longtext: 6i8w-pdb

content
HEADER    HYDROLASE                               21-NOV-18   6I8W
TITLE     CRYSTAL STRUCTURE OF A MEMBRANE PHOSPHOLIPASE A, A NOVEL BACTERIAL
TITLE    2 VIRULENCE FACTOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA/BETA FOLD HYDROLASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: ESTERASE,LIPASE,LIPASE 3,PUTATIVE LIPASE;
COMPND   5 EC: 3.1.1.3;
COMPND   6 ENGINEERED: YES;
COMPND   7 OTHER_DETAILS: FME:N-FORMYLMETHIONINE, C-TERMINAL HIS-TAG
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE   3 ORGANISM_TAXID: 287;
SOURCE   4 GENE: LIP3, AOY09_04297, C8257_11100, DN070_25360, NCTC13719_02038,
SOURCE   5 PAMH19_2121;
SOURCE   6 EXPRESSION_SYSTEM: PSEUDOMONAS AERUGINOSA PAO1;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 208964
KEYWDS    LIPASE, MEMBRANE PROTEIN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.GRANZIN,R.BATRA-SAFFERLING
REVDAT   3   29-JUL-20 6I8W    1       COMPND REMARK HETNAM SITE
REVDAT   2   10-JUN-20 6I8W    1       JRNL
REVDAT   1   27-NOV-19 6I8W    0
JRNL        AUTH   F.BLEFFERT,J.GRANZIN,M.CALISKAN,S.N.SCHOTT-VERDUGO,L.RAHME,
JRNL        AUTH 2 M.SIEBERS,B.THIELE,P.DOERMANN,H.GOHLKE,R.BATRA-SAFFERLING,
JRNL        AUTH 3 F.KOVACIC,K.-E.JAEGER
JRNL        TITL   STRUCTURAL AND MECHANISTIC INSIGHTS INTO PHOSPHOLIPASE
JRNL        TITL 2 A-MEDIATED MEMBRANE PHOSPHOLIPID DEGRADATION ASSOCIATED WITH
JRNL        TITL 3 BACTERIAL VIRULENCE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309
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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.33
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 65084
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164
REMARK   3   R VALUE            (WORKING SET) : 0.163
REMARK   3   FREE R VALUE                     : 0.186
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070
REMARK   3   FREE R VALUE TEST SET COUNT      : 3298
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 47.3438 -  5.7657    0.99     2777   140  0.1738 0.1784
REMARK   3     2  5.7657 -  4.5776    1.00     2652   143  0.1439 0.1858
REMARK   3     3  4.5776 -  3.9993    1.00     2634   129  0.1327 0.1468
REMARK   3     4  3.9993 -  3.6338    1.00     2600   132  0.1491 0.1695
REMARK   3     5  3.6338 -  3.3734    1.00     2589   147  0.1597 0.1508
REMARK   3     6  3.3734 -  3.1746    1.00     2584   146  0.1687 0.1752
REMARK   3     7  3.1746 -  3.0156    1.00     2588   131  0.1829 0.2145
REMARK   3     8  3.0156 -  2.8844    1.00     2578   124  0.1777 0.2104
REMARK   3     9  2.8844 -  2.7733    1.00     2578   137  0.1728 0.2119
REMARK   3    10  2.7733 -  2.6776    1.00     2554   126  0.1734 0.1970
REMARK   3    11  2.6776 -  2.5939    1.00     2554   145  0.1650 0.1879
REMARK   3    12  2.5939 -  2.5198    1.00     2571   132  0.1643 0.1931
REMARK   3    13  2.5198 -  2.4535    1.00     2547   148  0.1588 0.1916
REMARK   3    14  2.4535 -  2.3936    1.00     2536   147  0.1636 0.1998
REMARK   3    15  2.3936 -  2.3392    1.00     2560   133  0.1606 0.1957
REMARK   3    16  2.3392 -  2.2894    1.00     2567   126  0.1591 0.2015
REMARK   3    17  2.2894 -  2.2436    1.00     2532   155  0.1610 0.1783
REMARK   3    18  2.2436 -  2.2013    1.00     2542   125  0.1687 0.2261
REMARK   3    19  2.2013 -  2.1620    1.00     2529   140  0.1815 0.2074
REMARK   3    20  2.1620 -  2.1253    1.00     2535   132  0.1967 0.2512
REMARK   3    21  2.1253 -  2.0910    1.00     2527   144  0.2009 0.2411
REMARK   3    22  2.0910 -  2.0589    1.00     2542   142  0.2142 0.2914
REMARK   3    23  2.0589 -  2.0286    1.00     2559   134  0.2216 0.2571
