HEADER TRANSFERASE 19-APR-18 6D5Y
TITLE CRYSTAL STRUCTURE OF ERK2 G169D MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 13-360;
COMPND 5 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,
COMPND 6 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,
COMPND 7 MAPK 2;
COMPND 8 EC: 2.7.11.24;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MAPK1, ERK2, PRKM1, PRKM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.YIN,B.S.JAISWAL,W.WANG
REVDAT 2 13-MAR-24 6D5Y 1 REMARK
REVDAT 1 27-FEB-19 6D5Y 0
JRNL AUTH B.S.JAISWAL,S.DURINCK,E.W.STAWISKI,J.YIN,W.WANG,E.LIN,
JRNL AUTH 2 J.MOFFAT,S.E.MARTIN,Z.MODRUSAN,S.SESHAGIRI
JRNL TITL ERK MUTATIONS AND AMPLIFICATION CONFER RESISTANCE TO
JRNL TITL 2 ERK-INHIBITOR THERAPY.
JRNL REF CLIN. CANCER RES. V. 24 4044 2018
JRNL REFN ISSN 1078-0432
JRNL PMID 29760222
JRNL DOI 10.1158/1078-0432.CCR-17-3674
REMARK 2
REMARK 2 RESOLUTION. 2.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.420
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 14184
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.550
REMARK 3 FREE R VALUE TEST SET COUNT : 645
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 57.0737 - 4.8902 0.97 2855 119 0.1907 0.2772
REMARK 3 2 4.8902 - 3.8818 0.97 2862 129 0.1932 0.2331
REMARK 3 3 3.8818 - 3.3912 0.94 2761 130 0.2388 0.2539
REMARK 3 4 3.3912 - 3.0811 0.89 2572 140 0.2648 0.3173
REMARK 3 5 3.0811 - 2.8603 0.85 2489 127 0.3080 0.3388
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.930
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 2820
REMARK 3 ANGLE : 0.517 3819
REMARK 3 CHIRALITY : 0.022 423
REMARK 3 PLANARITY : 0.003 489
REMARK 3 DIHEDRAL : 11.184 1073
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESI 2:108
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2343 3.9678 6.4777
REMARK 3 T TENSOR
REMARK 3 T11: 0.5478 T22: 0.2341
REMARK 3 T33: 0.2995 T12: -0.0548
REMARK 3 T13: 0.1264 T23: 0.0397
REMARK 3 L TENSOR
REMARK 3 L11: 0.8293 L22: 1.1720
REMARK 3 L33: 2.3720 L12: 0.1973
REMARK 3 L13: -0.1232 L23: 0.6039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0288 S12: 0.1702 S13: -0.3287
REMARK 3 S21: -0.3864 S22: -0.2077 S23: -0.0786
REMARK 3 S31: 0.6956 S32: -0.1261 S33: -0.2951
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESI 109:360)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0839 16.4367 26.3089
REMARK 3 T TENSOR
REMARK 3 T11: 0.0927 T22: 0.2190
REMARK 3 T33: 0.2170 T12: -0.0282
REMARK 3 T13: -0.0352 T23: -0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 2.6668 L22: 2.2184
REMARK 3 L33: 3.1141 L12: 0.7070
REMARK 3 L13: -1.5074 L23: -0.1652
REMARK 3 S TENSOR
REMARK 3 S11: 0.1797 S12: -0.0983 S13: -0.0424
REMARK 3 S21: 0.0464 S22: -0.1242 S23: 0.0553
REMARK 3 S31: -0.2522 S32: -0.1674 S33: 0.0107
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6D5Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1000234031.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03317
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57377
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.860
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 10% ISOPROPANOL, AND 0.1
REMARK 280 M HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 22.43500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.39500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.39500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.43500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.70000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 PRO A 176
REMARK 465 ASP A 177
REMARK 465 HIS A 178
REMARK 465 ASP A 179
REMARK 465 HIS A 180
REMARK 465 THR A 181
REMARK 465 GLY A 182
REMARK 465 PHE A 183
REMARK 465 TYR A 358
REMARK 465 ARG A 359
REMARK 465 SER A 360
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 ILE A 31 -71.40 -112.72
