HEADER TRANSFERASE 02-APR-01 1ID0
TITLE CRYSTAL STRUCTURE OF THE NUCLEOTIDE BOND CONFORMATION OF PHOQ KINASE
TITLE 2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOQ HISTIDINE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 SYNONYM: SENSOR PROTEIN PHOQ;
COMPND 6 EC: 2.7.1.37;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PAE4D;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PAED4QKD
KEYWDS HISTIDINE KINASE, PHOQ/PHOP, SIGNAL TRANSDUCTION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MARINA,C.MOTT,A.AUYZENBERG,C.D.WALDBURGER,W.A.HENDRICKSON
REVDAT 6 07-FEB-24 1ID0 1 REMARK LINK
REVDAT 5 01-FEB-17 1ID0 1 AUTHOR VERSN
REVDAT 4 24-FEB-09 1ID0 1 VERSN
REVDAT 3 01-APR-03 1ID0 1 JRNL
REVDAT 2 28-DEC-01 1ID0 1 JRNL
REVDAT 1 17-OCT-01 1ID0 0
JRNL AUTH A.MARINA,C.MOTT,A.AUYZENBERG,W.A.HENDRICKSON,C.D.WALDBURGER
JRNL TITL STRUCTURAL AND MUTATIONAL ANALYSIS OF THE PHOQ HISTIDINE
JRNL TITL 2 KINASE CATALYTIC DOMAIN. INSIGHT INTO THE REACTION
JRNL TITL 3 MECHANISM.
JRNL REF J.BIOL.CHEM. V. 276 41182 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11493605
JRNL DOI 10.1074/JBC.M106080200
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 956397.320
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 19159
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) : 0.199
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1400
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 : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1156
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 90
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.031
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1137
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 189
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.39000
REMARK 3 B22 (A**2) : -1.57000
REMARK 3 B33 (A**2) : 4.96000
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) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.11
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 5.200
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) : 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 : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 46.29
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 : ANP_MUTL.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ANP_MUTL.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ID0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013170.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19159
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 22.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.40
REMARK 200 R MERGE FOR SHELL (I) : 0.18600
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: MADSYS, MLPHARE, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: A CACODYLATE, PEG 1500, MG ACETATE, PH
REMARK 280 6.5, VAPORDIFFUSION, HANGING DROP, TEMPERATURE 277K, VAPOR
REMARK 280 DIFFUSION, HANGING DROP
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 21.75150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.88200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.50200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.88200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.75150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.50200
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 SER A 481
REMARK 465 ALA A 482
REMARK 465 PRO A 483
REMARK 465 LYS A 484
REMARK 465 ASP A 485
REMARK 465 GLU A 486
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 NE2 GLN A 376 O HOH A 189 2.16
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 GLU A 396 -38.84 -151.16
REMARK 500 THR A 405 -165.43 -118.25
REMARK 500 ARG A 434 56.54 -93.73
REMARK 500 ASP A 436 68.40 26.61
REMARK 500 LEU A 438 68.38 -68.19
REMARK 500 PRO A 440 -11.03 -48.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 700 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 84 O
REMARK 620 2 ASN A 385 OD1 78.9
REMARK 620 3 GLN A 442 OE1 90.7 107.9
REMARK 620 4 ANP A 487 O2G 86.4 153.7 93.9
REMARK 620 5 ANP A 487 O2B 161.4 119.3 79.9 78.3
REMARK 620 6 ANP A 487 O2A 109.6 91.4 154.5 73.0 76.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 487
DBREF 1ID0 A 335 486 UNP P23837 PHOQ_ECOLI 335 486
SEQRES 1 A 152 ARG GLU LEU HIS PRO VAL ALA PRO LEU LEU ASP ASN LEU
SEQRES 2 A 152 THR SER ALA LEU ASN LYS VAL TYR GLN ARG LYS GLY VAL
SEQRES 3 A 152 ASN ILE SER LEU ASP ILE SER PRO GLU ILE SER PHE VAL
SEQRES 4 A 152 GLY GLU GLN ASN ASP PHE VAL GLU VAL MET GLY ASN VAL
SEQRES 5 A 152 LEU ASP ASN ALA CYS LYS TYR CYS LEU GLU PHE VAL GLU
SEQRES 6 A 152 ILE SER ALA ARG GLN THR ASP GLU HIS LEU TYR ILE VAL
SEQRES 7 A 152 VAL GLU ASP ASP GLY PRO GLY ILE PRO LEU SER LYS ARG
SEQRES 8 A 152 GLU VAL ILE PHE ASP ARG GLY GLN ARG VAL ASP THR LEU
SEQRES 9 A 152 ARG PRO GLY GLN GLY VAL GLY LEU ALA VAL ALA ARG GLU
SEQRES 10 A 152 ILE THR GLU GLN TYR GLU GLY LYS ILE VAL ALA GLY GLU
SEQRES 11 A 152 SER MET LEU GLY GLY ALA ARG MET GLU VAL ILE PHE GLY
SEQRES 12 A 152 ARG GLN HIS SER ALA PRO LYS ASP GLU
HET MG A 700 1
HET ANP A 487 31
HETNAM MG MAGNESIUM ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 2 MG MG 2+
FORMUL 3 ANP C10 H17 N6 O12 P3
FORMUL 4 HOH *189(H2 O)
HELIX 1 1 VAL A 340 TYR A 355 1 16
HELIX 2 2 GLU A 375 CYS A 394 1 20
HELIX 3 3 PRO A 421 ARG A 425 5 5
HELIX 4 4 GLU A 426 ASP A 430 5 5
HELIX 5 5 GLY A 445 TYR A 456 1 12
SHEET 1 A 2 LEU A 337 PRO A 339 0
SHEET 2 A 2 SER A 371 VAL A 373 -1 O PHE A 372 N HIS A 338
SHEET 1 B 5 ASN A 361 ASP A 365 0
SHEET 2 B 5 PHE A 397 GLN A 404 1 N VAL A 398 O ASN A 361
SHEET 3 B 5 LEU A 409 ASP A 415 -1 N TYR A 410 O ARG A 403
SHEET 4 B 5 ALA A 470 PHE A 476 -1 O ALA A 470 N ASP A 415
SHEET 5 B 5 LYS A 459 GLU A 464 -1 O LYS A 459 N ILE A 475
LINK O HOH A 84 MG MG A 700 1555 1555 2.28
LINK OD1 ASN A 385 MG MG A 700 1555 1555 2.31
LINK OE1 GLN A 442 MG MG A 700 1555 1555 2.49
LINK O2G ANP A 487 MG MG A 700 1555 1555 2.51
LINK O2B ANP A 487 MG MG A 700 1555 1555 2.43
LINK O2A ANP A 487 MG MG A 700 1555 1555 2.76
SITE 1 AC1 4 HOH A 84 ASN A 385 GLN A 442 ANP A 487
SITE 1 AC2 20 HOH A 5 HOH A 16 HOH A 67 HOH A 126
SITE 2 AC2 20 HOH A 184 ASN A 385 ASN A 389 LYS A 392
SITE 3 AC2 20 TYR A 393 ASP A 415 GLY A 419 ILE A 420
SITE 4 AC2 20 ILE A 428 ARG A 434 ARG A 439 GLN A 442
SITE 5 AC2 20 GLY A 445 LEU A 446 ALA A 470 MG A 700
CRYST1 43.503 45.004 71.764 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 0.022987 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013935 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