REMARK   3    24  2.0286 -  2.0000    1.00     2551   140  0.2410 0.2672
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : NULL
REMARK   3   SOLVENT RADIUS     : 1.20
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)     : 0.200
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.610
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 38.30
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      :  0.008           5067
REMARK   3   ANGLE     :  1.069           6892
REMARK   3   CHIRALITY :  0.047            786
REMARK   3   PLANARITY :  0.006            904
REMARK   3   DIHEDRAL  : 14.404           1914
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 10
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 19 )
REMARK   3    ORIGIN FOR THE GROUP (A): 104.4359  38.4985  11.9893
REMARK   3    T TENSOR
REMARK   3      T11:   0.9217 T22:   0.9527
REMARK   3      T33:   1.2703 T12:  -0.3696
REMARK   3      T13:  -0.0049 T23:  -0.1194
REMARK   3    L TENSOR
REMARK   3      L11:   4.3437 L22:   1.8875
REMARK   3      L33:   7.5132 L12:   2.1782
REMARK   3      L13:  -0.4565 L23:  -1.3233
REMARK   3    S TENSOR
REMARK   3      S11:   0.3162 S12:  -0.6284 S13:   1.8362
REMARK   3      S21:   0.2078 S22:   0.1453 S23:  -0.4678
REMARK   3      S31:  -0.9295 S32:   2.0465 S33:  -0.4707
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 63 )
REMARK   3    ORIGIN FOR THE GROUP (A):  75.3587  22.8505  -1.1034
REMARK   3    T TENSOR
REMARK   3      T11:   0.3944 T22:   0.3131
REMARK   3      T33:   0.3537 T12:  -0.0108
REMARK   3      T13:  -0.0093 T23:   0.1649
REMARK   3    L TENSOR
REMARK   3      L11:   1.6301 L22:   1.8720
REMARK   3      L33:   1.9623 L12:  -0.5828
REMARK   3      L13:  -0.1443 L23:  -1.2341
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0391 S12:   0.3787 S13:   0.2315
REMARK   3      S21:  -0.1372 S22:  -0.2545 S23:  -0.4322
REMARK   3      S31:  -0.1747 S32:   0.3248 S33:   0.2613
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 149 )
REMARK   3    ORIGIN FOR THE GROUP (A):  63.0905  27.0606  -0.9302
REMARK   3    T TENSOR
REMARK   3      T11:   0.3416 T22:   0.2437
REMARK   3      T33:   0.3210 T12:   0.0114
REMARK   3      T13:  -0.0063 T23:   0.1213
REMARK   3    L TENSOR
REMARK   3      L11:   2.1159 L22:   2.6173
REMARK   3      L33:   2.8367 L12:   1.0394
REMARK   3      L13:  -0.7326 L23:  -0.5894
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0447 S12:   0.3563 S13:   0.4554
REMARK   3      S21:  -0.0341 S22:   0.0073 S23:   0.0929
REMARK   3      S31:  -0.2502 S32:  -0.1082 S33:   0.0407
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 171 )
REMARK   3    ORIGIN FOR THE GROUP (A):  51.3149  28.9932   4.9707
REMARK   3    T TENSOR
REMARK   3      T11:   0.2896 T22:   0.2329
REMARK   3      T33:   0.4450 T12:   0.0002
REMARK   3      T13:   0.0660 T23:   0.0883
REMARK   3    L TENSOR
REMARK   3      L11:   3.3722 L22:   5.8023
REMARK   3      L33:   3.6835 L12:  -0.2335
REMARK   3      L13:   0.5134 L23:   1.9940
REMARK   3    S TENSOR
REMARK   3      S11:   0.0460 S12:   0.0231 S13:   0.6246
REMARK   3      S21:   0.2288 S22:  -0.1418 S23:   0.8700
REMARK   3      S31:  -0.1709 S32:  -0.4392 S33:   0.0438
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 172 THROUGH 207 )
REMARK   3    ORIGIN FOR THE GROUP (A):  66.5276  35.6845  19.4903
REMARK   3    T TENSOR
REMARK   3      T11:   0.8620 T22:   0.3650
REMARK   3      T33:   0.4690 T12:  -0.1788
REMARK   3      T13:   0.0203 T23:  -0.0164
REMARK   3    L TENSOR
REMARK   3      L11:   3.0668 L22:   3.2946
REMARK   3      L33:   2.0403 L12:  -1.1160
REMARK   3      L13:   0.6400 L23:   0.0837
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0167 S12:  -0.2572 S13:   0.4913
