HEADER LIGASE 06-APR-07 2YV1
TITLE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE ALPHA CHAIN FROM
TITLE 2 METHANOCALDOCOCCUS JANNASCHII DSM 2661
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUCCINYL-COA LIGASE [ADP-FORMING] SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SUCCINYL-COA SYNTHETASE SUBUNIT ALPHA, SCS-ALPHA;
COMPND 5 EC: 6.2.1.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_TAXID: 243232;
SOURCE 4 STRAIN: DSM 2661;
SOURCE 5 GENE: SUCD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-21A
KEYWDS COA-BINDING DOMAIN, LIGASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA X-RAY DIFFRACTION
AUTHOR H.NIWA,S.KURAMITSU,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 4 25-OCT-23 2YV1 1 REMARK
REVDAT 3 13-JUL-11 2YV1 1 VERSN
REVDAT 2 24-FEB-09 2YV1 1 VERSN
REVDAT 1 09-OCT-07 2YV1 0
JRNL AUTH H.NIWA,S.KURAMITSU,S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE ALPHA CHAIN
JRNL TITL 2 FROM METHANOCALDOCOCCUS JANNASCHII DSM 2661
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1285654.870
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 31212
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 SET) : 0.205
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1572
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4796
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 225
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1967
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 271
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.56000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -1.62000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.12
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.960
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.270 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.980 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.220 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.310 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 44.02
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2YV1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000027169.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31324
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 44.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.36600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1OI7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE, 20% PEG 3350,
REMARK 280 0.2M LITHIUM SULFATE, PH5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 32.94100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.97900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.52200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.97900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.94100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.52200
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 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 MET A 1
REMARK 465 VAL A 2
REMARK 465 LEU A 3
REMARK 465 ARG A 4
REMARK 465 ASP A 5
REMARK 465 LYS A 6
REMARK 465 SER A 242
REMARK 465 ALA A 243
REMARK 465 PRO A 244
REMARK 465 GLU A 245
REMARK 465 GLY A 246
REMARK 465 LYS A 247
REMARK 465 ARG A 248
REMARK 465 MET A 249
REMARK 465 GLY A 250
REMARK 465 HIS A 251
REMARK 465 ALA A 252
REMARK 465 GLY A 253
REMARK 465 ALA A 254
REMARK 465 ILE A 255
REMARK 465 VAL A 256
REMARK 465 GLU A 257
