SER HIS PRO ARG TYR MET HIS GLY ALA ALA THR THR
SEQRES 13 A 443 CYS SER ALA ASP VAL PHE ALA TYR ALA ALA ALA GLN VAL
SEQRES 14 A 443 LYS LYS ALA LEU GLU ILE THR LYS GLU LEU GLY GLY GLU
SEQRES 15 A 443 GLY TYR VAL PHE TRP GLY GLY ARG GLU GLY TYR GLU THR
SEQRES 16 A 443 LEU LEU ASN THR ASP LEU GLY PHE GLU LEU GLU ASN LEU
SEQRES 17 A 443 ALA ARG PHE LEU ARG MET ALA VAL ASP TYR ALA LYS ARG
SEQRES 18 A 443 ILE GLY PHE THR GLY GLN PHE LEU ILE GLU PRO LYS PRO
SEQRES 19 A 443 LYS GLU PRO THR LYS HIS GLN TYR ASP PHE ASP VAL ALA
SEQRES 20 A 443 THR ALA TYR ALA PHE LEU LYS SER HIS GLY LEU ASP GLU
SEQRES 21 A 443 TYR PHE LYS PHE ASN ILE GLU ALA ASN HIS ALA THR LEU
SEQRES 22 A 443 ALA GLY HIS THR PHE GLN HIS GLU LEU ARG MET ALA ARG
SEQRES 23 A 443 ILE LEU GLY LYS LEU GLY SER ILE ASP ALA ASN GLN GLY
SEQRES 24 A 443 ASP LEU LEU LEU GLY TRP ASP THR ASP GLN PHE PRO THR
SEQRES 25 A 443 ASN VAL TYR ASP THR THR LEU ALA MET TYR GLU VAL ILE
SEQRES 26 A 443 LYS ALA GLY GLY PHE THR LYS GLY GLY LEU ASN PHE ASP
SEQRES 27 A 443 ALA LYS VAL ARG ARG ALA SER TYR LYS VAL GLU ASP LEU
SEQRES 28 A 443 PHE ILE GLY HIS ILE ALA GLY MET ASP THR PHE ALA LEU
SEQRES 29 A 443 GLY PHE LYS VAL ALA TYR LYS LEU VAL LYS ASP GLY VAL
SEQRES 30 A 443 LEU ASP LYS PHE ILE GLU GLU LYS TYR ARG SER PHE ARG
SEQRES 31 A 443 GLU GLY ILE GLY ARG ASP ILE VAL GLU GLY LYS VAL ASP
SEQRES 32 A 443 PHE GLU LYS LEU GLU GLU TYR ILE ILE ASP LYS GLU THR
SEQRES 33 A 443 ILE GLU LEU PRO SER GLY LYS GLN GLU TYR LEU GLU SER
SEQRES 34 A 443 LEU ILE ASN SER TYR ILE VAL LYS THR ILE LEU GLU LEU
SEQRES 35 A 443 ARG
SEQRES 1 D 443 ALA GLU PHE PHE PRO GLU ILE PRO LYS VAL GLN PHE GLU
SEQRES 2 D 443 GLY LYS GLU SER THR ASN PRO LEU ALA PHE LYS PHE TYR
SEQRES 3 D 443 ASP PRO GLU GLU ILE ILE ASP GLY LYS PRO LEU LYS ASP
SEQRES 4 D 443 HIS LEU LYS PHE SER VAL ALA PHE TRP HIS THR PHE VAL
SEQRES 5 D 443 ASN GLU GLY ARG ASP PRO PHE GLY ASP PRO THR ALA ASP
SEQRES 6 D 443 ARG PRO TRP ASN ARG TYR THR ASP PRO MET ASP LYS ALA
SEQRES 7 D 443 PHE ALA ARG VAL ASP ALA LEU PHE GLU PHE CYS GLU LYS
SEQRES 8 D 443 LEU ASN ILE GLU TYR PHE CYS PHE HIS ASP ARG ASP ILE
SEQRES 9 D 443 ALA PRO GLU GLY LYS THR LEU ARG GLU THR ASN LYS ILE
SEQRES 10 D 443 LEU ASP LYS VAL VAL GLU ARG ILE LYS GLU ARG MET LYS
SEQRES 11 D 443 ASP SER ASN VAL LYS LEU LEU TRP GLY THR ALA ASN LEU
SEQRES 12 D 443 PHE SER HIS PRO ARG TYR MET HIS GLY ALA ALA THR THR
SEQRES 13 D 443 CYS SER ALA ASP VAL PHE ALA TYR ALA ALA ALA GLN VAL
SEQRES 14 D 443 LYS LYS ALA LEU GLU ILE THR LYS GLU LEU GLY GLY GLU
SEQRES 15 D 443 GLY TYR VAL PHE TRP GLY GLY ARG GLU GLY TYR GLU THR
SEQRES 16 D 443 LEU LEU ASN THR ASP LEU GLY PHE GLU LEU GLU ASN LEU
SEQRES 17 D 443 ALA ARG PHE LEU ARG MET ALA VAL ASP TYR ALA LYS ARG
SEQRES 18 D 443 ILE GLY PHE THR GLY GLN PHE LEU ILE GLU PRO LYS PRO