REMARK   3      S21:   0.8152 S22:  -0.0995 S23:  -0.1770
REMARK   3      S31:  -0.7771 S32:   0.2307 S33:   0.0951
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 208 THROUGH 234 )
REMARK   3    ORIGIN FOR THE GROUP (A):  71.7484  38.5745   9.9212
REMARK   3    T TENSOR
REMARK   3      T11:   0.6324 T22:   0.3389
REMARK   3      T33:   0.5516 T12:  -0.1167
REMARK   3      T13:  -0.0146 T23:   0.0978
REMARK   3    L TENSOR
REMARK   3      L11:   3.0371 L22:   5.8290
REMARK   3      L33:   4.3952 L12:  -3.8164
REMARK   3      L13:   2.3359 L23:  -1.9962
REMARK   3    S TENSOR
REMARK   3      S11:   0.0005 S12:  -0.3598 S13:   0.9972
REMARK   3      S21:   0.1746 S22:  -0.1722 S23:  -0.6093
REMARK   3      S31:  -0.7122 S32:   0.3535 S33:   0.1967
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 235 THROUGH 292 )
REMARK   3    ORIGIN FOR THE GROUP (A):  51.1457  26.7629  10.7793
REMARK   3    T TENSOR
REMARK   3      T11:   0.4041 T22:   0.2337
REMARK   3      T33:   0.4434 T12:   0.0310
REMARK   3      T13:   0.1247 T23:   0.0180
REMARK   3    L TENSOR
REMARK   3      L11:   2.3011 L22:   3.3587
REMARK   3      L33:   1.2997 L12:   1.5060
REMARK   3      L13:  -0.5168 L23:  -0.5145
REMARK   3    S TENSOR
REMARK   3      S11:   0.1948 S12:   0.0895 S13:   0.6983
REMARK   3      S21:   0.5032 S22:  -0.1022 S23:   0.6973
REMARK   3      S31:  -0.3784 S32:  -0.2340 S33:  -0.0927
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 310 )
REMARK   3    ORIGIN FOR THE GROUP (A):  55.5978  11.7793   6.6377
REMARK   3    T TENSOR
REMARK   3      T11:   0.4040 T22:   0.2947
REMARK   3      T33:   0.3579 T12:  -0.0293
REMARK   3      T13:   0.0600 T23:  -0.0246
REMARK   3    L TENSOR
REMARK   3      L11:   2.4956 L22:   2.2570
REMARK   3      L33:   8.5445 L12:  -1.8894
REMARK   3      L13:   3.4552 L23:  -0.9575
REMARK   3    S TENSOR
REMARK   3      S11:   0.2302 S12:   0.1329 S13:  -0.5182
REMARK   3      S21:   0.1399 S22:  -0.1609 S23:   0.3740
REMARK   3      S31:   0.6341 S32:  -0.3250 S33:  -0.1120
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 37 )
REMARK   3    ORIGIN FOR THE GROUP (A):  97.9057  30.3156   5.8969
REMARK   3    T TENSOR
REMARK   3      T11:   0.6294 T22:   0.5195
REMARK   3      T33:   0.8006 T12:  -0.1557
REMARK   3      T13:   0.0445 T23:   0.1393
REMARK   3    L TENSOR
REMARK   3      L11:   4.3209 L22:   6.0737
REMARK   3      L33:   0.1672 L12:   5.2474
REMARK   3      L13:  -1.1194 L23:  -1.3276
REMARK   3    S TENSOR
REMARK   3      S11:   0.4361 S12:   0.1774 S13:  -0.5389
REMARK   3      S21:   0.5568 S22:  -0.1441 S23:  -1.5693
REMARK   3      S31:  -0.2204 S32:   0.2786 S33:  -0.1390
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 38 THROUGH 310 )
REMARK   3    ORIGIN FOR THE GROUP (A):  93.2940  -2.0457  21.3392
REMARK   3    T TENSOR
REMARK   3      T11:   0.3201 T22:   0.2711
REMARK   3      T33:   0.2923 T12:  -0.0398
REMARK   3      T13:  -0.1151 T23:   0.0808
REMARK   3    L TENSOR
REMARK   3      L11:   3.1780 L22:   2.0848
REMARK   3      L33:   3.7494 L12:   0.7353
REMARK   3      L13:   1.4265 L23:   0.9889
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1129 S12:   0.2281 S13:   0.0430
REMARK   3      S21:   0.0094 S22:   0.1218 S23:  -0.2540
REMARK   3      S31:  -0.0898 S32:   0.3953 S33:  -0.0103
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 6I8W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1200013014.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-14
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID29
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686
