HEADER TRANSCRIPTION 08-SEP-16 5T8R
TITLE CRYSTAL STRUCTURE OF HUMAN BAZ2A PHD ZINC FINGER IN COMPLEX WITH
TITLE 2 UNMODIFIED H3 10-MER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2A;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: PHD DOMAIN, UNP RESIDUES 1673-1728;
COMPND 5 SYNONYM: TRANSCRIPTION TERMINATION FACTOR I-INTERACTING PROTEIN 5,
COMPND 6 TIP5,HWALP3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HISTONE H3.1;
COMPND 10 CHAIN: E, G;
COMPND 11 FRAGMENT: UNP RESIDUES 2-11;
COMPND 12 SYNONYM: HISTONE H3/A,HISTONE H3/B,HISTONE H3/C,HISTONE H3/D,HISTONE
COMPND 13 H3/F,HISTONE H3/H,HISTONE H3/I,HISTONE H3/J,HISTONE H3/K,HISTONE
COMPND 14 H3/L;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BAZ2A, KIAA0314, TIP5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS PHD ZINC FINGERS, HISTONE3, COMPLEX, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.AMATO,M.S.GADD,A.BORTOLUZZI,A.CIULLI
REVDAT 3 17-JAN-24 5T8R 1 REMARK
REVDAT 2 17-MAY-17 5T8R 1 JRNL
REVDAT 1 05-APR-17 5T8R 0
JRNL AUTH A.BORTOLUZZI,A.AMATO,X.LUCAS,M.BLANK,A.CIULLI
JRNL TITL STRUCTURAL BASIS OF MOLECULAR RECOGNITION OF HELICAL HISTONE
JRNL TITL 2 H3 TAIL BY PHD FINGER DOMAINS.
JRNL REF BIOCHEM. J. V. 474 1633 2017
JRNL REFN ESSN 1470-8728
JRNL PMID 28341809
JRNL DOI 10.1042/BCJ20161053
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 10309
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 556
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 769
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 29
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1740
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 96
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.58000
REMARK 3 B22 (A**2) : 0.58000
REMARK 3 B33 (A**2) : -1.16000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.365
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.245
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.186
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.647
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1815 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1663 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2438 ; 1.510 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3793 ; 1.123 ; 3.015
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 221 ; 6.120 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 81 ;31.663 ;23.827
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 294 ;14.333 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;14.299 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 266 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1992 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 401 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 902 ; 1.609 ; 3.900
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 901 ; 1.608 ; 3.895
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1117 ; 2.840 ; 5.813
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1676 A 1728
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7590 32.9030 19.7190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0507 T22: 0.1140
REMARK 3 T33: 0.0205 T12: 0.0425
REMARK 3 T13: 0.0184 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 5.4857 L22: 6.5291
REMARK 3 L33: 5.5275 L12: -2.9079
REMARK 3 L13: 2.6119 L23: -1.8182
REMARK 3 S TENSOR
REMARK 3 S11: 0.1546 S12: 0.3396 S13: -0.1716
REMARK 3 S21: -0.3067 S22: -0.2212 S23: -0.1134
REMARK 3 S31: 0.2771 S32: 0.4785 S33: 0.0666
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1676 B 1726
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3650 24.6610 45.5140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0103 T22: 0.0709
REMARK 3 T33: 0.0401 T12: 0.0203