SEQRES 19 D 443 LYS GLU PRO THR LYS HIS GLN TYR ASP PHE ASP VAL ALA
SEQRES 20 D 443 THR ALA TYR ALA PHE LEU LYS SER HIS GLY LEU ASP GLU
SEQRES 21 D 443 TYR PHE LYS PHE ASN ILE GLU ALA ASN HIS ALA THR LEU
SEQRES 22 D 443 ALA GLY HIS THR PHE GLN HIS GLU LEU ARG MET ALA ARG
SEQRES 23 D 443 ILE LEU GLY LYS LEU GLY SER ILE ASP ALA ASN GLN GLY
SEQRES 24 D 443 ASP LEU LEU LEU GLY TRP ASP THR ASP GLN PHE PRO THR
SEQRES 25 D 443 ASN VAL TYR ASP THR THR LEU ALA MET TYR GLU VAL ILE
SEQRES 26 D 443 LYS ALA GLY GLY PHE THR LYS GLY GLY LEU ASN PHE ASP
SEQRES 27 D 443 ALA LYS VAL ARG ARG ALA SER TYR LYS VAL GLU ASP LEU
SEQRES 28 D 443 PHE ILE GLY HIS ILE ALA GLY MET ASP THR PHE ALA LEU
SEQRES 29 D 443 GLY PHE LYS VAL ALA TYR LYS LEU VAL LYS ASP GLY VAL
SEQRES 30 D 443 LEU ASP LYS PHE ILE GLU GLU LYS TYR ARG SER PHE ARG
SEQRES 31 D 443 GLU GLY ILE GLY ARG ASP ILE VAL GLU GLY LYS VAL ASP
SEQRES 32 D 443 PHE GLU LYS LEU GLU GLU TYR ILE ILE ASP LYS GLU THR
SEQRES 33 D 443 ILE GLU LEU PRO SER GLY LYS GLN GLU TYR LEU GLU SER
SEQRES 34 D 443 LEU ILE ASN SER TYR ILE VAL LYS THR ILE LEU GLU LEU
SEQRES 35 D 443 ARG
HET CO A 491 1
HET CO A 492 1
HET CO A 493 1
HET CO D 491 1
HET CO D 492 1
HET CO D 493 1
HETNAM CO COBALT (II) ION
FORMUL 3 CO 6(CO 2+)
FORMUL 9 HOH *256(H2 O)
HELIX 1 1 LEU A 37 LEU A 41 1 5
HELIX 2 2 PHE A 47 THR A 50 1 4
HELIX 3 3 PRO A 67 ASN A 69 5 3
HELIX 4 4 PRO A 74 LEU A 92 1 19
HELIX 5 5 ASP A 101 ILE A 104 1 4
HELIX 6 6 LEU A 111 ASP A 131 1 21
HELIX 7 7 PRO A 147 TYR A 149 5 3
HELIX 8 8 ALA A 159 GLU A 178 1 20
HELIX 9 9 LEU A 201 ILE A 222 1 22
HELIX 10 10 VAL A 246 HIS A 256 1 11
HELIX 11 11 ASP A 259 TYR A 261 5 3
HELIX 12 12 ALA A 268 LEU A 273 1 6
HELIX 13 13 PHE A 278 ILE A 287 1 10
HELIX 14 14 VAL A 314 ALA A 327 1 14
HELIX 15 15 VAL A 348 ASP A 375 1 28
HELIX 16 16 VAL A 377 LYS A 385 1 9
HELIX 17 17 ARG A 387 PHE A 389 5 3
HELIX 18 18 GLY A 392 GLU A 399 1 8
HELIX 19 19 PHE A 404 ILE A 411 1 8
HELIX 20 20 GLN A 424 GLU A 441 1 18
HELIX 21 21 LEU D 37 LEU D 41 1 5
HELIX 22 22 PHE D 47 THR D 50 1 4
HELIX 23 23 PRO D 67 ASN D 69 5 3
HELIX 24 24 PRO D 74 LEU D 92 1 19
HELIX 25 25 ASP D 101 ILE D 104 1 4
HELIX 26 26 LEU D 111 ASP D 131 1 21
HELIX 27 27 PRO D 147 TYR D 149 5 3
HELIX 28 28 ALA D 159 GLU D 178 1 20
HELIX 29 29 LEU D 201 ILE D 222 1 22
HELIX 30 30 VAL D 246 HIS D 256 1 11
HELIX 31 31 ASP D 259 TYR D 261 5 3
HELIX 32 32 ALA D 268 LEU D 273 1 6
HELIX 33 33 PHE D 278 ILE D 287 1 10
HELIX 34 34 VAL D 314 ALA D 327 1 14
HELIX 35 35 VAL D 348 ASP D 375 1 28
HELIX 36 36 VAL D 377 LYS D 385 1 9
HELIX 37 37 ARG D 387 PHE D 389 5 3
HELIX 38 38 GLY D 392 GLU D 399 1 8
HELIX 39 39 PHE D 404 ILE D 411 1 8
HELIX 40 40 GLN D 424 GLU D 441 1 18
SHEET 1 A 5 TRP A 138 THR A 140 0
SHEET 2 A 5 GLY A 183 PHE A 186 1 N GLY A 183 O GLY A 139