REMARK 200  MONOCHROMATOR                  : SILICON (111) CHANNEL-CUT
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65113
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.330
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 10.30
REMARK 200  R MERGE                    (I) : 0.05300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 24.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.50
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MRBUMP
REMARK 200 STARTING MODEL: 2VF2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRISODIUM CITRATE, 10% (W/V) PEG
REMARK 280  4000, 10% (W/V) ISOPROPANOL, PH 5.6, VAPOR DIFFUSION, SITTING
REMARK 280  DROP, TEMPERATURE 292.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       3555   -Y,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X,Z+3/4
REMARK 290       5555   -X+1/2,Y,-Z+3/4
REMARK 290       6555   X,-Y+1/2,-Z+1/4
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2
REMARK 290       8555   -Y,-X,-Z
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2
REMARK 290      10555   -X,-Y,Z
REMARK 290      11555   -Y+1/2,X,Z+3/4
REMARK 290      12555   Y,-X+1/2,Z+1/4
REMARK 290      13555   -X,Y+1/2,-Z+1/4
REMARK 290      14555   X+1/2,-Y,-Z+3/4
REMARK 290      15555   Y,X,-Z
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2
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       66.93550
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       66.93550
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      106.17900
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       66.93550
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       53.08950
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       66.93550
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      159.26850
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       66.93550
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      159.26850
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.93550
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       53.08950
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       66.93550
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       66.93550
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      106.17900
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       66.93550
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       66.93550
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      106.17900
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       66.93550
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      159.26850
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       66.93550
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       53.08950
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       66.93550
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       53.08950
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       66.93550
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      159.26850
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       66.93550
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       66.93550
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      106.17900
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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     GLN A   311
REMARK 465     VAL A   312
REMARK 465     ALA A   313
REMARK 465     GLY A   314
REMARK 465     ARG A   315
REMARK 465     GLY A   316
REMARK 465     HIS A   317
REMARK 465     HIS A   318
REMARK 465     HIS A   319
REMARK 465     HIS A   320
REMARK 465     HIS A   321
REMARK 465     HIS A   322
REMARK 465     GLN B   311
REMARK 465     VAL B   312
