longtext: 4Q3O-pdb

content
HEADER    HYDROLASE                               11-APR-14   4Q3O
TITLE     CRYSTAL STRUCTURE OF MGS-MT1, AN ALPHA/BETA HYDROLASE ENZYME FROM A
TITLE    2 LAKE MATAPAN DEEP-SEA METAGENOME LIBRARY
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MGS-MT1;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;
COMPND   4 FRAGMENT: MGS-MT1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE   3 ORGANISM_TAXID: 32644;
SOURCE   4 GENE: MGS-MT1;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: P15TV-LIC
KEYWDS    METAGENOME, METAGENOMIC LIBRARY, ALPHA AND BETA PROTEINS, ALPHA/BETA
KEYWDS   2 HYDROLASE SUPERFAMILY, ESTERASE/LIPASE FOLD, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.J.STOGIOS,X.XU,H.CUI,M.ALCAIDE,M.FERRER,A.SAVCHENKO
REVDAT   2   18-MAR-15 4Q3O    1       JRNL
REVDAT   1   04-MAR-15 4Q3O    0
JRNL        AUTH   M.ALCAIDE,P.J.STOGIOS,A.LAFRAYA,A.TCHIGVINTSEV,R.FLICK,
JRNL        AUTH 2 R.BARGIELA,T.N.CHERNIKOVA,O.N.REVA,T.HAI,C.C.LEGGEWIE,
JRNL        AUTH 3 N.KATZKE,V.LA CONO,R.MATESANZ,M.JEBBAR,K.E.JAEGER,
JRNL        AUTH 4 M.M.YAKIMOV,A.F.YAKUNIN,P.N.GOLYSHIN,O.V.GOLYSHINA,
JRNL        AUTH 5 A.SAVCHENKO,M.FERRER
JRNL        TITL   PRESSURE ADAPTATION IS LINKED TO THERMAL ADAPTATION IN
JRNL        TITL 2 SALT-SATURATED MARINE HABITATS.
JRNL        REF    ENVIRON MICROBIOL             V.  17   332 2015
JRNL        REFN
JRNL        PMID   25330254
JRNL        DOI    10.1111/1462-2920.12660
REMARK   2
REMARK   2 RESOLUTION.    1.74 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.72
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 271731
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.147
REMARK   3   R VALUE            (WORKING SET) : 0.145
REMARK   3   FREE R VALUE                     : 0.185
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050
REMARK   3   FREE R VALUE TEST SET COUNT      : 13720
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 19.7249 -  5.3712    0.94     8263   440  0.1853 0.2043
REMARK   3     2  5.3712 -  4.2775    0.97     8454   458  0.1356 0.1558
REMARK   3     3  4.2775 -  3.7410    0.99     8566   443  0.1197 0.1520
REMARK   3     4  3.7410 -  3.4009    0.99     8620   442  0.1238 0.1500
REMARK   3     5  3.4009 -  3.1582    1.00     8638   471  0.1315 0.1661
REMARK   3     6  3.1582 -  2.9726    1.00     8640   429  0.1369 0.1782
REMARK   3     7  2.9726 -  2.8242    1.00     8673   459  0.1369 0.1747
REMARK   3     8  2.8242 -  2.7016    1.00     8633   463  0.1313 0.1833
REMARK   3     9  2.7016 -  2.5978    1.00     8657   458  0.1385 0.1869
REMARK   3    10  2.5978 -  2.5084    1.00     8578   470  0.1374 0.1911
REMARK   3    11  2.5084 -  2.4301    1.00     8675   440  0.1331 0.1915
REMARK   3    12  2.4301 -  2.3607    1.00     8648   469  0.1336 0.1720
REMARK   3    13  2.3607 -  2.2987    1.00     8539   484  0.1343 0.1784
REMARK   3    14  2.2987 -  2.2427    1.00     8667   449  0.1582 0.2257
REMARK   3    15  2.2427 -  2.1918    1.00     8597   447  0.1456 0.1962
REMARK   3    16  2.1918 -  2.1452    1.00     8660   453  0.1336 0.1702
REMARK   3    17  2.1452 -  2.1023    1.00     8598   459  0.1343 0.1876
REMARK   3    18  2.1023 -  2.0627    1.00     8591   451  0.1483 0.1958
