HEADER TRANSFERASE (PHOSPHOTRANSFERASE) 02-JAN-95 1IRK
TITLE CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE
TITLE 2 HUMAN INSULIN RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN RECEPTOR TYROSINE KINASE DOMAIN;
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 TRANSFERASE (PHOSPHOTRANSFERASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR S.R.HUBBARD,L.WEI,L.ELLIS,W.A.HENDRICKSON
REVDAT 2 24-FEB-09 1IRK 1 VERSN
REVDAT 1 27-FEB-95 1IRK 0
JRNL AUTH S.R.HUBBARD,L.WEI,L.ELLIS,W.A.HENDRICKSON
JRNL TITL CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF
JRNL TITL 2 THE HUMAN INSULIN RECEPTOR.
JRNL REF NATURE V. 372 746 1994
JRNL REFN ISSN 0028-0836
JRNL PMID 7997262
JRNL DOI 10.1038/372746A0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.WEI,S.R.HUBBARD,W.A.HENDRICKSON,L.ELLIS
REMARK 1 TITL EXPRESSION, CHARACTERIZATION AND CRYSTALLIZATION
REMARK 1 TITL 2 OF THE CATALYTIC CORE OF THE HUMAN INSULIN
REMARK 1 TITL 3 RECEPTOR PROTEIN TYROSINE KINASE DOMAIN
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.EBINA,L.ELLIS,K.JARNAGIN,M.EDERY,L.GRAF,
REMARK 1 AUTH 2 E.CLAUSER,J.-H.OU,F.MASIARZ,Y.W.KAN,I.D.GOLDFINE,
REMARK 1 AUTH 3 R.A.ROTH,W.J.RUTTER
REMARK 1 TITL THE HUMAN INSULIN RECEPTOR CDNA: THE STRUCTURAL
REMARK 1 TITL 2 BASIS FOR HORMONE-ACTIVATED TRANSMEMBRANE
REMARK 1 TITL 3 SIGNALLING
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 40 747 1985
REMARK 1 REFN ISSN 0092-8674
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 34747
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) : 0.196
REMARK 3 FREE R VALUE : 0.232
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 : 2380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 199
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.60
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.58
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.46
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) : 1.660 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.720 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.930 ; 1.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.130 ; 2.000
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 1IRK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 : 37359
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 (%) : 93.9
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
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 27.01500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.59000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.49500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.59000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.01500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.49500
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 VAL A 978
REMARK 465 PHE A 979
REMARK 465 PRO A 980
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 PHE A 984 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 988 CG CD OE1 OE2
REMARK 470 GLU A1094 CG CD OE1 OE2
REMARK 470 GLU A1096 CG CD OE1 OE2
REMARK 470 MET A1153 CG SD CE
REMARK 470 THR A1154 OG1 CG2
REMARK 470 ARG A1155 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1156 CG OD1 OD2
REMARK 470 ILE A1157 CG1 CG2 CD1
REMARK 470 GLU A1159 CG CD OE1 OE2
REMARK 470 ARG A1237 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 ARG A1131 -13.51 77.45
REMARK 500 ASP A1132 41.00 -145.75
REMARK 500 MET A1153 70.88 -113.07
REMARK 500 ASP A1156 -148.23 -173.00
REMARK 500 LYS A1168 -129.09 -93.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE MODEL INCLUDES TWO ETHYL MERCURY GROUPS (EMC)
REMARK 600 WHICH ARE COVALENTLY BOUND TO CYS 1056 AND CYS 1234.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMC A 500
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMC A 501
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 RESIDUE NUMBERING IS ACCORDING TO EBINA ET AL.
REMARK 999 (REFERENCE 2).