REMARK 465 LYS A 258
REMARK 465 GLY A 259
REMARK 465 LYS A 260
REMARK 465 LYS A 294
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 MET A 7 CG SD CE
REMARK 470 LYS A 231 CG CD CE NZ
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 LEU A 9 -104.77 -104.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MJA001001246.1 RELATED DB: TARGETDB
DBREF 2YV1 A 1 294 UNP Q58643 SUCD_METJA 1 294
SEQRES 1 A 294 MET VAL LEU ARG ASP LYS MET ILE LEU LEU ASP GLU ASN
SEQRES 2 A 294 THR LYS ALA ILE VAL GLN GLY ILE THR GLY ARG GLN GLY
SEQRES 3 A 294 SER PHE HIS THR LYS LYS MET LEU GLU CYS GLY THR LYS
SEQRES 4 A 294 ILE VAL GLY GLY VAL THR PRO GLY LYS GLY GLY GLN ASN
SEQRES 5 A 294 VAL HIS GLY VAL PRO VAL PHE ASP THR VAL LYS GLU ALA
SEQRES 6 A 294 VAL LYS GLU THR ASP ALA ASN ALA SER VAL ILE PHE VAL
SEQRES 7 A 294 PRO ALA PRO PHE ALA LYS ASP ALA VAL PHE GLU ALA ILE
SEQRES 8 A 294 ASP ALA GLY ILE GLU LEU ILE VAL VAL ILE THR GLU HIS
SEQRES 9 A 294 ILE PRO VAL HIS ASP THR MET GLU PHE VAL ASN TYR ALA
SEQRES 10 A 294 GLU ASP VAL GLY VAL LYS ILE ILE GLY PRO ASN THR PRO
SEQRES 11 A 294 GLY ILE ALA SER PRO LYS VAL GLY LYS LEU GLY ILE ILE
SEQRES 12 A 294 PRO MET GLU VAL LEU LYS GLU GLY SER VAL GLY MET VAL
SEQRES 13 A 294 SER ARG SER GLY THR LEU THR TYR GLU ILE ALA HIS GLN
SEQRES 14 A 294 ILE LYS LYS ALA GLY PHE GLY VAL SER THR CYS VAL GLY
SEQRES 15 A 294 ILE GLY GLY ASP PRO ILE VAL GLY LEU ARG TYR LYS GLU
SEQRES 16 A 294 VAL LEU ASP LEU PHE GLU LYS ASP ASP GLU THR GLU ALA
SEQRES 17 A 294 ILE VAL MET ILE GLY GLU ILE GLY GLY GLY ALA GLU GLU
SEQRES 18 A 294 GLU ALA ALA LYS PHE ILE GLU LYS MET LYS LYS PRO VAL
SEQRES 19 A 294 ILE GLY TYR ILE ALA GLY GLN SER ALA PRO GLU GLY LYS
SEQRES 20 A 294 ARG MET GLY HIS ALA GLY ALA ILE VAL GLU LYS GLY LYS
SEQRES 21 A 294 GLY THR ALA GLU SER LYS MET LYS ALA LEU GLU GLU ALA
SEQRES 22 A 294 GLY ALA TYR VAL ALA LYS ASN ILE SER ASP ILE PRO LYS
SEQRES 23 A 294 LEU LEU ALA GLY ILE LEU GLY LYS
FORMUL 2 HOH *271(H2 O)
HELIX 1 1 GLY A 23 CYS A 36 1 14
HELIX 2 2 THR A 61 ASP A 70 1 10
HELIX 3 3 PRO A 79 ALA A 93 1 15
HELIX 4 4 PRO A 106 GLY A 121 1 16
HELIX 5 5 PRO A 144 LEU A 148 5 5
HELIX 6 6 GLY A 160 ALA A 173 1 14
HELIX 7 7 ARG A 192 LYS A 202 1 11
HELIX 8 8 GLY A 218 GLU A 228 1 11
HELIX 9 9 THR A 262 GLY A 274 1 13
HELIX 10 10 SER A 282 GLY A 293 1 12
SHEET 1 A 7 ASN A 52 VAL A 53 0
SHEET 2 A 7 VAL A 56 PHE A 59 -1 O VAL A 56 N VAL A 53
SHEET 3 A 7 ILE A 40 VAL A 44 1 N GLY A 43 O PHE A 59
SHEET 4 A 7 ALA A 16 GLN A 19 1 N VAL A 18 O VAL A 44
SHEET 5 A 7 ALA A 73 ILE A 76 1 O VAL A 75 N GLN A 19
SHEET 6 A 7 LEU A 97 VAL A 100 1 O VAL A 99 N ILE A 76
SHEET 7 A 7 LYS A 123 ILE A 125 1 O LYS A 123 N ILE A 98
SHEET 1 B 7 GLY A 138 GLY A 141 0
SHEET 2 B 7 GLY A 131 SER A 134 -1 N SER A 134 O GLY A 138
SHEET 3 B 7 VAL A 177 GLY A 182 -1 O CYS A 180 N ALA A 133
SHEET 4 B 7 VAL A 153 SER A 157 1 N MET A 155 O THR A 179
SHEET 5 B 7 ALA A 208 GLU A 214 1 O VAL A 210 N GLY A 154
SHEET 6 B 7 VAL A 234 ALA A 239 1 O ILE A 235 N ILE A 209
SHEET 7 B 7 TYR A 276 VAL A 277 1 O TYR A 276 N VAL A 234
CISPEP 1 GLY A 126 PRO A 127 0 0.73
CRYST1 65.882 65.044 65.958 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 0.015179 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015374 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015161 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
