longtext: 4FLE-pdb

content
HEADER    HYDROLASE                               14-JUN-12   4FLE
TITLE     CRYSTAL STRUCTURE OF THE ESTERASE YQIA (YE3661) FROM YERSINIA
TITLE    2 ENTEROCOLITICA, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET YER85
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ESTERASE;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: YERSINIA ENTEROCOLITICA SUBSP. ENTEROCOLITICA;
SOURCE   3 ORGANISM_TAXID: 393305;
SOURCE   4 STRAIN: 8081;
SOURCE   5 GENE: YE3661;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS    STRUCTURAL GENOMICS, PSI-BIOLOGY, NORTHEAST STRUCTURAL GENOMICS
KEYWDS   2 CONSORTIUM, NESG, ALPHA-BETA PROTEIN, ROSSMANN FOLD, DISPLAYS
KEYWDS   3 ESTERASE ACTIVITY TOWARD PALMITOYL-COA AND PNP-BUTYRATE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    F.FOROUHAR,S.LEW,J.SEETHARAMAN,R.SHASTRY,E.KOHAN,M.MAGLAQUI,L.MAO,
AUTHOR   2 R.XIAO,T.B.ACTON,J.K.EVERETT,G.T.MONTELIONE,L.TONG,J.F.HUNT,
AUTHOR   3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,NORTHEAST STRUCTURAL
AUTHOR   4 GENOMICS CONSORTIUM (NESG)
REVDAT   1   08-AUG-12 4FLE    0
JRNL        AUTH   F.FOROUHAR,S.LEW,J.SEETHARAMAN,R.SHASTRY,E.KOHAN,M.MAGLAQUI,
JRNL        AUTH 2 L.MAO,R.XIAO,T.B.ACTON,J.K.EVERETT,G.T.MONTELIONE,L.TONG,
JRNL        AUTH 3 J.F.HUNT,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
JRNL        TITL   CRYSTAL STRUCTURE OF THE ESTERASE YQIA (YE3661) FROM
JRNL        TITL 2 YERSINIA ENTEROCOLITICA, NORTHEAST STRUCTURAL GENOMICS
JRNL        TITL 3 CONSORTIUM TARGET YER85 (CASP TARGET)
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.3
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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.06
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 161453.650
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.1
REMARK   3   NUMBER OF REFLECTIONS             : 22145
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) : 0.194
REMARK   3   FREE R VALUE                     : 0.249
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.400
REMARK   3   FREE R VALUE TEST SET COUNT      : 2078
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.60
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3109
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1860
REMARK   3   BIN FREE R VALUE                    : 0.2460
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 342
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1543
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 183
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 9.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.85000
REMARK   3    B22 (A**2) : -0.49000
REMARK   3    B33 (A**2) : 1.34000
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) : 0.22
REMARK   3   ESD FROM SIGMAA              (A) : 0.07
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) : 0.28
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.15
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.40
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.72
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        : 0.38
REMARK   3   BSOL        : 54.54
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 4FLE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB073044.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-MAR-12
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8
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) : 0.97911
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : MIRRORS
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   : 22631
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.060
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 6.900
REMARK 200  R MERGE                    (I) : 0.06700
REMARK 200  R SYM                      (I) : 0.05800
REMARK 200   FOR THE DATA SET  : 31.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.20700
REMARK 200  R SYM FOR SHELL            (I) : 0.21400
REMARK 200   FOR SHELL         : 7.350
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 43.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 10 MM TRIS (PH 7.5),
REMARK 280  100 MM SODIUM CHLORIDE, AND 5 MM DTT. CRYSTILLIZATION SOLUTION:
REMARK 280  100 MM TRIS (PH 8), 24% PEG 20K, AND 100 MM MG(NO3)2:6H2O. ,
REMARK 280  MICROBATCH UNDEROIL, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       27.52800
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.77150
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.52800
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.77150
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 300 REMARK: MONOMER ACCORDING TO STATIC LIGHT SCATTERING.
