longtext: 7z2x-pdb

content
HEADER    HYDROLASE                               01-MAR-22   7Z2X
TITLE     WILD-TYPE FERULIC ACID ESTERASE FROM LACTOBACILLUS BUCHNERI
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: FERULIC ACID ESTERASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 EC: 3.1.1.73;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: LENTILACTOBACILLUS BUCHNERI;
SOURCE   3 ORGANISM_TAXID: 1581;
SOURCE   4 GENE: FAEA;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 37762;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: T1;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS    FERULIC ACID ESTERASE, LACTOBACILLUS BUCHNERI, WILD TYPE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.K.MOGODINIYAI,T.REICHENBACH,D.C.KALYANI,M.M.KESKITALO,C.DIVNE
REVDAT   1   30-NOV-22 7Z2X    0
JRNL        AUTH   K.K.MOGODINIYAI,T.REICHENBACH,D.C.KALYANI,A.JIMENEZ QUERO,
JRNL        AUTH 2 M.M.KESKITALO,F.VILAPLANA,C.DIVNE
JRNL        TITL   WILD-TYPE FERULIC ACID ESTERASE FROM LACTOBACILLUS BUCHNERI
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.15.2_3472: ???)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.93
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.6
REMARK   3   NUMBER OF REFLECTIONS             : 155652
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183
REMARK   3   R VALUE            (WORKING SET) : 0.182
REMARK   3   FREE R VALUE                     : 0.211
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.280
REMARK   3   FREE R VALUE TEST SET COUNT      : 1986
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 30.9340 -  3.6135    0.95    11136   142  0.1564 0.1457
REMARK   3     2  3.6135 -  2.8688    0.95    11119   144  0.1662 0.1887
REMARK   3     3  2.8688 -  2.5063    0.96    11184   147  0.1803 0.2423
REMARK   3     4  2.5063 -  2.2773    0.96    11245   139  0.1799 0.2273
REMARK   3     5  2.2773 -  2.1141    0.95    11181   150  0.1723 0.2078
REMARK   3     6  2.1141 -  1.9895    0.95    11197   126  0.1793 0.2338
REMARK   3     7  1.9895 -  1.8898    0.94    11046   158  0.1903 0.2257
REMARK   3     8  1.8898 -  1.8076    0.94    11072   145  0.1976 0.2332
REMARK   3     9  1.8076 -  1.7380    0.94    10943   136  0.2067 0.2471
REMARK   3    10  1.7380 -  1.6780    0.93    10906   144  0.2198 0.2839
REMARK   3    11  1.6780 -  1.6256    0.92    10876   135  0.2239 0.2460
REMARK   3    12  1.6256 -  1.5791    0.91    10660   138  0.2320 0.2552
REMARK   3    13  1.5791 -  1.5375    0.90    10583   153  0.2444 0.2564
REMARK   3    14  1.5375 -  1.5000    0.90    10518   129  0.2640 0.3002
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.000
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 14.40
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  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.005           8582
REMARK   3   ANGLE     :  0.808          11581
REMARK   3   CHIRALITY :  0.051           1230
REMARK   3   PLANARITY :  0.005           1525
REMARK   3   DIHEDRAL  : 16.205           5055
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 7Z2X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAR-22.
