HEADER STRUCTURAL PROTEIN 28-DEC-00 1IO1
TITLE CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHASE 1 FLAGELLIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: F41 L-TYPE (RESIDUES 54-451);
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 STRAIN: SJW 1660;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA-FOLIUM, FLAGELLIN, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.A.SAMATEY,K.IMADA,S.NAGASHIMA,F.VONDERVISZ,T.KUMASAKA,M.YAMAMOTO,
AUTHOR 2 K.NAMBA
REVDAT 4 27-DEC-23 1IO1 1 SEQADV
REVDAT 3 24-FEB-09 1IO1 1 VERSN
REVDAT 2 15-APR-03 1IO1 1 SOURCE DBREF SEQADV
REVDAT 1 04-APR-01 1IO1 0
JRNL AUTH F.A.SAMATEY,K.IMADA,S.NAGASHIMA,F.VONDERVISZ,T.KUMASAKA,
JRNL AUTH 2 M.YAMAMOTO,K.NAMBA
JRNL TITL STRUCTURE OF THE BACTERIAL FLAGELLAR PROTOFILAMENT AND
JRNL TITL 2 IMPLICATIONS FOR A SWITCH FOR SUPERCOILING
JRNL REF NATURE V. 410 331 2001
JRNL REFN ISSN 0028-0836
JRNL PMID 11268201
JRNL DOI 10.1038/35066504
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 29866
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2467
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 : 2880
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 354
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.47
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.523
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: NULL
REMARK 4
REMARK 4 1IO1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000005108.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : DIAMOND 111 + GERMANIUM 220
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121314
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 31.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.27200
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: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, NACL, GLYCEROL, ISO
REMARK 280 -PROPANOL, PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 289K
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 18.22000
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: 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 PHE A 53
REMARK 465 THR A 54
REMARK 465 ALA A 55
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 655 O HOH A 677 1.70
REMARK 500 OD1 ASN A 82 O HOH A 846 1.76
REMARK 500 O SER A 205 O HOH A 849 1.79
REMARK 500 OG SER A 310 O HOH A 854 1.93
REMARK 500 OE1 GLN A 89 O HOH A 848 1.94
REMARK 500 O HOH A 563 O HOH A 609 1.95
REMARK 500 O HOH A 826 O HOH A 846 1.97
REMARK 500 O HOH A 603 O HOH A 607 2.00
REMARK 500 OE1 GLU A 114 O HOH A 847 2.00
REMARK 500 O HOH A 659 O HOH A 667 2.01
REMARK 500 OH TYR A 230 O HOH A 851 2.03
REMARK 500 O HOH A 546 O HOH A 677 2.09
REMARK 500 O HOH A 565 O HOH A 724 2.09
REMARK 500 O HOH A 744 O HOH A 754 2.12
REMARK 500 O HOH A 589 O HOH A 677 2.15
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 THR A 193 -160.04 -104.15
REMARK 500 LEU A 197 104.18 -55.47
REMARK 500 ASP A 224 8.07 -69.36
REMARK 500 LYS A 251 3.55 -65.57
REMARK 500 THR A 252 -63.76 -107.12
REMARK 500 LYS A 348 106.40 72.21
REMARK 500 ALA A 351 -167.52 51.61
REMARK 500 ASP A 352 -46.19 168.32
REMARK 500 ASP A 353 44.91 -162.17
REMARK 500 THR A 355 160.67 88.35
REMARK 500 GLN A 393 78.07 -151.54
REMARK 500 PRO A 394 -136.15 -75.65
REMARK 500 ASP A 395 103.64 29.12
REMARK 500 GLU A 398 -168.34 -70.79
REMARK 500 ALA A 449 156.58 165.16
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IO1 A 53 450 UNP P06179 FLIC_SALTY 53 450
SEQADV 1IO1 ALA A 426 UNP P06179 GLY 426 CONFLICT
SEQRES 1 A 398 PHE THR ALA ASN ILE LYS GLY LEU THR GLN ALA SER ARG
SEQRES 2 A 398 ASN ALA ASN ASP GLY ILE SER ILE ALA GLN THR THR GLU