REMARK 465     ALA B   313
REMARK 465     GLY B   314
REMARK 465     ARG B   315
REMARK 465     GLY B   316
REMARK 465     HIS B   317
REMARK 465     HIS B   318
REMARK 465     HIS B   319
REMARK 465     HIS B   320
REMARK 465     HIS B   321
REMARK 465     HIS B   322
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     LYS A   2    CG   CD   CE   NZ
REMARK 470     GLU A  87    CG   CD   OE1  OE2
REMARK 470     ARG A 129    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 130    CZ   NH1  NH2
REMARK 470     ARG A 169    NE   CZ   NH1  NH2
REMARK 470     LYS A 194    CD   CE   NZ
REMARK 470     GLU A 247    CG   CD   OE1  OE2
REMARK 470     ARG A 308    CZ   NH1  NH2
REMARK 470     ARG B   3    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B  60    CG   CD   OE1  OE2
REMARK 470     LYS B  61    CD   CE   NZ
REMARK 470     ARG B  88    CZ   NH1  NH2
REMARK 470     GLN B 106    CG   CD   OE1  NE2
REMARK 470     GLN B 107    CG   CD   OE1  NE2
REMARK 470     ARG B 129    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 130    NE   CZ   NH1  NH2
REMARK 470     LYS B 170    CD   CE   NZ
REMARK 470     GLU B 175    CD   OE1  OE2
REMARK 470     LYS B 194    CD   CE   NZ
REMARK 470     ARG B 212    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 217    CD   NE   CZ   NH1  NH2
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   OD2  ASP A   101     O    HOH A   501              2.06
REMARK 500   O    ILE B   246     O    HOH B   601              2.07
REMARK 500   O2   CO2 A   406     O    HOH A   502              2.13
REMARK 500   O    VAL B   185     O    HOH B   602              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    SER A 137     -120.68     56.77
REMARK 500    SER A 137     -118.47     53.29
REMARK 500    SER B 137     -120.58     56.73
REMARK 500    SER B 137     -119.18     54.45
REMARK 500
REMARK 500 REMARK: NULL
DBREF  6I8W A    1   315  UNP    Q9KJG6   Q9KJG6_PSEAI     1    315
DBREF  6I8W B    1   315  UNP    Q9KJG6   Q9KJG6_PSEAI     1    315
SEQADV 6I8W GLY A  316  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS A  317  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS A  318  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS A  319  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS A  320  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS A  321  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS A  322  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W GLY B  316  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS B  317  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS B  318  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS B  319  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS B  320  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS B  321  UNP  Q9KJG6              EXPRESSION TAG
SEQADV 6I8W HIS B  322  UNP  Q9KJG6              EXPRESSION TAG
SEQRES   1 A  322  FME LYS ARG PHE LEU LEU GLY LEU VAL LEU LEU LEU ALA
SEQRES   2 A  322  VAL ALA ALA GLY VAL LEU TYR PHE VAL PRO ALA THR LEU
SEQRES   3 A  322  LEU ALA SER VAL ARG THR VAL GLU ARG GLY LEU ALA GLY
SEQRES   4 A  322  LEU SER GLU HIS SER VAL GLN VAL ASP ASN LEU GLU ILE
SEQRES   5 A  322  ALA TYR LEU GLU GLY GLY SER GLU LYS ASN PRO THR LEU
SEQRES   6 A  322  LEU LEU ILE HIS GLY PHE GLY ALA ASP LYS ASP ASN TRP
SEQRES   7 A  322  LEU ARG PHE ALA ARG PRO LEU THR GLU ARG TYR HIS VAL
SEQRES   8 A  322  VAL ALA LEU ASP LEU PRO GLY PHE GLY ASP SER SER LYS
SEQRES   9 A  322  PRO GLN GLN ALA SER TYR ASP VAL GLY THR GLN ALA GLU
SEQRES  10 A  322  ARG VAL ALA ASN PHE ALA ALA ALA ILE GLY VAL ARG ARG
SEQRES  11 A  322  LEU HIS LEU ALA GLY ASN SER MET GLY GLY HIS ILE ALA