REMARK 100 THE DEPOSITION ID IS D_1292119942.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-20
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : DIAMOND
REMARK 200  BEAMLINE                       : I24
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96852
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XDS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 155659
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.934
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.5
REMARK 200  DATA REDUNDANCY                : 2.800
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.60
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.0
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   FOR SHELL         : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: L. BUCHNERI FAE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 0.2 M NACL, 25%
REMARK 280  P3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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     MET A   -21
REMARK 465     HIS A   -20
REMARK 465     HIS A   -19
REMARK 465     HIS A   -18
REMARK 465     HIS A   -17
REMARK 465     HIS A   -16
REMARK 465     HIS A   -15
REMARK 465     SER A   -14
REMARK 465     SER A   -13
REMARK 465     GLY A   -12
REMARK 465     VAL A   -11
REMARK 465     ASP A   -10
REMARK 465     LEU A    -9
REMARK 465     GLY A    -8
REMARK 465     THR A    -7
REMARK 465     GLU A    -6
REMARK 465     LYS A   260
REMARK 465     MET B   -21
REMARK 465     HIS B   -20
REMARK 465     HIS B   -19
REMARK 465     HIS B   -18
REMARK 465     HIS B   -17
REMARK 465     HIS B   -16
REMARK 465     HIS B   -15
REMARK 465     SER B   -14
REMARK 465     SER B   -13
REMARK 465     GLY B   -12
REMARK 465     VAL B   -11
REMARK 465     ASP B   -10
REMARK 465     LEU B    -9
REMARK 465     GLY B    -8
REMARK 465     THR B    -7
REMARK 465     GLU B    -6
REMARK 465     ASN B    -5
REMARK 465     LEU B    -4
REMARK 465     TYR B    -3
REMARK 465     PHE B    -2
REMARK 465     GLN B    -1
REMARK 465     LYS B   260
REMARK 465     MET C   -21
REMARK 465     HIS C   -20
REMARK 465     HIS C   -19
REMARK 465     HIS C   -18
REMARK 465     HIS C   -17
REMARK 465     HIS C   -16
REMARK 465     HIS C   -15
REMARK 465     SER C   -14
REMARK 465     SER C   -13
REMARK 465     GLY C   -12
REMARK 465     VAL C   -11
REMARK 465     ASP C   -10
REMARK 465     LEU C    -9
REMARK 465     GLY C    -8
REMARK 465     THR C    -7
REMARK 465     GLU C    -6
REMARK 465     LYS C   260
REMARK 465     MET D   -21
REMARK 465     HIS D   -20
REMARK 465     HIS D   -19
REMARK 465     HIS D   -18
REMARK 465     HIS D   -17
REMARK 465     HIS D   -16
REMARK 465     HIS D   -15
REMARK 465     SER D   -14
REMARK 465     SER D   -13
REMARK 465     GLY D   -12
REMARK 465     VAL D   -11
REMARK 465     ASP D   -10
REMARK 465     LEU D    -9
REMARK 465     GLY D    -8
REMARK 465     THR D    -7
REMARK 465     GLU D    -6
REMARK 465     ASN D    -5
REMARK 465     LEU D    -4
REMARK 465     TYR D    -3
REMARK 465     PHE D    -2
REMARK 465     GLN D    -1
REMARK 465     LYS D   260
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  44     -175.52     53.50
REMARK 500    SER A 114     -127.14     62.03
REMARK 500    ALA A 140       47.72    -88.85
REMARK 500    GLN A 236       41.28   -105.86
REMARK 500    GLU B  44     -175.49     54.24
REMARK 500    SER B 114     -126.63     62.53
REMARK 500    GLN B 236       42.18   -107.47
REMARK 500    GLU C  44     -176.67     56.63
REMARK 500    SER C 114     -127.71     63.20
REMARK 500    ALA C 140       48.56    -87.59
REMARK 500    GLU D  44     -172.77     54.70
REMARK 500    SER D 114     -126.10     62.63
REMARK 500    ALA D 140       49.99    -84.63
REMARK 500    GLN D 236       41.66   -105.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH C 518        DISTANCE =  6.09 ANGSTROMS
DBREF  7Z2X A    1   260  UNP    D7RU28   D7RU28_LENBU     1    260