REMARK 500 ALA A 35 -127.33 55.68
REMARK 500 ARG A 148 -18.75 68.01
REMARK 500 ASN A 158 -164.06 -122.27
REMARK 500 THR A 160 31.35 -96.11
REMARK 500 ASP A 167 80.86 53.71
REMARK 500 THR A 206 -155.34 -116.58
REMARK 500 LEU A 294 46.57 -100.19
REMARK 500 ASP A 318 88.75 -162.60
REMARK 500 LYS A 330 118.77 -169.80
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6D5Y A 13 360 UNP P28482 MK01_HUMAN 13 360
SEQADV 6D5Y ASP A 169 UNP P28482 GLY 169 ENGINEERED MUTATION
SEQRES 1 A 348 MET VAL ARG GLY GLN VAL PHE ASP VAL GLY PRO ARG TYR
SEQRES 2 A 348 THR ASN LEU SER TYR ILE GLY GLU GLY ALA TYR GLY MET
SEQRES 3 A 348 VAL CYS SER ALA TYR ASP ASN VAL ASN LYS VAL ARG VAL
SEQRES 4 A 348 ALA ILE LYS LYS ILE SER PRO PHE GLU HIS GLN THR TYR
SEQRES 5 A 348 CYS GLN ARG THR LEU ARG GLU ILE LYS ILE LEU LEU ARG
SEQRES 6 A 348 PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN ASP ILE ILE
SEQRES 7 A 348 ARG ALA PRO THR ILE GLU GLN MET LYS ASP VAL TYR ILE
SEQRES 8 A 348 VAL GLN ASP LEU MET GLU THR ASP LEU TYR LYS LEU LEU
SEQRES 9 A 348 LYS THR GLN HIS LEU SER ASN ASP HIS ILE CYS TYR PHE
SEQRES 10 A 348 LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER
SEQRES 11 A 348 ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO SER ASN LEU
SEQRES 12 A 348 LEU LEU ASN THR THR CYS ASP LEU LYS ILE CYS ASP PHE
SEQRES 13 A 348 ASP LEU ALA ARG VAL ALA ASP PRO ASP HIS ASP HIS THR
SEQRES 14 A 348 GLY PHE LEU THR GLU TYR VAL ALA THR ARG TRP TYR ARG
SEQRES 15 A 348 ALA PRO GLU ILE MET LEU ASN SER LYS GLY TYR THR LYS
SEQRES 16 A 348 SER ILE ASP ILE TRP SER VAL GLY CYS ILE LEU ALA GLU
SEQRES 17 A 348 MET LEU SER ASN ARG PRO ILE PHE PRO GLY LYS HIS TYR
SEQRES 18 A 348 LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE LEU GLY SER
SEQRES 19 A 348 PRO SER GLN GLU ASP LEU ASN CYS ILE ILE ASN LEU LYS
SEQRES 20 A 348 ALA ARG ASN TYR LEU LEU SER LEU PRO HIS LYS ASN LYS
SEQRES 21 A 348 VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA ASP SER LYS
SEQRES 22 A 348 ALA LEU ASP LEU LEU ASP LYS MET LEU THR PHE ASN PRO
SEQRES 23 A 348 HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU ALA HIS PRO
SEQRES 24 A 348 TYR LEU GLU GLN TYR TYR ASP PRO SER ASP GLU PRO ILE
SEQRES 25 A 348 ALA GLU ALA PRO PHE LYS PHE ASP MET GLU LEU ASP ASP
SEQRES 26 A 348 LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE PHE GLU GLU
SEQRES 27 A 348 THR ALA ARG PHE GLN PRO GLY TYR ARG SER
HELIX 1 AA1 HIS A 61 PHE A 78 1 18
HELIX 2 AA2 LEU A 112 GLN A 119 1 8
HELIX 3 AA3 SER A 122 ALA A 143 1 22
HELIX 4 AA4 ALA A 195 LEU A 200 1 6
HELIX 5 AA5 LYS A 207 ASN A 224 1 18
HELIX 6 AA6 HIS A 232 GLY A 245 1 14
HELIX 7 AA7 ASN A 257 LEU A 267 1 11
HELIX 8 AA8 PRO A 274 PHE A 279 1 6
HELIX 9 AA9 ASP A 283 LEU A 294 1 12
HELIX 10 AB1 GLU A 303 ALA A 309 1 7
HELIX 11 AB2 HIS A 310 GLU A 314 5 5
HELIX 12 AB3 ASP A 318 GLU A 322 5 5
HELIX 13 AB4 PRO A 339 THR A 351 1 13
SHEET 1 AA1 5 TYR A 25 GLY A 32 0
SHEET 2 AA1 5 VAL A 39 ASP A 44 -1 O SER A 41 N SER A 29
SHEET 3 AA1 5 VAL A 49 ILE A 56 -1 O VAL A 51 N ALA A 42
SHEET 4 AA1 5 VAL A 101 ASP A 106 -1 O GLN A 105 N ALA A 52
SHEET 5 AA1 5 ILE A 86 ILE A 90 -1 N ASP A 88 O VAL A 104
SHEET 1 AA2 3 THR A 110 ASP A 111 0
SHEET 2 AA2 3 LEU A 155 LEU A 157 -1 O LEU A 157 N THR A 110
SHEET 3 AA2 3 LEU A 163 ILE A 165 -1 O LYS A 164 N LEU A 156
SHEET 1 AA3 2 VAL A 145 LEU A 146 0
SHEET 2 AA3 2 ARG A 172 VAL A 173 -1 O ARG A 172 N LEU A 146
CISPEP 1 GLY A 22 PRO A 23 0 1.80
CISPEP 2 GLY A 34 ALA A 35 0 0.77
CISPEP 3 PRO A 356 GLY A 357 0 0.02
CRYST1 44.870 65.400 116.790 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 0.022287 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015291 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008562 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