REMARK 3 T13: -0.0116 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 5.3121 L22: 5.7878
REMARK 3 L33: 6.8676 L12: -0.5201
REMARK 3 L13: -0.8122 L23: 0.3171
REMARK 3 S TENSOR
REMARK 3 S11: -0.0987 S12: -0.5323 S13: 0.1546
REMARK 3 S21: 0.1420 S22: 0.0829 S23: -0.4637
REMARK 3 S31: 0.2110 S32: 0.4247 S33: 0.0158
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1676 C 1727
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3920 38.6760 34.5630
REMARK 3 T TENSOR
REMARK 3 T11: 0.0173 T22: 0.0509
REMARK 3 T33: 0.0206 T12: 0.0244
REMARK 3 T13: -0.0116 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 2.3023 L22: 6.5595
REMARK 3 L33: 6.0671 L12: 1.5041
REMARK 3 L13: -1.0636 L23: -2.1300
REMARK 3 S TENSOR
REMARK 3 S11: -0.0126 S12: -0.1642 S13: -0.0058
REMARK 3 S21: 0.2082 S22: 0.0569 S23: -0.2871
REMARK 3 S31: 0.1219 S32: 0.3274 S33: -0.0444
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1676 D 1728
REMARK 3 ORIGIN FOR THE GROUP (A): 33.7480 23.5420 30.2130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1211 T22: 0.0391
REMARK 3 T33: 0.0390 T12: -0.0355
REMARK 3 T13: 0.0559 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 5.7433 L22: 4.8077
REMARK 3 L33: 8.7142 L12: 2.3675
REMARK 3 L13: -3.4096 L23: -5.3647
REMARK 3 S TENSOR
REMARK 3 S11: -0.2673 S12: 0.3346 S13: 0.0695
REMARK 3 S21: -0.4956 S22: 0.0795 S23: -0.2808
REMARK 3 S31: 0.3999 S32: 0.0604 S33: 0.1879
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5T8R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000219259.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8 - 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10901
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 45.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.78200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 4QF2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M NA/K PHOSPHATE, PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 49.71550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 36.30350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 36.30350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 74.57325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 36.30350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 36.30350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 24.85775
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 36.30350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.30350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 74.57325
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 36.30350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.30350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 24.85775
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 49.71550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, G
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
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, E
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 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 HIS A 1671
REMARK 465 MET A 1672
REMARK 465 SER A 1673
REMARK 465 VAL A 1674
REMARK 465 HIS B 1671
REMARK 465 MET B 1672
REMARK 465 SER B 1673
REMARK 465 VAL B 1674
REMARK 465 ASN B 1675
REMARK 465 GLN B 1727
REMARK 465 VAL B 1728
REMARK 465 HIS C 1671
REMARK 465 MET C 1672
REMARK 465 SER C 1673
REMARK 465 VAL C 1674
REMARK 465 VAL C 1728
REMARK 465 HIS D 1671
REMARK 465 MET D 1672
REMARK 465 SER D 1673
REMARK 465 VAL D 1674
REMARK 465 ARG E 8
REMARK 465 LYS E 9
REMARK 465 SER E 10
REMARK 465 LYS G 9
REMARK 465 SER G 10
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 A1676 CG CD CE NZ
REMARK 470 LYS B1676 CG CD CE NZ
REMARK 470 GLU C1715 CG CD OE1 OE2