DBREF  7Z2X B    1   260  UNP    D7RU28   D7RU28_LENBU     1    260
DBREF  7Z2X C    1   260  UNP    D7RU28   D7RU28_LENBU     1    260
DBREF  7Z2X D    1   260  UNP    D7RU28   D7RU28_LENBU     1    260
SEQADV 7Z2X MET A  -21  UNP  D7RU28              INITIATING METHIONINE
SEQADV 7Z2X HIS A  -20  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS A  -19  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS A  -18  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS A  -17  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS A  -16  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS A  -15  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER A  -14  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER A  -13  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLY A  -12  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X VAL A  -11  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X ASP A  -10  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X LEU A   -9  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLY A   -8  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X THR A   -7  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLU A   -6  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X ASN A   -5  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X LEU A   -4  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X TYR A   -3  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X PHE A   -2  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLN A   -1  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER A    0  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X MET B  -21  UNP  D7RU28              INITIATING METHIONINE
SEQADV 7Z2X HIS B  -20  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS B  -19  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS B  -18  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS B  -17  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS B  -16  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS B  -15  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER B  -14  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER B  -13  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLY B  -12  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X VAL B  -11  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X ASP B  -10  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X LEU B   -9  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLY B   -8  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X THR B   -7  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLU B   -6  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X ASN B   -5  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X LEU B   -4  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X TYR B   -3  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X PHE B   -2  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLN B   -1  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER B    0  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X MET C  -21  UNP  D7RU28              INITIATING METHIONINE
SEQADV 7Z2X HIS C  -20  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS C  -19  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS C  -18  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS C  -17  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS C  -16  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS C  -15  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER C  -14  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER C  -13  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLY C  -12  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X VAL C  -11  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X ASP C  -10  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X LEU C   -9  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLY C   -8  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X THR C   -7  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLU C   -6  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X ASN C   -5  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X LEU C   -4  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X TYR C   -3  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X PHE C   -2  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLN C   -1  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER C    0  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X MET D  -21  UNP  D7RU28              INITIATING METHIONINE
SEQADV 7Z2X HIS D  -20  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS D  -19  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS D  -18  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS D  -17  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS D  -16  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X HIS D  -15  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER D  -14  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER D  -13  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLY D  -12  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X VAL D  -11  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X ASP D  -10  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X LEU D   -9  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLY D   -8  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X THR D   -7  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLU D   -6  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X ASN D   -5  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X LEU D   -4  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X TYR D   -3  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X PHE D   -2  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X GLN D   -1  UNP  D7RU28              EXPRESSION TAG
SEQADV 7Z2X SER D    0  UNP  D7RU28              EXPRESSION TAG
SEQRES   1 A  282  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 A  282  GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE LYS PHE
SEQRES   3 A  282  VAL THR THR GLU ILE ASN GLY LEU THR LEU ARG GLY THR
SEQRES   4 A  282  ALA HIS VAL PRO ASP GLY GLU PRO GLY GLN GLN PHE PRO
SEQRES   5 A  282  THR VAL LEU MET PHE HIS GLY PHE GLY ALA VAL ARG ASP
SEQRES   6 A  282  GLU GLY PHE ARG LEU PHE ILE GLN MET SER ASN ARG LEU
SEQRES   7 A  282  MET GLU ASN GLY ILE ALA ALA VAL ARG PHE ASP PHE GLY
SEQRES   8 A  282  CYS HIS GLY GLU SER ASP GLY GLU PHE GLU ASP PHE THR
SEQRES   9 A  282  PHE SER GLN GLU LEU ASN GLU GLY SER ALA LEU ILE ASP
SEQRES  10 A  282  ALA VAL LYS SER MET SER PHE VAL ASP SER THR LYS PHE
SEQRES  11 A  282  SER LEU LEU GLY GLU SER LEU GLY SER VAL ALA ALA SER
SEQRES  12 A  282  ILE VAL ALA GLY LYS ARG SER THR GLU LEU THR SER LEU
SEQRES  13 A  282  CYS MET TRP SER PRO ALA ALA SER PHE LEU ASP GLU ILE
SEQRES  14 A  282  LEU ASN ASP HIS THR LEU GLN GLY LYS THR VAL ASP ASN
SEQRES  15 A  282  VAL GLU LYS ASP GLY TYR PHE ASP PHE TYR GLY LEU LYS
SEQRES  16 A  282  LEU GLY LYS ALA PHE PHE ASP ASP LEU LYS ASN ILE ASN
SEQRES  17 A  282  ILE PHE ASP ASN ALA LYS LYS TYR GLN GLY PRO VAL LYS
SEQRES  18 A  282  ILE VAL TYR GLY THR ASN ASP PHE ILE PRO GLU LYS TYR
SEQRES  19 A  282  SER HIS LYS TYR MET ASP GLY TYR GLU ASN GLY GLU LEU
SEQRES  20 A  282  VAL ILE VAL GLN ASP GLY ASP HIS GLY TRP GLN SER VAL
SEQRES  21 A  282  PRO SER ARG LYS ARG ILE LEU ASP GLU THR MET LYS PHE
SEQRES  22 A  282  PHE ARG LYS THR LEU LEU GLU ALA LYS
SEQRES   1 B  282  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 B  282  GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE LYS PHE
SEQRES   3 B  282  VAL THR THR GLU ILE ASN GLY LEU THR LEU ARG GLY THR
SEQRES   4 B  282  ALA HIS VAL PRO ASP GLY GLU PRO GLY GLN GLN PHE PRO
SEQRES   5 B  282  THR VAL LEU MET PHE HIS GLY PHE GLY ALA VAL ARG ASP