SEQRES  12 A  322  ALA LEU TYR ALA ALA ARG HIS PRO GLU GLN VAL LEU SER
SEQRES  13 A  322  LEU ALA LEU ILE ASP ASN ALA GLY VAL MET PRO ALA ARG
SEQRES  14 A  322  LYS SER GLU LEU PHE GLU ASP LEU GLU ARG GLY GLU ASN
SEQRES  15 A  322  PRO LEU VAL VAL ARG GLN PRO GLU ASP PHE GLN LYS LEU
SEQRES  16 A  322  LEU ASP PHE VAL PHE VAL GLN GLN PRO PRO LEU PRO ALA
SEQRES  17 A  322  PRO LEU LYS ARG TYR LEU GLY GLU ARG ALA VAL ALA ALA
SEQRES  18 A  322  SER ALA PHE ASN ALA GLN ILE PHE GLU GLN LEU ARG GLN
SEQRES  19 A  322  ARG TYR ILE PRO LEU GLU PRO GLU LEU PRO LYS ILE GLU
SEQRES  20 A  322  ALA PRO THR LEU LEU LEU TRP GLY ASP ARG ASP ARG VAL
SEQRES  21 A  322  LEU ASP VAL SER SER ILE GLU VAL MET ARG PRO LEU LEU
SEQRES  22 A  322  LYS ARG PRO SER VAL VAL ILE MET GLU ASN CYS GLY HIS
SEQRES  23 A  322  VAL PRO MET VAL GLU ARG PRO GLU GLU THR ALA GLN HIS
SEQRES  24 A  322  TYR GLN ALA PHE LEU ASP GLY VAL ARG ASN ALA GLN VAL
SEQRES  25 A  322  ALA GLY ARG GLY HIS HIS HIS HIS HIS HIS
SEQRES   1 B  322  FME LYS ARG PHE LEU LEU GLY LEU VAL LEU LEU LEU ALA
SEQRES   2 B  322  VAL ALA ALA GLY VAL LEU TYR PHE VAL PRO ALA THR LEU
SEQRES   3 B  322  LEU ALA SER VAL ARG THR VAL GLU ARG GLY LEU ALA GLY
SEQRES   4 B  322  LEU SER GLU HIS SER VAL GLN VAL ASP ASN LEU GLU ILE
SEQRES   5 B  322  ALA TYR LEU GLU GLY GLY SER GLU LYS ASN PRO THR LEU
SEQRES   6 B  322  LEU LEU ILE HIS GLY PHE GLY ALA ASP LYS ASP ASN TRP
SEQRES   7 B  322  LEU ARG PHE ALA ARG PRO LEU THR GLU ARG TYR HIS VAL
SEQRES   8 B  322  VAL ALA LEU ASP LEU PRO GLY PHE GLY ASP SER SER LYS
SEQRES   9 B  322  PRO GLN GLN ALA SER TYR ASP VAL GLY THR GLN ALA GLU
SEQRES  10 B  322  ARG VAL ALA ASN PHE ALA ALA ALA ILE GLY VAL ARG ARG
SEQRES  11 B  322  LEU HIS LEU ALA GLY ASN SER MET GLY GLY HIS ILE ALA
SEQRES  12 B  322  ALA LEU TYR ALA ALA ARG HIS PRO GLU GLN VAL LEU SER
SEQRES  13 B  322  LEU ALA LEU ILE ASP ASN ALA GLY VAL MET PRO ALA ARG
SEQRES  14 B  322  LYS SER GLU LEU PHE GLU ASP LEU GLU ARG GLY GLU ASN
SEQRES  15 B  322  PRO LEU VAL VAL ARG GLN PRO GLU ASP PHE GLN LYS LEU
SEQRES  16 B  322  LEU ASP PHE VAL PHE VAL GLN GLN PRO PRO LEU PRO ALA
SEQRES  17 B  322  PRO LEU LYS ARG TYR LEU GLY GLU ARG ALA VAL ALA ALA
SEQRES  18 B  322  SER ALA PHE ASN ALA GLN ILE PHE GLU GLN LEU ARG GLN
SEQRES  19 B  322  ARG TYR ILE PRO LEU GLU PRO GLU LEU PRO LYS ILE GLU
SEQRES  20 B  322  ALA PRO THR LEU LEU LEU TRP GLY ASP ARG ASP ARG VAL
SEQRES  21 B  322  LEU ASP VAL SER SER ILE GLU VAL MET ARG PRO LEU LEU
SEQRES  22 B  322  LYS ARG PRO SER VAL VAL ILE MET GLU ASN CYS GLY HIS
SEQRES  23 B  322  VAL PRO MET VAL GLU ARG PRO GLU GLU THR ALA GLN HIS
SEQRES  24 B  322  TYR GLN ALA PHE LEU ASP GLY VAL ARG ASN ALA GLN VAL
SEQRES  25 B  322  ALA GLY ARG GLY HIS HIS HIS HIS HIS HIS
MODRES 6I8W FME A    1  MET  MODIFIED RESIDUE
MODRES 6I8W FME B    1  MET  MODIFIED RESIDUE
HET    FME  A   1      10
HET    FME  B   1      17
HET    MYR  A 401      16
HET    BOG  A 402      20
HET    IPA  A 403       4
HET    CO2  A 404       3
HET    CO2  A 405       3
HET    CO2  A 406       3
HET    11A  B 501      13
HET    BOG  B 502      20
HET    IPA  B 503       4
HET    IPA  B 504       4
HET    CO2  B 505       3
HET    CO2  B 506       3
HETNAM     FME N-FORMYLMETHIONINE
HETNAM     MYR MYRISTIC ACID
HETNAM     BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETNAM     IPA ISOPROPYL ALCOHOL
HETNAM     CO2 CARBON DIOXIDE
HETNAM     11A UNDECANOIC ACID
HETSYN     IPA 2-PROPANOL
FORMUL   1  FME    2(C6 H11 N O3 S)
FORMUL   3  MYR    C14 H28 O2
FORMUL   4  BOG    2(C14 H28 O6)
FORMUL   5  IPA    3(C3 H8 O)
FORMUL   6  CO2    5(C O2)
FORMUL   9  11A    C11 H22 O2
FORMUL  15  HOH   *233(H2 O)