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     MSE A     1
REMARK 465     MSE A     2
REMARK 465     HIS A   198
REMARK 465     HIS A   199
REMARK 465     HIS A   200
REMARK 465     HIS A   201
REMARK 465     HIS A   202
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    SER A  13     -165.60   -104.31
REMARK 500    SER A  70     -125.94     56.74
REMARK 500    PHE A 175      102.98     75.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NESG-YER85   RELATED DB: TARGETTRACK
DBREF  4FLE A    1   194  UNP    A1JQU0   A1JQU0_YERE8     1    194
SEQADV 4FLE LEU A  195  UNP  A1JQU0              EXPRESSION TAG
SEQADV 4FLE GLU A  196  UNP  A1JQU0              EXPRESSION TAG
SEQADV 4FLE HIS A  197  UNP  A1JQU0              EXPRESSION TAG
SEQADV 4FLE HIS A  198  UNP  A1JQU0              EXPRESSION TAG
SEQADV 4FLE HIS A  199  UNP  A1JQU0              EXPRESSION TAG
SEQADV 4FLE HIS A  200  UNP  A1JQU0              EXPRESSION TAG
SEQADV 4FLE HIS A  201  UNP  A1JQU0              EXPRESSION TAG
SEQADV 4FLE HIS A  202  UNP  A1JQU0              EXPRESSION TAG
SEQRES   1 A  202  MSE MSE SER THR LEU LEU TYR ILE HIS GLY PHE ASN SER
SEQRES   2 A  202  SER PRO SER SER ALA LYS ALA THR THR PHE LYS SER TRP
SEQRES   3 A  202  LEU GLN GLN HIS HIS PRO HIS ILE GLU MSE GLN ILE PRO
SEQRES   4 A  202  GLN LEU PRO PRO TYR PRO ALA GLU ALA ALA GLU MSE LEU
SEQRES   5 A  202  GLU SER ILE VAL MSE ASP LYS ALA GLY GLN SER ILE GLY
SEQRES   6 A  202  ILE VAL GLY SER SER LEU GLY GLY TYR PHE ALA THR TRP
SEQRES   7 A  202  LEU SER GLN ARG PHE SER ILE PRO ALA VAL VAL VAL ASN
SEQRES   8 A  202  PRO ALA VAL ARG PRO PHE GLU LEU LEU SER ASP TYR LEU
SEQRES   9 A  202  GLY GLU ASN GLN ASN PRO TYR THR GLY GLN LYS TYR VAL
SEQRES  10 A  202  LEU GLU SER ARG HIS ILE TYR ASP LEU LYS ALA MSE GLN
SEQRES  11 A  202  ILE GLU LYS LEU GLU SER PRO ASP LEU LEU TRP LEU LEU
SEQRES  12 A  202  GLN GLN THR GLY ASP GLU VAL LEU ASP TYR ARG GLN ALA
SEQRES  13 A  202  VAL ALA TYR TYR THR PRO CYS ARG GLN THR VAL GLU SER
SEQRES  14 A  202  GLY GLY ASN HIS ALA PHE VAL GLY PHE ASP HIS TYR PHE
SEQRES  15 A  202  SER PRO ILE VAL THR PHE LEU GLY LEU ALA THR ALA LEU
SEQRES  16 A  202  GLU HIS HIS HIS HIS HIS HIS
MODRES 4FLE MSE A   36  MET  SELENOMETHIONINE
MODRES 4FLE MSE A   51  MET  SELENOMETHIONINE
MODRES 4FLE MSE A   57  MET  SELENOMETHIONINE
MODRES 4FLE MSE A  129  MET  SELENOMETHIONINE
HET    MSE  A  36       8
HET    MSE  A  51       8
HET    MSE  A  57       8
HET    MSE  A 129       8
HETNAM     MSE SELENOMETHIONINE
FORMUL   1  MSE    4(C5 H11 N O2 SE)
FORMUL   2  HOH   *183(H2 O)
HELIX    1   1 SER A   17  HIS A   31  1                                  15
HELIX    2   2 TYR A   44  ALA A   60  1                                  17
HELIX    3   3 LEU A   71  PHE A   83  1                                  13
HELIX    4   4 ARG A   95  LEU A  100  1                                   6
HELIX    5   5 SER A  101  LEU A  104  5                                   4
HELIX    6   6 GLU A  119  ALA A  128  1                                  10
HELIX    7   7 SER A  136  ASP A  138  5                                   3
HELIX    8   8 ASP A  152  TYR A  160  1                                   9
HELIX    9   9 GLY A  177  HIS A  180  5                                   4
HELIX   10  10 TYR A  181  GLY A  190  1                                  10
SHEET    1   A 6 GLU A  35  GLN A  37  0
SHEET    2   A 6 THR A   4  ILE A   8  1  N  LEU A   5   O  GLU A  35
SHEET    3   A 6 ILE A  64  SER A  69  1  O  GLY A  65   N  LEU A   6
SHEET    4   A 6 ALA A  87  VAL A  90  1  O  VAL A  88   N  ILE A  66
SHEET    5   A 6 LEU A 140  GLN A 145  1  O  LEU A 143   N  VAL A  89
SHEET    6   A 6 ARG A 164  GLU A 168  1  O  GLU A 168   N  GLN A 144
SHEET    1   B 2 GLY A 105  GLN A 108  0
SHEET    2   B 2 LYS A 115  LEU A 118 -1  O  TYR A 116   N  ASN A 107
LINK         C   GLU A  35                 N   MSE A  36     1555   1555  1.33
LINK         C   MSE A  36                 N   GLN A  37     1555   1555  1.33
LINK         C   GLU A  50                 N   MSE A  51     1555   1555  1.33
LINK         C   MSE A  51                 N   LEU A  52     1555   1555  1.33
LINK         C   VAL A  56                 N   MSE A  57     1555   1555  1.33
LINK         C   MSE A  57                 N   ASP A  58     1555   1555  1.33
LINK         C   ALA A 128                 N   MSE A 129     1555   1555  1.33
LINK         C   MSE A 129                 N   GLN A 130     1555   1555  1.33
CRYST1   55.056   79.543   46.060  90.00  90.00  90.00 P 21 21 2     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      0.018163  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012572  0.000000        0.00000
SCALE3      0.000000  0.000000  0.021711        0.00000
TER    1544      HIS A 197
MASTER      250    0    4   10    8    0    0    6 1726    1   40   16
END