SEQRES   6 B  282  GLU GLY PHE ARG LEU PHE ILE GLN MET SER ASN ARG LEU
SEQRES   7 B  282  MET GLU ASN GLY ILE ALA ALA VAL ARG PHE ASP PHE GLY
SEQRES   8 B  282  CYS HIS GLY GLU SER ASP GLY GLU PHE GLU ASP PHE THR
SEQRES   9 B  282  PHE SER GLN GLU LEU ASN GLU GLY SER ALA LEU ILE ASP
SEQRES  10 B  282  ALA VAL LYS SER MET SER PHE VAL ASP SER THR LYS PHE
SEQRES  11 B  282  SER LEU LEU GLY GLU SER LEU GLY SER VAL ALA ALA SER
SEQRES  12 B  282  ILE VAL ALA GLY LYS ARG SER THR GLU LEU THR SER LEU
SEQRES  13 B  282  CYS MET TRP SER PRO ALA ALA SER PHE LEU ASP GLU ILE
SEQRES  14 B  282  LEU ASN ASP HIS THR LEU GLN GLY LYS THR VAL ASP ASN
SEQRES  15 B  282  VAL GLU LYS ASP GLY TYR PHE ASP PHE TYR GLY LEU LYS
SEQRES  16 B  282  LEU GLY LYS ALA PHE PHE ASP ASP LEU LYS ASN ILE ASN
SEQRES  17 B  282  ILE PHE ASP ASN ALA LYS LYS TYR GLN GLY PRO VAL LYS
SEQRES  18 B  282  ILE VAL TYR GLY THR ASN ASP PHE ILE PRO GLU LYS TYR
SEQRES  19 B  282  SER HIS LYS TYR MET ASP GLY TYR GLU ASN GLY GLU LEU
SEQRES  20 B  282  VAL ILE VAL GLN ASP GLY ASP HIS GLY TRP GLN SER VAL
SEQRES  21 B  282  PRO SER ARG LYS ARG ILE LEU ASP GLU THR MET LYS PHE
SEQRES  22 B  282  PHE ARG LYS THR LEU LEU GLU ALA LYS
SEQRES   1 C  282  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 C  282  GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE LYS PHE
SEQRES   3 C  282  VAL THR THR GLU ILE ASN GLY LEU THR LEU ARG GLY THR
SEQRES   4 C  282  ALA HIS VAL PRO ASP GLY GLU PRO GLY GLN GLN PHE PRO
SEQRES   5 C  282  THR VAL LEU MET PHE HIS GLY PHE GLY ALA VAL ARG ASP
SEQRES   6 C  282  GLU GLY PHE ARG LEU PHE ILE GLN MET SER ASN ARG LEU
SEQRES   7 C  282  MET GLU ASN GLY ILE ALA ALA VAL ARG PHE ASP PHE GLY
SEQRES   8 C  282  CYS HIS GLY GLU SER ASP GLY GLU PHE GLU ASP PHE THR
SEQRES   9 C  282  PHE SER GLN GLU LEU ASN GLU GLY SER ALA LEU ILE ASP
SEQRES  10 C  282  ALA VAL LYS SER MET SER PHE VAL ASP SER THR LYS PHE
SEQRES  11 C  282  SER LEU LEU GLY GLU SER LEU GLY SER VAL ALA ALA SER
SEQRES  12 C  282  ILE VAL ALA GLY LYS ARG SER THR GLU LEU THR SER LEU
SEQRES  13 C  282  CYS MET TRP SER PRO ALA ALA SER PHE LEU ASP GLU ILE
SEQRES  14 C  282  LEU ASN ASP HIS THR LEU GLN GLY LYS THR VAL ASP ASN
SEQRES  15 C  282  VAL GLU LYS ASP GLY TYR PHE ASP PHE TYR GLY LEU LYS
SEQRES  16 C  282  LEU GLY LYS ALA PHE PHE ASP ASP LEU LYS ASN ILE ASN
SEQRES  17 C  282  ILE PHE ASP ASN ALA LYS LYS TYR GLN GLY PRO VAL LYS
SEQRES  18 C  282  ILE VAL TYR GLY THR ASN ASP PHE ILE PRO GLU LYS TYR
SEQRES  19 C  282  SER HIS LYS TYR MET ASP GLY TYR GLU ASN GLY GLU LEU
SEQRES  20 C  282  VAL ILE VAL GLN ASP GLY ASP HIS GLY TRP GLN SER VAL
SEQRES  21 C  282  PRO SER ARG LYS ARG ILE LEU ASP GLU THR MET LYS PHE
SEQRES  22 C  282  PHE ARG LYS THR LEU LEU GLU ALA LYS
SEQRES   1 D  282  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 D  282  GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE LYS PHE
SEQRES   3 D  282  VAL THR THR GLU ILE ASN GLY LEU THR LEU ARG GLY THR
SEQRES   4 D  282  ALA HIS VAL PRO ASP GLY GLU PRO GLY GLN GLN PHE PRO
SEQRES   5 D  282  THR VAL LEU MET PHE HIS GLY PHE GLY ALA VAL ARG ASP
SEQRES   6 D  282  GLU GLY PHE ARG LEU PHE ILE GLN MET SER ASN ARG LEU
SEQRES   7 D  282  MET GLU ASN GLY ILE ALA ALA VAL ARG PHE ASP PHE GLY
SEQRES   8 D  282  CYS HIS GLY GLU SER ASP GLY GLU PHE GLU ASP PHE THR
SEQRES   9 D  282  PHE SER GLN GLU LEU ASN GLU GLY SER ALA LEU ILE ASP
SEQRES  10 D  282  ALA VAL LYS SER MET SER PHE VAL ASP SER THR LYS PHE
SEQRES  11 D  282  SER LEU LEU GLY GLU SER LEU GLY SER VAL ALA ALA SER
SEQRES  12 D  282  ILE VAL ALA GLY LYS ARG SER THR GLU LEU THR SER LEU
SEQRES  13 D  282  CYS MET TRP SER PRO ALA ALA SER PHE LEU ASP GLU ILE
SEQRES  14 D  282  LEU ASN ASP HIS THR LEU GLN GLY LYS THR VAL ASP ASN
SEQRES  15 D  282  VAL GLU LYS ASP GLY TYR PHE ASP PHE TYR GLY LEU LYS
SEQRES  16 D  282  LEU GLY LYS ALA PHE PHE ASP ASP LEU LYS ASN ILE ASN
SEQRES  17 D  282  ILE PHE ASP ASN ALA LYS LYS TYR GLN GLY PRO VAL LYS