HELIX    1 AA1 FME A    1  TYR A   20  1                                  20
HELIX    2 AA2 TYR A   20  GLY A   39  1                                  20
HELIX    3 AA3 ASP A   74  ASN A   77  5                                   4
HELIX    4 AA4 TRP A   78  ARG A   83  1                                   6
HELIX    5 AA5 ASP A  111  ILE A  126  1                                  16
HELIX    6 AA6 SER A  137  HIS A  150  1                                  14
HELIX    7 AA7 SER A  171  GLU A  178  1                                   8
HELIX    8 AA8 GLU A  190  PHE A  200  1                                  11
HELIX    9 AA9 PRO A  207  ARG A  235  1                                  29
HELIX   10 AB1 GLU A  242  ILE A  246  5                                   5
HELIX   11 AB2 SER A  264  ARG A  270  1                                   7
HELIX   12 AB3 PRO A  271  LEU A  273  5                                   3
HELIX   13 AB4 VAL A  287  ARG A  292  1                                   6
HELIX   14 AB5 ARG A  292  ASN A  309  1                                  18
HELIX   15 AB6 LYS B    2  ALA B   38  1                                  37
HELIX   16 AB7 ASP B   74  ASN B   77  5                                   4
HELIX   17 AB8 TRP B   78  ARG B   83  1                                   6
HELIX   18 AB9 ASP B  111  ILE B  126  1                                  16
HELIX   19 AC1 SER B  137  HIS B  150  1                                  14
HELIX   20 AC2 SER B  171  GLU B  178  1                                   8
HELIX   21 AC3 GLU B  190  PHE B  200  1                                  11
HELIX   22 AC4 PRO B  207  ARG B  235  1                                  29
HELIX   23 AC5 GLU B  242  ILE B  246  5                                   5
HELIX   24 AC6 SER B  264  ARG B  270  1                                   7
HELIX   25 AC7 PRO B  271  LEU B  273  5                                   3
HELIX   26 AC8 VAL B  287  ARG B  292  1                                   6
HELIX   27 AC9 ARG B  292  ASN B  309  1                                  18
SHEET    1 AA1 8 SER A  41  VAL A  47  0
SHEET    2 AA1 8 LEU A  50  GLY A  57 -1  O  TYR A  54   N  HIS A  43
SHEET    3 AA1 8 HIS A  90  LEU A  94 -1  O  ALA A  93   N  LEU A  55
SHEET    4 AA1 8 THR A  64  ILE A  68  1  N  LEU A  67   O  VAL A  92
SHEET    5 AA1 8 LEU A 131  ASN A 136  1  O  HIS A 132   N  LEU A  66
SHEET    6 AA1 8 VAL A 154  ILE A 160  1  O  ILE A 160   N  GLY A 135
SHEET    7 AA1 8 THR A 250  GLY A 255  1  O  LEU A 251   N  LEU A 159
SHEET    8 AA1 8 PRO A 276  MET A 281  1  O  MET A 281   N  TRP A 254
SHEET    1 AA2 8 SER B  41  VAL B  47  0
SHEET    2 AA2 8 LEU B  50  GLY B  57 -1  O  LEU B  50   N  VAL B  47
SHEET    3 AA2 8 HIS B  90  LEU B  94 -1  O  ALA B  93   N  LEU B  55
SHEET    4 AA2 8 THR B  64  ILE B  68  1  N  LEU B  67   O  VAL B  92
SHEET    5 AA2 8 LEU B 131  ASN B 136  1  O  HIS B 132   N  LEU B  66
SHEET    6 AA2 8 VAL B 154  ILE B 160  1  O  ILE B 160   N  GLY B 135
SHEET    7 AA2 8 THR B 250  GLY B 255  1  O  LEU B 251   N  LEU B 159
SHEET    8 AA2 8 PRO B 276  MET B 281  1  O  MET B 281   N  TRP B 254
LINK         C   FME A   1                 N   LYS A   2     1555   1555  1.33
LINK         C   FME B   1                 N   LYS B   2     1555   1555  1.33
CRYST1  133.871  133.871  212.358  90.00  90.00  90.00 I 41 2 2     32
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      0.007470  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007470  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004709        0.00000
TER    2442      ALA A 310
TER    4860      ALA B 310
MASTER      508    0   14   27   16    0    0    6 5092    2  125   50
END