DBREF 1IRK A 978 1283 UNP P06213 INSR_HUMAN 1005 1310
SEQADV 1IRK SER A 981 UNP P06213 CYS 1008 CONFLICT
SEQADV 1IRK PHE A 984 UNP P06213 TYR 1011 CONFLICT
SEQRES 1 A 306 VAL PHE PRO SER SER VAL PHE VAL PRO ASP GLU TRP GLU
SEQRES 2 A 306 VAL SER ARG GLU LYS ILE THR LEU LEU ARG GLU LEU GLY
SEQRES 3 A 306 GLN GLY SER PHE GLY MET VAL TYR GLU GLY ASN ALA ARG
SEQRES 4 A 306 ASP ILE ILE LYS GLY GLU ALA GLU THR ARG VAL ALA VAL
SEQRES 5 A 306 LYS THR VAL ASN GLU SER ALA SER LEU ARG GLU ARG ILE
SEQRES 6 A 306 GLU PHE LEU ASN GLU ALA SER VAL MET LYS GLY PHE THR
SEQRES 7 A 306 CYS HIS HIS VAL VAL ARG LEU LEU GLY VAL VAL SER LYS
SEQRES 8 A 306 GLY GLN PRO THR LEU VAL VAL MET GLU LEU MET ALA HIS
SEQRES 9 A 306 GLY ASP LEU LYS SER TYR LEU ARG SER LEU ARG PRO GLU
SEQRES 10 A 306 ALA GLU ASN ASN PRO GLY ARG PRO PRO PRO THR LEU GLN
SEQRES 11 A 306 GLU MET ILE GLN MET ALA ALA GLU ILE ALA ASP GLY MET
SEQRES 12 A 306 ALA TYR LEU ASN ALA LYS LYS PHE VAL HIS ARG ASP LEU
SEQRES 13 A 306 ALA ALA ARG ASN CYS MET VAL ALA HIS ASP PHE THR VAL
SEQRES 14 A 306 LYS ILE GLY ASP PHE GLY MET THR ARG ASP ILE TYR GLU
SEQRES 15 A 306 THR ASP TYR TYR ARG LYS GLY GLY LYS GLY LEU LEU PRO
SEQRES 16 A 306 VAL ARG TRP MET ALA PRO GLU SER LEU LYS ASP GLY VAL
SEQRES 17 A 306 PHE THR THR SER SER ASP MET TRP SER PHE GLY VAL VAL
SEQRES 18 A 306 LEU TRP GLU ILE THR SER LEU ALA GLU GLN PRO TYR GLN
SEQRES 19 A 306 GLY LEU SER ASN GLU GLN VAL LEU LYS PHE VAL MET ASP
SEQRES 20 A 306 GLY GLY TYR LEU ASP GLN PRO ASP ASN CYS PRO GLU ARG
SEQRES 21 A 306 VAL THR ASP LEU MET ARG MET CYS TRP GLN PHE ASN PRO
SEQRES 22 A 306 LYS MET ARG PRO THR PHE LEU GLU ILE VAL ASN LEU LEU
SEQRES 23 A 306 LYS ASP ASP LEU HIS PRO SER PHE PRO GLU VAL SER PHE
SEQRES 24 A 306 PHE HIS SER GLU GLU ASN LYS
HET EMC A 500 3
HET EMC A 501 3
HETNAM EMC ETHYL MERCURY ION
FORMUL 2 EMC 2(C2 H5 HG 1+)
FORMUL 4 HOH *199(H2 O)
HELIX 1 C LEU A 1038 MET A 1051 1 14
HELIX 2 D LEU A 1084 SER A 1090 1 7
HELIX 3 E LEU A 1106 ALA A 1125 1 20
HELIX 4 EF PRO A 1178 ASP A 1183 1 6
HELIX 5 F THR A 1188 SER A 1204 1 17
HELIX 6 G ASN A 1215 MET A 1223 1 9
HELIX 7 H GLU A 1236 CYS A 1245 1 10
HELIX 8 I PHE A 1256 LEU A 1263 1 8
HELIX 9 J PHE A 1271 VAL A 1274 1 4
SHEET 1 A 5 LEU A1062 VAL A1066 0
SHEET 2 A 5 LEU A1073 GLU A1077 -1 N VAL A1075 O LEU A1063
SHEET 3 A 5 GLU A1022 LYS A1030 -1 N LYS A1030 O VAL A1074
SHEET 4 A 5 MET A1009 ILE A1019 -1 N ALA A1015 O THR A1025
SHEET 5 A 5 ILE A 996 GLN A1004 -1 N ARG A1000 O GLU A1012
SHEET 1 B 2 CYS A1138 VAL A1140 0
SHEET 2 B 2 VAL A1146 ILE A1148 -1 N LYS A1147 O MET A1139
SHEET 1 C 2 TYR A1163 ARG A1164 0
SHEET 2 C 2 LEU A1170 LEU A1171 -1 N LEU A1171 O TYR A1163
LINK HG EMC A 500 SG CYS A1056 1555 1555 2.38
LINK HG EMC A 501 SG CYS A1234 1555 1555 2.37
CISPEP 1 GLN A 1070 PRO A 1071 0 -0.47
SITE 1 AC1 3 CYS A1056 PHE A1276 SER A1279
SITE 1 AC2 2 MET A1109 CYS A1234
CRYST1 54.030 72.990 89.180 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 0.018508 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013701 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011213 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