SEQRES  18 D  282  ILE VAL TYR GLY THR ASN ASP PHE ILE PRO GLU LYS TYR
SEQRES  19 D  282  SER HIS LYS TYR MET ASP GLY TYR GLU ASN GLY GLU LEU
SEQRES  20 D  282  VAL ILE VAL GLN ASP GLY ASP HIS GLY TRP GLN SER VAL
SEQRES  21 D  282  PRO SER ARG LYS ARG ILE LEU ASP GLU THR MET LYS PHE
SEQRES  22 D  282  PHE ARG LYS THR LEU LEU GLU ALA LYS
FORMUL   5  HOH   *879(H2 O)
HELIX    1 AA1 GLU A   44  PHE A   46  5                                   3
HELIX    2 AA2 ARG A   47  ASN A   59  1                                  13
HELIX    3 AA3 GLU A   77  PHE A   81  5                                   5
HELIX    4 AA4 THR A   82  SER A   99  1                                  18
HELIX    5 AA5 LEU A  115  ARG A  127  1                                  13
HELIX    6 AA6 SER A  128  LEU A  131  5                                   4
HELIX    7 AA7 SER A  142  ASN A  149  1                                   8
HELIX    8 AA8 ASN A  160  GLY A  165  1                                   6
HELIX    9 AA9 GLY A  175  LEU A  182  1                                   8
HELIX   10 AB1 LYS A  183  ILE A  185  5                                   3
HELIX   11 AB2 ASN A  186  LYS A  192  1                                   7
HELIX   12 AB3 GLU A  210  TYR A  220  1                                  11
HELIX   13 AB4 SER A  237  LEU A  257  1                                  21
HELIX   14 AB5 GLU B   44  PHE B   46  5                                   3
HELIX   15 AB6 ARG B   47  ASN B   59  1                                  13
HELIX   16 AB7 GLU B   77  PHE B   81  5                                   5
HELIX   17 AB8 THR B   82  SER B   99  1                                  18
HELIX   18 AB9 SER B  114  ARG B  127  1                                  14
HELIX   19 AC1 SER B  128  LEU B  131  5                                   4
HELIX   20 AC2 SER B  142  ASN B  149  1                                   8
HELIX   21 AC3 ASN B  160  GLY B  165  1                                   6
HELIX   22 AC4 GLY B  175  LEU B  182  1                                   8
HELIX   23 AC5 LYS B  183  ILE B  185  5                                   3
HELIX   24 AC6 ILE B  187  LYS B  192  1                                   6
HELIX   25 AC7 GLU B  210  TYR B  220  1                                  11
HELIX   26 AC8 SER B  237  LEU B  257  1                                  21
HELIX   27 AC9 GLU C   44  PHE C   46  5                                   3
HELIX   28 AD1 ARG C   47  ASN C   59  1                                  13
HELIX   29 AD2 GLU C   77  PHE C   81  5                                   5
HELIX   30 AD3 THR C   82  SER C   99  1                                  18
HELIX   31 AD4 LEU C  115  ARG C  127  1                                  13
HELIX   32 AD5 SER C  128  LEU C  131  5                                   4
HELIX   33 AD6 SER C  142  HIS C  151  1                                  10
HELIX   34 AD7 ASN C  160  GLY C  165  1                                   6
HELIX   35 AD8 GLY C  175  LEU C  182  1                                   8
HELIX   36 AD9 LYS C  183  ILE C  185  5                                   3
HELIX   37 AE1 ILE C  187  LYS C  192  1                                   6
HELIX   38 AE2 GLU C  210  TYR C  220  1                                  11
HELIX   39 AE3 SER C  237  LEU C  257  1                                  21
HELIX   40 AE4 GLU D   44  PHE D   46  5                                   3
HELIX   41 AE5 ARG D   47  ASN D   59  1                                  13
HELIX   42 AE6 GLU D   77  PHE D   81  5                                   5
HELIX   43 AE7 THR D   82  SER D   99  1                                  18
HELIX   44 AE8 SER D  114  ARG D  127  1                                  14
HELIX   45 AE9 SER D  128  LEU D  131  5                                   4
HELIX   46 AF1 SER D  142  ASN D  149  1                                   8