SEQRES 3 A 398 GLY ALA LEU ASN GLU ILE ASN ASN ASN LEU GLN ARG VAL
SEQRES 4 A 398 ARG GLU LEU ALA VAL GLN SER ALA ASN SER THR ASN SER
SEQRES 5 A 398 GLN SER ASP LEU ASP SER ILE GLN ALA GLU ILE THR GLN
SEQRES 6 A 398 ARG LEU ASN GLU ILE ASP ARG VAL SER GLY GLN THR GLN
SEQRES 7 A 398 PHE ASN GLY VAL LYS VAL LEU ALA GLN ASP ASN THR LEU
SEQRES 8 A 398 THR ILE GLN VAL GLY ALA ASN ASP GLY GLU THR ILE ASP
SEQRES 9 A 398 ILE ASP LEU LYS GLN ILE ASN SER GLN THR LEU GLY LEU
SEQRES 10 A 398 ASP THR LEU ASN VAL GLN GLN LYS TYR LYS VAL SER ASP
SEQRES 11 A 398 THR ALA ALA THR VAL THR GLY TYR ALA ASP THR THR ILE
SEQRES 12 A 398 ALA LEU ASP ASN SER THR PHE LYS ALA SER ALA THR GLY
SEQRES 13 A 398 LEU GLY GLY THR ASP GLN LYS ILE ASP GLY ASP LEU LYS
SEQRES 14 A 398 PHE ASP ASP THR THR GLY LYS TYR TYR ALA LYS VAL THR
SEQRES 15 A 398 VAL THR GLY GLY THR GLY LYS ASP GLY TYR TYR GLU VAL
SEQRES 16 A 398 SER VAL ASP LYS THR ASN GLY GLU VAL THR LEU ALA GLY
SEQRES 17 A 398 GLY ALA THR SER PRO LEU THR GLY GLY LEU PRO ALA THR
SEQRES 18 A 398 ALA THR GLU ASP VAL LYS ASN VAL GLN VAL ALA ASN ALA
SEQRES 19 A 398 ASP LEU THR GLU ALA LYS ALA ALA LEU THR ALA ALA GLY
SEQRES 20 A 398 VAL THR GLY THR ALA SER VAL VAL LYS MET SER TYR THR
SEQRES 21 A 398 ASP ASN ASN GLY LYS THR ILE ASP GLY GLY LEU ALA VAL
SEQRES 22 A 398 LYS VAL GLY ASP ASP TYR TYR SER ALA THR GLN ASN LYS
SEQRES 23 A 398 ASP GLY SER ILE SER ILE ASN THR THR LYS TYR THR ALA
SEQRES 24 A 398 ASP ASP GLY THR SER LYS THR ALA LEU ASN LYS LEU GLY
SEQRES 25 A 398 GLY ALA ASP GLY LYS THR GLU VAL VAL SER ILE GLY GLY
SEQRES 26 A 398 LYS THR TYR ALA ALA SER LYS ALA GLU GLY HIS ASN PHE
SEQRES 27 A 398 LYS ALA GLN PRO ASP LEU ALA GLU ALA ALA ALA THR THR
SEQRES 28 A 398 THR GLU ASN PRO LEU GLN LYS ILE ASP ALA ALA LEU ALA
SEQRES 29 A 398 GLN VAL ASP THR LEU ARG SER ASP LEU ALA ALA VAL GLN
SEQRES 30 A 398 ASN ARG PHE ASN SER ALA ILE THR ASN LEU GLY ASN THR
SEQRES 31 A 398 VAL ASN ASN LEU THR SER ALA ARG
FORMUL 2 HOH *354(H2 O)
HELIX 1 1 ILE A 57 ALA A 99 1 43
HELIX 2 2 SER A 104 THR A 129 1 26
HELIX 3 3 ASN A 199 PHE A 202 5 4
HELIX 4 4 ALA A 206 GLY A 210 5 5
HELIX 5 5 LEU A 288 ALA A 298 1 11
HELIX 6 6 ALA A 382 GLU A 386 1 5
HELIX 7 7 ASN A 406 SER A 448 1 43
SHEET 1 A 2 ASN A 141 GLN A 146 0
SHEET 2 A 2 THR A 154 LEU A 159 -1 O ILE A 155 N ILE A 145
SHEET 1 B 5 LYS A 179 ALA A 184 0
SHEET 2 B 5 ALA A 304 THR A 312 -1 N LYS A 308 O THR A 183
SHEET 3 B 5 THR A 318 VAL A 327 -1 O ILE A 319 N TYR A 311
SHEET 4 B 5 ASP A 330 GLN A 336 -1 O ASP A 330 N VAL A 327
SHEET 5 B 5 ILE A 342 ILE A 344 -1 N SER A 343 O THR A 335
SHEET 1 C 2 TYR A 190 ALA A 196 0
SHEET 2 C 2 ASN A 280 ALA A 284 -1 N VAL A 281 O ILE A 195
SHEET 1 D 4 VAL A 256 LEU A 258 0
SHEET 2 D 4 GLY A 243 VAL A 249 -1 N SER A 248 O THR A 257
SHEET 3 D 4 TYR A 229 THR A 236 -1 O TYR A 229 N VAL A 247
SHEET 4 D 4 ASP A 213 ILE A 216 -1 O ASP A 213 N THR A 236
SHEET 1 E 5 VAL A 256 LEU A 258 0
SHEET 2 E 5 GLY A 243 VAL A 249 -1 N SER A 248 O THR A 257
SHEET 3 E 5 TYR A 229 THR A 236 -1 O TYR A 229 N VAL A 247
SHEET 4 E 5 LEU A 220 PHE A 222 -1 O LYS A 221 N TYR A 230
SHEET 5 E 5 GLU A 276 VAL A 278 -1 O GLU A 276 N PHE A 222
SHEET 1 F 3 ASN A 361 GLY A 364 0
SHEET 2 F 3 THR A 370 ILE A 375 -1 O THR A 370 N GLY A 364
SHEET 3 F 3 LYS A 378 ALA A 381 -1 N LYS A 378 O ILE A 375
CRYST1 51.750 36.440 118.350 90.00 91.15 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 0.019324 0.000000 0.000388 0.00000
SCALE2 0.000000 0.027442 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008451 0.00000
(ATOM LINES ARE NOT SHOWN.)
END