SHEET 3 A 5 GLN A 227 ILE A 230 1 N GLN A 227 O TYR A 184
SHEET 4 A 5 PHE A 262 GLU A 267 1 N LYS A 263 O PHE A 228
SHEET 5 A 5 LEU A 291 ASP A 295 1 N GLY A 292 O PHE A 264
SHEET 1 B 5 TRP D 138 THR D 140 0
SHEET 2 B 5 GLY D 183 PHE D 186 1 N GLY D 183 O GLY D 139
SHEET 3 B 5 GLN D 227 ILE D 230 1 N GLN D 227 O TYR D 184
SHEET 4 B 5 PHE D 262 GLU D 267 1 N LYS D 263 O PHE D 228
SHEET 5 B 5 LEU D 291 ASP D 295 1 N GLY D 292 O PHE D 264
LINK CO CO A 491 OE2 GLU A 231 1555 1555 1.99
LINK CO CO A 491 OE1 GLU A 267 1555 1555 2.12
LINK CO CO A 491 OD2 ASP A 295 1555 1555 2.16
LINK CO CO A 491 OD2 ASP A 338 1555 1555 1.94
LINK CO CO A 492 OE2 GLU A 267 1555 1555 1.94
LINK CO CO A 492 NE2 HIS A 270 1555 1555 2.39
LINK CO CO A 493 OE2 GLU A 2 1555 1555 2.01
LINK CO CO D 491 OE2 GLU D 231 1555 1555 1.99
LINK CO CO D 491 OE1 GLU D 267 1555 1555 2.12
LINK CO CO D 491 OD2 ASP D 295 1555 1555 2.16
LINK CO CO D 491 OD2 ASP D 338 1555 1555 1.94
LINK CO CO D 492 OE2 GLU D 267 1555 1555 1.94
LINK CO CO D 492 NE2 HIS D 270 1555 1555 2.39
LINK CO CO D 493 OE2 GLU D 2 1555 1555 2.01
LINK CO CO A 491 O HOH A 613 1555 1555 2.51
LINK CO CO A 492 O HOH A 613 1555 1555 2.05
LINK CO CO A 492 O HOH A 615 1555 1555 2.64
LINK CO CO A 492 O HOH A 616 1555 1555 2.41
LINK CO CO D 491 O HOH D 618 1555 1555 2.51
LINK CO CO D 492 O HOH D 620 1555 1555 2.64
LINK CO CO D 492 O HOH D 621 1555 1555 2.41
LINK CO CO D 492 O HOH D 618 1555 1555 2.05
LINK CO CO A 493 OE2 GLU A 2 1555 3655 2.24
LINK CO CO D 493 OE2 GLU D 2 1555 3555 1.67
CISPEP 1 GLU A 236 PRO A 237 0 1.04
CISPEP 2 GLU D 236 PRO D 237 0 1.07
SITE 1 CO1 5 GLU A 231 GLU A 267 ASP A 295 ASP A 338
SITE 2 CO1 5 HOH A 614
SITE 1 CO2 5 GLU A 267 HIS A 270 HOH A 614 HOH A 615
SITE 2 CO2 5 HOH A 616
SITE 1 CO3 1 GLU A 2
SITE 1 CO4 5 GLU D 231 GLU D 267 ASP D 295 ASP D 338
SITE 2 CO4 5 HOH D 619
SITE 1 CO5 5 GLU D 267 HIS D 270 HOH D 619 HOH D 620
SITE 2 CO5 5 HOH D 621
SITE 1 CO6 1 GLU D 2
SITE 1 AC1 5 GLU A 231 GLU A 267 ASP A 295 ASP A 338
SITE 2 AC1 5 HOH A 613
SITE 1 AC2 8 GLU A 267 HIS A 270 ASP A 306 ASP A 308
SITE 2 AC2 8 HOH A 613 HOH A 614 HOH A 615 HOH A 616
SITE 1 AC3 1 GLU A 2
SITE 1 AC4 5 GLU D 231 GLU D 267 ASP D 295 ASP D 338
SITE 2 AC4 5 HOH D 618
SITE 1 AC5 8 GLU D 267 HIS D 270 ASP D 306 ASP D 308
SITE 2 AC5 8 HOH D 618 HOH D 619 HOH D 620 HOH D 621
SITE 1 AC6 1 GLU D 2
CRYST1 161.790 121.870 98.860 90.00 90.00 90.00 C 2 2 21 16
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 0.006181 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008205 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010115 0.00000
MTRIX1 1 -0.999990 0.002980 0.002100 80.53531 1
MTRIX2 1 -0.002590 -0.985770 0.168110 0.16098 1
MTRIX3 1 0.002570 0.168100 0.985770 -0.04196 1
(ATOM LINES ARE NOT SHOWN.)
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