HELIX   47 AF2 ASN D  160  GLY D  165  1                                   6
HELIX   48 AF3 GLY D  175  LEU D  182  1                                   8
HELIX   49 AF4 LYS D  183  ILE D  185  5                                   3
HELIX   50 AF5 ILE D  187  LYS D  192  1                                   6
HELIX   51 AF6 GLU D  210  TYR D  220  1                                  11
HELIX   52 AF7 SER D  237  LEU D  257  1                                  21
SHEET    1 AA1 8 MET A   1  ILE A   9  0
SHEET    2 AA1 8 LEU A  12  VAL A  20 -1  O  ALA A  18   N  LYS A   3
SHEET    3 AA1 8 ALA A  62  PHE A  66 -1  O  ALA A  63   N  HIS A  19
SHEET    4 AA1 8 PHE A  29  PHE A  35  1  N  PRO A  30   O  ALA A  62
SHEET    5 AA1 8 VAL A 103  GLU A 113  1  O  LEU A 111   N  PHE A  35
SHEET    6 AA1 8 SER A 133  TRP A 137  1  O  TRP A 137   N  GLY A 112
SHEET    7 AA1 8 VAL A 198  GLY A 203  1  O  LYS A 199   N  MET A 136
SHEET    8 AA1 8 GLY A 223  VAL A 228  1  O  VAL A 226   N  ILE A 200
SHEET    1 AA2 2 THR A 152  LEU A 153  0
SHEET    2 AA2 2 LYS A 156  THR A 157 -1  O  LYS A 156   N  LEU A 153
SHEET    1 AA3 2 PHE A 167  PHE A 169  0
SHEET    2 AA3 2 LEU A 172  LEU A 174 -1  O  LEU A 174   N  PHE A 167
SHEET    1 AA4 8 MET B   1  ILE B   9  0
SHEET    2 AA4 8 LEU B  12  VAL B  20 -1  O  ALA B  18   N  LYS B   3
SHEET    3 AA4 8 ALA B  62  PHE B  66 -1  O  ALA B  63   N  HIS B  19
SHEET    4 AA4 8 PHE B  29  PHE B  35  1  N  PRO B  30   O  ALA B  62
SHEET    5 AA4 8 VAL B 103  GLU B 113  1  O  LEU B 111   N  PHE B  35
SHEET    6 AA4 8 SER B 133  TRP B 137  1  O  CYS B 135   N  LEU B 110
SHEET    7 AA4 8 VAL B 198  GLY B 203  1  O  LYS B 199   N  MET B 136
SHEET    8 AA4 8 GLY B 223  VAL B 228  1  O  VAL B 226   N  ILE B 200
SHEET    1 AA5 2 THR B 152  LEU B 153  0
SHEET    2 AA5 2 LYS B 156  THR B 157 -1  O  LYS B 156   N  LEU B 153
SHEET    1 AA6 2 PHE B 167  PHE B 169  0
SHEET    2 AA6 2 LEU B 172  LEU B 174 -1  O  LEU B 174   N  PHE B 167
SHEET    1 AA7 8 MET C   1  ILE C   9  0
SHEET    2 AA7 8 LEU C  12  VAL C  20 -1  O  ALA C  18   N  LYS C   3
SHEET    3 AA7 8 ALA C  62  PHE C  66 -1  O  ALA C  63   N  HIS C  19
SHEET    4 AA7 8 PHE C  29  PHE C  35  1  N  PRO C  30   O  ALA C  62
SHEET    5 AA7 8 VAL C 103  GLU C 113  1  O  LEU C 111   N  PHE C  35
SHEET    6 AA7 8 SER C 133  TRP C 137  1  O  TRP C 137   N  GLY C 112
SHEET    7 AA7 8 VAL C 198  GLY C 203  1  O  LYS C 199   N  MET C 136
SHEET    8 AA7 8 GLY C 223  VAL C 228  1  O  VAL C 226   N  ILE C 200
SHEET    1 AA8 2 THR C 152  LEU C 153  0
SHEET    2 AA8 2 LYS C 156  THR C 157 -1  O  LYS C 156   N  LEU C 153
SHEET    1 AA9 2 PHE C 167  PHE C 169  0
SHEET    2 AA9 2 LEU C 172  LEU C 174 -1  O  LEU C 174   N  PHE C 167
SHEET    1 AB1 8 MET D   1  ILE D   9  0
SHEET    2 AB1 8 LEU D  12  VAL D  20 -1  O  LEU D  14   N  THR D   7
SHEET    3 AB1 8 ALA D  62  PHE D  66 -1  O  ALA D  63   N  HIS D  19
SHEET    4 AB1 8 PHE D  29  PHE D  35  1  N  PRO D  30   O  ALA D  62
SHEET    5 AB1 8 VAL D 103  GLU D 113  1  O  SER D 109   N  LEU D  33
SHEET    6 AB1 8 LEU D 134  TRP D 137  1  O  CYS D 135   N  LEU D 110
SHEET    7 AB1 8 VAL D 198  GLY D 203  1  O  LYS D 199   N  MET D 136
SHEET    8 AB1 8 GLY D 223  VAL D 228  1  O  VAL D 226   N  ILE D 200
SHEET    1 AB2 2 THR D 152  LEU D 153  0
SHEET    2 AB2 2 LYS D 156  THR D 157 -1  O  LYS D 156   N  LEU D 153
SHEET    1 AB3 2 PHE D 167  PHE D 169  0
SHEET    2 AB3 2 LEU D 172  LEU D 174 -1  O  LEU D 172   N  PHE D 169
CRYST1   47.830   62.230   94.850 103.05 101.52  92.80 P 1           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      0.020907  0.001023  0.004645        0.00000
SCALE2      0.000000  0.016089  0.003991        0.00000
SCALE3      0.000000  0.000000  0.011086        0.00000
TER    2121      ALA A 259
TER    4203      ALA B 259
TER    6315      ALA C 259
TER    8388      ALA D 259
MASTER      324    0    0   52   48    0    0    6 9163    4    0   88
END