HEADER HYDROLASE, SIGNALING PROTEIN 11-OCT-00 1G1H
TITLE CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B
TITLE 2 COMPLEXED WITH A BIS-PHOSPHORYLATED PEPTIDE (ETD(PTR)(PTR)
TITLE 3 RKGGKGLL) FROM THE INSULIN RECEPTOR KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TYROSINE PHOSPHATASE 1B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: PTP1B, PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR
COMPND 6 TYPE 1;
COMPND 7 EC: 3.1.3.48;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: BI-PHOSPHORYLATED PEPTIDE FROM THE INSULIN
COMPND 12 RECEPTOR KINASE;
COMPND 13 CHAIN: B;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-19B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: SEQUENCE FROM THE ACTIVATION SEGMENT OF THE
SOURCE 12 INSULIN RECPTOR KINASE
KEYWDS HYDROLASE (PHOSPHORYLATION), TYROSINE PHOSPHATASE, PEPTIDE
KEYWDS 2 COMPLEX, HYDROLASE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SALMEEN,J.N.ANDERSEN,M.P.MYERS,N.K.TONKS,D.BARFORD
REVDAT 4 24-FEB-09 1G1H 1 VERSN
REVDAT 3 01-APR-03 1G1H 1 JRNL
REVDAT 2 17-SEP-01 1G1H 1 AUTHOR JRNL
REVDAT 1 17-JAN-01 1G1H 0
JRNL AUTH A.SALMEEN,J.N.ANDERSEN,M.P.MYERS,N.K.TONKS,
JRNL AUTH 2 D.BARFORD
JRNL TITL MOLECULAR BASIS FOR THE DEPHOSPHORYLATION OF THE
JRNL TITL 2 ACTIVATION SEGMENT OF THE INSULIN RECEPTOR BY
JRNL TITL 3 PROTEIN TYROSINE PHOSPHATASE 1B.
JRNL REF MOL.CELL V. 6 1401 2000
JRNL REFN ISSN 1097-2765
JRNL PMID 11163213
JRNL DOI 10.1016/S1097-2765(00)00137-4
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : CNS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 16411
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) : 0.207
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 830
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 : 2501
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.40
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) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 2.50
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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: NULL
REMARK 4
REMARK 4 1G1H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-00.
REMARK 100 THE RCSB ID CODE IS RCSB012115.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.4880
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 16411
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.3000
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) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.13200
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MGCL2, DITHIOTHREITOL,
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 302.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 45.05600
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 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 GLU B 1159
REMARK 465 GLY B 1167
REMARK 465 LYS B 1168
REMARK 465 GLY B 1169
REMARK 465 LEU B 1170
REMARK 465 LEU B 1171
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 B1165 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 GLU A 2 119.43 67.92
REMARK 500 ASP A 63 -74.64 -57.35
REMARK 500 PRO A 206 -8.70 -59.50
REMARK 500 ALA A 215 -137.75 -146.33
REMARK 500 ASP A 240 76.77 -171.17
REMARK 500 ILE A 261 114.81 84.66
REMARK 500 GLU A 297 36.73 -79.58
REMARK 500 LYS B1165 74.88 -109.45