REMARK 470 GLN C1727 CG CD OE1 NE2
REMARK 470 GLU D1689 CG CD OE1 OE2
REMARK 470 ARG E 2 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 5 CG CD OE1 NE2
REMARK 470 ARG G 8 CG CD NE CZ NH1 NH2
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 LYS C1676 69.37 62.46
REMARK 500 LYS D1676 45.37 -98.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B1921 DISTANCE = 6.18 ANGSTROMS
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 ZN A1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1679 SG
REMARK 620 2 CYS A1682 SG 108.6
REMARK 620 3 HIS A1702 ND1 100.7 99.0
REMARK 620 4 CYS A1705 SG 115.9 111.6 119.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1694 SG
REMARK 620 2 CYS A1697 SG 111.1
REMARK 620 3 CYS A1720 SG 112.5 104.6
REMARK 620 4 CYS A1723 SG 98.6 112.4 117.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1679 SG
REMARK 620 2 CYS B1682 SG 109.9
REMARK 620 3 HIS B1702 ND1 103.9 98.7
REMARK 620 4 CYS B1705 SG 118.6 111.7 112.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1694 SG
REMARK 620 2 CYS B1697 SG 105.9
REMARK 620 3 CYS B1720 SG 114.2 109.4
REMARK 620 4 CYS B1723 SG 97.4 112.9 116.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C1679 SG
REMARK 620 2 CYS C1682 SG 105.8
REMARK 620 3 HIS C1702 ND1 105.5 101.3
REMARK 620 4 CYS C1705 SG 116.9 110.9 115.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C1694 SG
REMARK 620 2 CYS C1697 SG 109.3
REMARK 620 3 CYS C1720 SG 112.0 106.7
REMARK 620 4 CYS C1723 SG 102.1 110.8 115.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D1679 SG
REMARK 620 2 CYS D1682 SG 107.8
REMARK 620 3 HIS D1702 ND1 103.3 103.9
REMARK 620 4 CYS D1705 SG 113.3 113.7 114.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D1694 SG
REMARK 620 2 CYS D1697 SG 114.0
REMARK 620 3 CYS D1720 SG 111.8 102.6
REMARK 620 4 CYS D1723 SG 96.8 112.9 119.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1802
DBREF 5T8R A 1673 1728 UNP Q9UIF9 BAZ2A_HUMAN 1673 1728
DBREF 5T8R B 1673 1728 UNP Q9UIF9 BAZ2A_HUMAN 1673 1728
DBREF 5T8R C 1673 1728 UNP Q9UIF9 BAZ2A_HUMAN 1673 1728
DBREF 5T8R D 1673 1728 UNP Q9UIF9 BAZ2A_HUMAN 1673 1728
DBREF 5T8R E 1 10 UNP P68431 H31_HUMAN 2 11
DBREF 5T8R G 1 10 UNP P68431 H31_HUMAN 2 11
SEQADV 5T8R HIS A 1671 UNP Q9UIF9 EXPRESSION TAG
SEQADV 5T8R MET A 1672 UNP Q9UIF9 EXPRESSION TAG
SEQADV 5T8R HIS B 1671 UNP Q9UIF9 EXPRESSION TAG
SEQADV 5T8R MET B 1672 UNP Q9UIF9 EXPRESSION TAG
SEQADV 5T8R HIS C 1671 UNP Q9UIF9 EXPRESSION TAG
SEQADV 5T8R MET C 1672 UNP Q9UIF9 EXPRESSION TAG
SEQADV 5T8R HIS D 1671 UNP Q9UIF9 EXPRESSION TAG
SEQADV 5T8R MET D 1672 UNP Q9UIF9 EXPRESSION TAG
SEQRES 1 A 58 HIS MET SER VAL ASN LYS VAL THR CYS LEU VAL CYS ARG
SEQRES 2 A 58 LYS GLY ASP ASN ASP GLU PHE LEU LEU LEU CYS ASP GLY
SEQRES 3 A 58 CYS ASP ARG GLY CYS HIS ILE TYR CYS HIS ARG PRO LYS
SEQRES 4 A 58 MET GLU ALA VAL PRO GLU GLY ASP TRP PHE CYS THR VAL
SEQRES 5 A 58 CYS LEU ALA GLN GLN VAL
SEQRES 1 B 58 HIS MET SER VAL ASN LYS VAL THR CYS LEU VAL CYS ARG
SEQRES 2 B 58 LYS GLY ASP ASN ASP GLU PHE LEU LEU LEU CYS ASP GLY
SEQRES 3 B 58 CYS ASP ARG GLY CYS HIS ILE TYR CYS HIS ARG PRO LYS
SEQRES 4 B 58 MET GLU ALA VAL PRO GLU GLY ASP TRP PHE CYS THR VAL
SEQRES 5 B 58 CYS LEU ALA GLN GLN VAL
SEQRES 1 C 58 HIS MET SER VAL ASN LYS VAL THR CYS LEU VAL CYS ARG
SEQRES 2 C 58 LYS GLY ASP ASN ASP GLU PHE LEU LEU LEU CYS ASP GLY
SEQRES 3 C 58 CYS ASP ARG GLY CYS HIS ILE TYR CYS HIS ARG PRO LYS
SEQRES 4 C 58 MET GLU ALA VAL PRO GLU GLY ASP TRP PHE CYS THR VAL
SEQRES 5 C 58 CYS LEU ALA GLN GLN VAL
SEQRES 1 D 58 HIS MET SER VAL ASN LYS VAL THR CYS LEU VAL CYS ARG
SEQRES 2 D 58 LYS GLY ASP ASN ASP GLU PHE LEU LEU LEU CYS ASP GLY
SEQRES 3 D 58 CYS ASP ARG GLY CYS HIS ILE TYR CYS HIS ARG PRO LYS
