HEADER DNA EXCISION REPAIR 10-NOV-99 1QOJ
TITLE CRYSTAL STRUCTURE OF E.COLI UVRB C-TERMINAL DOMAIN, AND A MODEL FOR
TITLE 2 UVRB-UVRC INTERACTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UVRB;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: PP3398
KEYWDS DNA EXCISION REPAIR, NUCLEOTIDE EXCISION REPAIR, UVRB PROTEIN, UVRB-C
KEYWDS 2 INTERACTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SOHI,A.ALEXANDROVICH,G.MOOLENAAR,R.VISSE,N.GOOSEN,X.VERNEDE,
AUTHOR 2 J.FONTECILLA-CAMPS,J.CHAMPNESS,M.R.SANDERSON
REVDAT 3 06-MAR-19 1QOJ 1 REMARK LINK
REVDAT 2 24-FEB-09 1QOJ 1 VERSN
REVDAT 1 10-NOV-00 1QOJ 0
JRNL AUTH M.SOHI,A.ALEXANDROVICH,G.MOOLENAAR,R.VISSE,N.GOOSEN,
JRNL AUTH 2 X.VERNEDE,J.FONTECILLA-CAMPS,J.CHAMPNESS,M.R.SANDERSON
JRNL TITL CRYSTAL STRUCTURE OF E.COLI UVRB C-TERMINAL DOMAIN, AND A
JRNL TITL 2 MODEL FOR UVRB-UVRC INTERACTION
JRNL REF FEBS LETT. V. 465 161 2000
JRNL REFN ISSN 0014-5793
JRNL PMID 10631326
JRNL DOI 10.1016/S0014-5793(99)01690-7
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.327
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 8435
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.286
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 377
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 6689
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 713
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 3031
REMARK 3 NUMBER OF RESTRAINTS : 3887
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 ANGLE DISTANCES (A) : 0.022
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QOJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1290004285.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8856, 0.9788, 0.9789
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 4450
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.860
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.71
REMARK 200 R MERGE FOR SHELL (I) : 0.51100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.750
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXL-97, SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BY VAPOUR DIFFUSION 3UL PROTEIN
REMARK 280 SOLUTION: 2MG/ML UVRB DOMAIN, 20MM TRIS-CL PH7.0, 150MM NACL 0.1%
REMARK 280 NAN3 + 3UL WELL SOLUTION 0.5ML WELL SOLUTION: 35% SAT. AMMONIUM
REMARK 280 SULPHATE 100MM TRIS-CL PH8.8, 0.1% NAN3, PH 8.50, VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.46000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.73000
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 35.46000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 17.73000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 146.89523
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MSE A 611
REMARK 465 HIS A 612
REMARK 465 HIS A 613
REMARK 465 HIS A 614
REMARK 465 HIS A 615
REMARK 465 HIS A 616
REMARK 465 HIS A 617
REMARK 465 LEU A 618
REMARK 465 GLU A 619
REMARK 465 PRO A 620
REMARK 465 ASP A 621
REMARK 465 ASN A 622
REMARK 465 VAL A 623
REMARK 465 PRO A 624
REMARK 465 MSE A 625
REMARK 465 ASP A 626
REMARK 465 MSE A 627
REMARK 465 MSE B 611
REMARK 465 HIS B 612
REMARK 465 HIS B 613
REMARK 465 HIS B 614
REMARK 465 HIS B 615
REMARK 465 HIS B 616
REMARK 465 HIS B 617
REMARK 465 LEU B 618
REMARK 465 GLU B 619
REMARK 465 PRO B 620
REMARK 465 ASP B 621
REMARK 465 ASN B 622
REMARK 465 VAL B 623
REMARK 465 PRO B 624
REMARK 465 MSE B 625
REMARK 465 ASP B 626
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 630 CG CD CE NZ
