HEADER LIPOPROTEIN 22-AUG-91 1LPE
TITLE THREE-DIMENSIONAL STRUCTURE OF THE LDL RECEPTOR-BINDING DOMAIN OF
TITLE 2 HUMAN APOLIPOPROTEIN E
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOLIPOPROTEIN E3;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS LIPOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.WILSON,D.A.AGARD
REVDAT 3 14-FEB-24 1LPE 1 REMARK
REVDAT 2 24-FEB-09 1LPE 1 VERSN
REVDAT 1 15-OCT-92 1LPE 0
JRNL AUTH C.WILSON,M.R.WARDELL,K.H.WEISGRABER,R.W.MAHLEY,D.A.AGARD
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE LDL RECEPTOR-BINDING
JRNL TITL 2 DOMAIN OF HUMAN APOLIPOPROTEIN E.
JRNL REF SCIENCE V. 252 1817 1991
JRNL REFN ISSN 0036-8075
JRNL PMID 2063194
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.P.AGGERBECK,J.R.WETTERAU,K.H.WEISGRABER,R.W.MAHLEY,
REMARK 1 AUTH 2 D.A.AGARD
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES ON
REMARK 1 TITL 2 THE AMINO-TERMINAL (RECEPTOR-BINDING) DOMAIN OF HUMAN
REMARK 1 TITL 3 APOLIPOPROTEIN E3 FROM SERUM VERY LOW DENSITY LIPOPROTEINS
REMARK 1 REF J.MOL.BIOL. V. 202 179 1988
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1172
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 121
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 3.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 X-RAY DATA WAS COLLECTED AT -150OC TO MINIMIZE RADIATION
REMARK 3 DECAY. PHASE INFORMATION WAS PROVIDED BY ISOMORPHOUS AND
REMARK 3 ANOMALOUS DIFFERENCES MEASURED FOR THE DIMETHYL MERCURY
REMARK 3 DERIVATIVE. EXTENSIVE SOLVENT FLATTENING (B.C. WANG
REMARK 3 PROGRAMS) WAS USED TO REFINE THE PHASES PRIOR TO BUILDING
REMARK 3 AN ATOMIC MODEL.
REMARK 3
REMARK 3 THE LOOP CONNECTING THE SECOND AND THIRD HELICES OF THE
REMARK 3 FOUR-HELIX BUNDLE (RESIDUES 83-88) IS POORLY DEFINED IN
REMARK 3 THE ELECTRON DENSITY MAP. X-PLOR-REFINED COORDINATES FOR
REMARK 3 THE LOOP HAVE BEEN INCLUDED IN THE STRUCTURE BUT ARE LIKELY
REMARK 3 TO CONTAIN ERRORS.
REMARK 4
REMARK 4 1LPE 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_1000174788.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 20.32500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.71500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.98000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.71500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.32500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.98000
REMARK 290 SMTRY3 4 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 400
REMARK 400 COMPOUND
REMARK 400 THREE ISOFORMS OF APO-E ARE RELATIVELY COMMON. THE
REMARK 400 STRUCTURE WAS SOLVED USING THE MOST FREQUENTLY OCCURRING
REMARK 400 ISOFORM, APO-E3.
REMARK 400
REMARK 400 SECONDARY STRUCTURE WAS ASSIGNED USING THE *DEFINE* PROGRAM
REMARK 400 (RICHARDS AND KUNDROT, PROTEINS V. 3, 71 (1988)).
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 TRP A 26 CD1 - CG - CD2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 TRP A 26 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP A 26 CE2 - CD2 - CG ANGL. DEV. = -6.8 DEGREES
REMARK 500 TRP A 34 CD1 - CG - CD2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 TRP A 34 CB - CG - CD1 ANGL. DEV. = -8.7 DEGREES
REMARK 500 TRP A 34 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 TRP A 34 CE2 - CD2 - CG ANGL. DEV. = -6.7 DEGREES
REMARK 500 TRP A 34 CG - CD2 - CE3 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 38 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TRP A 39 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 TRP A 39 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 VAL A 47 CG1 - CB - CG2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 MET A 64 CG - SD - CE ANGL. DEV. = -10.3 DEGREES
REMARK 500 ASP A 65 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 103 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG A 103 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 114 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 114 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 MET A 125 CG - SD - CE ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG A 134 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 142 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 145 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 150 NE - CZ - NH2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 158 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 158 NE - CZ - NH2 ANGL. DEV. = -3.7 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 GLN A 24 20.49 -141.90
REMARK 500 GLU A 79 -9.21 -58.50
REMARK 500 PRO A 84 67.42 -34.01
REMARK 500 GLU A 87 -39.65 -37.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 162 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1LPE A 23 166 UNP P02649 APOE_HUMAN 41 184
SEQRES 1 A 144 GLY GLN ARG TRP GLU LEU ALA LEU GLY ARG PHE TRP ASP
SEQRES 2 A 144 TYR LEU ARG TRP VAL GLN THR LEU SER GLU GLN VAL GLN
SEQRES 3 A 144 GLU GLU LEU LEU SER SER GLN VAL THR GLN GLU LEU ARG
SEQRES 4 A 144 ALA LEU MET ASP GLU THR MET LYS GLU LEU LYS ALA TYR
SEQRES 5 A 144 LYS SER GLU LEU GLU GLU GLN LEU THR PRO VAL ALA GLU
SEQRES 6 A 144 GLU THR ARG ALA ARG LEU SER LYS GLU LEU GLN ALA ALA
SEQRES 7 A 144 GLN ALA ARG LEU GLY ALA ASP MET GLU ASP VAL CYS GLY
SEQRES 8 A 144 ARG LEU VAL GLN TYR ARG GLY GLU VAL GLN ALA MET LEU
SEQRES 9 A 144 GLY GLN SER THR GLU GLU LEU ARG VAL ARG LEU ALA SER
SEQRES 10 A 144 HIS LEU ARG LYS LEU ARG LYS ARG LEU LEU ARG ASP ALA
SEQRES 11 A 144 ASP ASP LEU GLN LYS ARG LEU ALA VAL TYR GLN ALA GLY
SEQRES 12 A 144 ALA
FORMUL 2 HOH *121(H2 O)
HELIX 1 H1 GLN A 24 THR A 42 1 19
HELIX 2 HC SER A 44 SER A 53 1 10
HELIX 3 H2 SER A 54 GLN A 81 1 28
HELIX 4 H3 GLU A 87 VAL A 122 1 36
HELIX 5 H4 THR A 130 ALA A 164 1 35
CRYST1 40.650 53.960 85.430 90.00 90.00 90.00 P 21 21 21 4
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 0.024600 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011705 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