SEQRES 4 D 58 MET GLU ALA VAL PRO GLU GLY ASP TRP PHE CYS THR VAL
SEQRES 5 D 58 CYS LEU ALA GLN GLN VAL
SEQRES 1 E 10 ALA ARG THR LYS GLN THR ALA ARG LYS SER
SEQRES 1 G 10 ALA ARG THR LYS GLN THR ALA ARG LYS SER
HET ZN A1801 1
HET ZN A1802 1
HET PO4 A1803 5
HET ZN B1801 1
HET ZN B1802 1
HET PO4 B1803 5
HET ZN C1801 1
HET ZN C1802 1
HET GOL C1803 6
HET ZN D1801 1
HET ZN D1802 1
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 ZN 8(ZN 2+)
FORMUL 9 PO4 2(O4 P 3-)
FORMUL 15 GOL C3 H8 O3
FORMUL 18 HOH *96(H2 O)
HELIX 1 AA1 ASN A 1687 GLU A 1689 5 3
HELIX 2 AA2 TYR A 1704 HIS A 1706 5 3
HELIX 3 AA3 CYS A 1720 GLN A 1727 1 8
HELIX 4 AA4 ASN B 1687 GLU B 1689 5 3
HELIX 5 AA5 TYR B 1704 HIS B 1706 5 3
HELIX 6 AA6 CYS B 1720 GLN B 1726 1 7
HELIX 7 AA7 ASN C 1687 GLU C 1689 5 3
HELIX 8 AA8 CYS C 1720 ALA C 1725 1 6
HELIX 9 AA9 CYS D 1720 ALA D 1725 1 6
HELIX 10 AB1 THR G 3 ARG G 8 1 6
SHEET 1 AA1 2 LEU A1691 LEU A1693 0
SHEET 2 AA1 2 GLY A1700 HIS A1702 -1 O CYS A1701 N LEU A1692
SHEET 1 AA2 2 LEU B1691 LEU B1693 0
SHEET 2 AA2 2 GLY B1700 HIS B1702 -1 O CYS B1701 N LEU B1692
SHEET 1 AA3 2 LEU C1691 LEU C1693 0
SHEET 2 AA3 2 GLY C1700 HIS C1702 -1 O CYS C1701 N LEU C1692
SHEET 1 AA4 2 LEU D1691 LEU D1693 0
SHEET 2 AA4 2 GLY D1700 HIS D1702 -1 O CYS D1701 N LEU D1692
LINK SG CYS A1679 ZN ZN A1801 1555 1555 2.32
LINK SG CYS A1682 ZN ZN A1801 1555 1555 2.31
LINK SG CYS A1694 ZN ZN A1802 1555 1555 2.31
LINK SG CYS A1697 ZN ZN A1802 1555 1555 2.30
LINK ND1 HIS A1702 ZN ZN A1801 1555 1555 2.08
LINK SG CYS A1705 ZN ZN A1801 1555 1555 2.30
LINK SG CYS A1720 ZN ZN A1802 1555 1555 2.34
LINK SG CYS A1723 ZN ZN A1802 1555 1555 2.33
LINK SG CYS B1679 ZN ZN B1801 1555 1555 2.32
LINK SG CYS B1682 ZN ZN B1801 1555 1555 2.36
LINK SG CYS B1694 ZN ZN B1802 1555 1555 2.33
LINK SG CYS B1697 ZN ZN B1802 1555 1555 2.33
LINK ND1 HIS B1702 ZN ZN B1801 1555 1555 2.09
LINK SG CYS B1705 ZN ZN B1801 1555 1555 2.33
LINK SG CYS B1720 ZN ZN B1802 1555 1555 2.35
LINK SG CYS B1723 ZN ZN B1802 1555 1555 2.35
LINK SG CYS C1679 ZN ZN C1801 1555 1555 2.33
LINK SG CYS C1682 ZN ZN C1801 1555 1555 2.31
LINK SG CYS C1694 ZN ZN C1802 1555 1555 2.32
LINK SG CYS C1697 ZN ZN C1802 1555 1555 2.31
LINK ND1 HIS C1702 ZN ZN C1801 1555 1555 2.06
LINK SG CYS C1705 ZN ZN C1801 1555 1555 2.31
LINK SG CYS C1720 ZN ZN C1802 1555 1555 2.34
LINK SG CYS C1723 ZN ZN C1802 1555 1555 2.35
LINK SG CYS D1679 ZN ZN D1801 1555 1555 2.33
LINK SG CYS D1682 ZN ZN D1801 1555 1555 2.32
LINK SG CYS D1694 ZN ZN D1802 1555 1555 2.30
LINK SG CYS D1697 ZN ZN D1802 1555 1555 2.29
LINK ND1 HIS D1702 ZN ZN D1801 1555 1555 2.15
LINK SG CYS D1705 ZN ZN D1801 1555 1555 2.32
LINK SG CYS D1720 ZN ZN D1802 1555 1555 2.35
LINK SG CYS D1723 ZN ZN D1802 1555 1555 2.35
CISPEP 1 ARG A 1707 PRO A 1708 0 3.25
CISPEP 2 ARG B 1707 PRO B 1708 0 9.31
CISPEP 3 ARG C 1707 PRO C 1708 0 1.16
CISPEP 4 ARG D 1707 PRO D 1708 0 6.13
SITE 1 AC1 4 CYS A1679 CYS A1682 HIS A1702 CYS A1705
SITE 1 AC2 4 CYS A1694 CYS A1697 CYS A1720 CYS A1723
SITE 1 AC3 5 ARG A1707 HOH A1904 HOH A1912 HOH A1913
SITE 2 AC3 5 HOH A1917
SITE 1 AC4 4 CYS B1679 CYS B1682 HIS B1702 CYS B1705
SITE 1 AC5 4 CYS B1694 CYS B1697 CYS B1720 CYS B1723
SITE 1 AC6 2 ARG B1707 HOH B1910
SITE 1 AC7 4 CYS C1679 CYS C1682 HIS C1702 CYS C1705
SITE 1 AC8 4 CYS C1694 CYS C1697 CYS C1720 CYS C1723
SITE 1 AC9 2 ARG C1707 HOH C1920
SITE 1 AD1 4 CYS D1679 CYS D1682 HIS D1702 CYS D1705
SITE 1 AD2 4 CYS D1694 CYS D1697 CYS D1720 CYS D1723
CRYST1 72.607 72.607 99.431 90.00 90.00 90.00 P 43 21 2 32
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 0.013773 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013773 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010057 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