REMARK 470 GLN A 634 CG CD OE1 NE2
REMARK 470 ILE A 636 CD1
REMARK 470 GLU A 638 CG CD OE1 OE2
REMARK 470 LEU A 642 CG CD1 CD2
REMARK 470 GLN A 645 CD OE1 NE2
REMARK 470 GLN A 648 CD OE1 NE2
REMARK 470 ILE A 670 CD1
REMARK 470 SER A 673 O
REMARK 470 LYS B 630 CG CD CE NZ
REMARK 470 GLN B 634 CG CD OE1 NE2
REMARK 470 LYS B 635 CD CE NZ
REMARK 470 ILE B 636 CD1
REMARK 470 GLN B 645 CD OE1 NE2
REMARK 470 ILE B 658 CD1
REMARK 470 GLN B 661 OE1 NE2
REMARK 470 SER B 673 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MSE B 644 CB - CG - SE ANGL. DEV. = 18.4 DEGREES
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 652 -143.42 -69.01
REMARK 500 GLU A 653 -87.31 62.11
REMARK 500 PHE A 669 -71.50 -53.42
REMARK 500 ALA A 672 47.83 -80.66
REMARK 500 PHE B 652 -149.50 -68.75
REMARK 500 GLU B 653 -87.53 65.82
REMARK 500 ARG B 666 -74.66 -50.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E52 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF ESCHERICHIA COLI UVRB C-TERMINAL DOMAIN
DBREF 1QOJ A 611 617 PDB 1QOJ 1QOJ 611 617
DBREF 1QOJ A 618 673 UNP P07025 UVRB_ECOLI 618 673
DBREF 1QOJ B 611 617 PDB 1QOJ 1QOJ 611 617
DBREF 1QOJ B 618 673 UNP P07025 UVRB_ECOLI 618 673
SEQADV 1QOJ MSE A 643 UNP P07025 MET 643 MODIFIED RESIDUE
SEQADV 1QOJ MSE A 644 UNP P07025 MET 644 MODIFIED RESIDUE
SEQADV 1QOJ MSE B 627 UNP P07025 MET 627 MODIFIED RESIDUE
SEQADV 1QOJ MSE B 643 UNP P07025 MET 643 MODIFIED RESIDUE
SEQADV 1QOJ MSE B 644 UNP P07025 MET 644 MODIFIED RESIDUE
SEQRES 1 A 63 MSE HIS HIS HIS HIS HIS HIS LEU GLU PRO ASP ASN VAL
SEQRES 2 A 63 PRO MSE ASP MSE SER PRO LYS ALA LEU GLN GLN LYS ILE
SEQRES 3 A 63 HIS GLU LEU GLU GLY LEU MSE MSE GLN HIS ALA GLN ASN
SEQRES 4 A 63 LEU GLU PHE GLU GLU ALA ALA GLN ILE ARG ASP GLN LEU
SEQRES 5 A 63 HIS GLN LEU ARG GLU LEU PHE ILE ALA ALA SER
SEQRES 1 B 63 MSE HIS HIS HIS HIS HIS HIS LEU GLU PRO ASP ASN VAL
SEQRES 2 B 63 PRO MSE ASP MSE SER PRO LYS ALA LEU GLN GLN LYS ILE
SEQRES 3 B 63 HIS GLU LEU GLU GLY LEU MSE MSE GLN HIS ALA GLN ASN
SEQRES 4 B 63 LEU GLU PHE GLU GLU ALA ALA GLN ILE ARG ASP GLN LEU
SEQRES 5 B 63 HIS GLN LEU ARG GLU LEU PHE ILE ALA ALA SER
MODRES 1QOJ MSE A 643 MET SELENOMETHIONINE
MODRES 1QOJ MSE A 644 MET SELENOMETHIONINE
MODRES 1QOJ MSE B 627 MET SELENOMETHIONINE
MODRES 1QOJ MSE B 643 MET SELENOMETHIONINE
MODRES 1QOJ MSE B 644 MET SELENOMETHIONINE
HET MSE A 643 8
HET MSE A 644 8
HET MSE B 627 8
HET MSE B 643 8
HET MSE B 644 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 5(C5 H11 N O2 SE)
HELIX 1 1 SER A 628 LEU A 642 1 15
HELIX 2 2 HIS A 646 LEU A 650 5 5
HELIX 3 3 GLU A 653 ALA A 672 1 20
HELIX 4 4 SER B 628 LEU B 642 1 15
HELIX 5 5 HIS B 646 LEU B 650 5 5
HELIX 6 6 GLU B 653 SER B 673 1 21
LINK C LEU A 642 N MSE A 643 1555 1555 1.33
LINK C MSE A 643 N MSE A 644 1555 1555 1.31
LINK C MSE A 644 N GLN A 645 1555 1555 1.33
LINK C MSE B 627 N SER B 628 1555 1555 1.33
LINK C LEU B 642 N MSE B 643 1555 1555 1.34
LINK C MSE B 643 N MSE B 644 1555 1555 1.34
LINK C MSE B 644 N GLN B 645 1555 1555 1.32
CRYST1 84.810 84.810 53.190 90.00 90.00 120.00 P 62 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 0.011791 0.006807 0.000000 0.00000
SCALE2 0.000000 0.013615 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018800 0.00000
MTRIX1 1 0.952280 0.297190 0.069570 -14.65653 1
MTRIX2 1 0.291700 -0.953220 0.079230 93.76870 1
MTRIX3 1 0.089860 -0.055150 -0.994430 9.34176 1
(ATOM LINES ARE NOT SHOWN.)
END