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1G1H A 1 298 UNP P18031 PTN1_HUMAN 1 298
DBREF 1G1H B 1159 1171 PDB 1G1H 1G1H 1159 1171
SEQADV 1G1H ALA A 215 UNP P18031 CYS 215 ENGINEERED
SEQRES 1 A 298 MET GLU MET GLU LYS GLU PHE GLU GLN ILE ASP LYS SER
SEQRES 2 A 298 GLY SER TRP ALA ALA ILE TYR GLN ASP ILE ARG HIS GLU
SEQRES 3 A 298 ALA SER ASP PHE PRO CYS ARG VAL ALA LYS LEU PRO LYS
SEQRES 4 A 298 ASN LYS ASN ARG ASN ARG TYR ARG ASP VAL SER PRO PHE
SEQRES 5 A 298 ASP HIS SER ARG ILE LYS LEU HIS GLN GLU ASP ASN ASP
SEQRES 6 A 298 TYR ILE ASN ALA SER LEU ILE LYS MET GLU GLU ALA GLN
SEQRES 7 A 298 ARG SER TYR ILE LEU THR GLN GLY PRO LEU PRO ASN THR
SEQRES 8 A 298 CYS GLY HIS PHE TRP GLU MET VAL TRP GLU GLN LYS SER
SEQRES 9 A 298 ARG GLY VAL VAL MET LEU ASN ARG VAL MET GLU LYS GLY
SEQRES 10 A 298 SER LEU LYS CYS ALA GLN TYR TRP PRO GLN LYS GLU GLU
SEQRES 11 A 298 LYS GLU MET ILE PHE GLU ASP THR ASN LEU LYS LEU THR
SEQRES 12 A 298 LEU ILE SER GLU ASP ILE LYS SER TYR TYR THR VAL ARG
SEQRES 13 A 298 GLN LEU GLU LEU GLU ASN LEU THR THR GLN GLU THR ARG
SEQRES 14 A 298 GLU ILE LEU HIS PHE HIS TYR THR THR TRP PRO ASP PHE
SEQRES 15 A 298 GLY VAL PRO GLU SER PRO ALA SER PHE LEU ASN PHE LEU
SEQRES 16 A 298 PHE LYS VAL ARG GLU SER GLY SER LEU SER PRO GLU HIS
SEQRES 17 A 298 GLY PRO VAL VAL VAL HIS ALA SER ALA GLY ILE GLY ARG
SEQRES 18 A 298 SER GLY THR PHE CYS LEU ALA ASP THR CYS LEU LEU LEU
SEQRES 19 A 298 MET ASP LYS ARG LYS ASP PRO SER SER VAL ASP ILE LYS
SEQRES 20 A 298 LYS VAL LEU LEU GLU MET ARG LYS PHE ARG MET GLY LEU
SEQRES 21 A 298 ILE GLN THR ALA ASP GLN LEU ARG PHE SER TYR LEU ALA
SEQRES 22 A 298 VAL ILE GLU GLY ALA LYS PHE ILE MET GLY ASP SER SER
SEQRES 23 A 298 VAL GLN ASP GLN TRP LYS GLU LEU SER HIS GLU ASP
SEQRES 1 B 13 GLU THR ASP PTR PTR ARG LYS GLY GLY LYS GLY LEU LEU
MODRES 1G1H PTR B 1162 TYR O-PHOSPHOTYROSINE
MODRES 1G1H PTR B 1163 TYR O-PHOSPHOTYROSINE
HET PTR B1162 16
HET PTR B1163 16
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR 2(C9 H12 N O6 P)
FORMUL 3 HOH *116(H2 O)
HELIX 1 1 GLU A 2 GLY A 14 1 13
HELIX 2 2 SER A 15 ALA A 27 1 13
HELIX 3 3 LEU A 37 ASN A 44 5 8
HELIX 4 4 THR A 91 GLN A 102 1 12
HELIX 5 5 SER A 187 GLY A 202 1 16
HELIX 6 6 ILE A 219 ARG A 238 1 20
HELIX 7 7 ASP A 240 VAL A 244 5 5
HELIX 8 8 ASP A 245 ARG A 254 1 10
HELIX 9 9 THR A 263 MET A 282 1 20
HELIX 10 10 SER A 286 HIS A 296 1 11
SHEET 1 A 8 ALA A 69 MET A 74 0
SHEET 2 A 8 ARG A 79 THR A 84 -1 O ARG A 79 N MET A 74
SHEET 3 A 8 VAL A 211 HIS A 214 1 O VAL A 211 N ILE A 82
SHEET 4 A 8 GLY A 106 MET A 109 1 O GLY A 106 N VAL A 212
SHEET 5 A 8 THR A 168 TYR A 176 1 O LEU A 172 N VAL A 107
SHEET 6 A 8 TYR A 153 ASN A 162 -1 O THR A 154 N HIS A 175
SHEET 7 A 8 LEU A 140 ILE A 149 -1 O LYS A 141 N GLU A 161
SHEET 8 A 8 MET A 133 PHE A 135 -1 O MET A 133 N LEU A 142
SHEET 1 B 2 MET A 114 GLU A 115 0
SHEET 2 B 2 SER A 118 LEU A 119 -1 O SER A 118 N GLU A 115
LINK C ASP B1161 N PTR B1162 1555 1555 1.34
LINK C PTR B1162 N PTR B1163 1555 1555 1.34
LINK C PTR B1163 N ARG B1164 1555 1555 1.33
CRYST1 44.827 90.112 53.591 90.00 99.21 90.00 P 1 21 1 2
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 0.022310 0.000000 0.003620 0.00000
SCALE2 0.000000 0.011100 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018900 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