REMARK   3    19  2.0627 -  2.0259    1.00     8617   451  0.1555 0.1990
REMARK   3    20  2.0259 -  1.9916    1.00     8625   485  0.1469 0.1913
REMARK   3    21  1.9916 -  1.9595    1.00     8631   432  0.1512 0.1912
REMARK   3    22  1.9595 -  1.9294    1.00     8553   491  0.1637 0.2150
REMARK   3    23  1.9294 -  1.9010    1.00     8599   465  0.1903 0.2335
REMARK   3    24  1.9010 -  1.8743    1.00     8600   440  0.1822 0.2354
REMARK   3    25  1.8743 -  1.8489    1.00     8655   453  0.1833 0.2340
REMARK   3    26  1.8489 -  1.8249    1.00     8557   500  0.1819 0.2414
REMARK   3    27  1.8249 -  1.8021    1.00     8608   437  0.1839 0.2256
REMARK   3    28  1.8021 -  1.7804    1.00     8637   471  0.1883 0.2292
REMARK   3    29  1.7804 -  1.7598    1.00     8621   448  0.2000 0.2530
REMARK   3    30  1.7598 -  1.7400    1.00     8611   462  0.2028 0.2505
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)     : 0.160
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.200
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
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      :  0.015          20641
REMARK   3   ANGLE     :  1.482          28138
REMARK   3   CHIRALITY :  0.083           3172
REMARK   3   PLANARITY :  0.008           3572
REMARK   3   DIHEDRAL  : 14.074           7600
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 32
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: (chain A and resid 31:60 )
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3325 -23.0825  25.7834
REMARK   3    T TENSOR
REMARK   3      T11:   0.3670 T22:   0.2256
REMARK   3      T33:   0.2127 T12:  -0.0649
REMARK   3      T13:   0.0195 T23:   0.1037
REMARK   3    L TENSOR
REMARK   3      L11:   2.8078 L22:   3.8453
REMARK   3      L33:   7.1632 L12:  -1.2582
REMARK   3      L13:  -1.4264 L23:   5.1896
REMARK   3    S TENSOR
REMARK   3      S11:   0.0802 S12:  -0.2993 S13:  -0.4747
REMARK   3      S21:   0.4954 S22:  -0.3131 S23:   0.2445
REMARK   3      S31:   1.0117 S32:  -0.4626 S33:   0.1961
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: (chain A and resid 61:189 )
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1756 -10.7277   6.5930
REMARK   3    T TENSOR
REMARK   3      T11:   0.0654 T22:   0.1740
REMARK   3      T33:   0.1402 T12:  -0.0304
REMARK   3      T13:   0.0027 T23:   0.0013
REMARK   3    L TENSOR
REMARK   3      L11:   2.4658 L22:   2.4047
REMARK   3      L33:   1.8751 L12:  -0.3317
REMARK   3      L13:   0.2465 L23:   0.5588
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0695 S12:  -0.0200 S13:   0.0295
REMARK   3      S21:   0.0545 S22:  -0.0098 S23:   0.1850
REMARK   3      S31:   0.0488 S32:  -0.3079 S33:   0.0519
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: (chain A and resid 190:336 )
REMARK   3    ORIGIN FOR THE GROUP (A):  29.2352 -11.4978   8.2625
REMARK   3    T TENSOR
REMARK   3      T11:   0.0604 T22:   0.0832
REMARK   3      T33:   0.0889 T12:  -0.0175
REMARK   3      T13:   0.0044 T23:   0.0056
REMARK   3    L TENSOR
REMARK   3      L11:   0.9946 L22:   0.7731
REMARK   3      L33:   1.1531 L12:  -0.0377
REMARK   3      L13:   0.2620 L23:   0.0595
REMARK   3    S TENSOR
REMARK   3      S11:   0.0002 S12:  -0.0025 S13:   0.0149
REMARK   3      S21:   0.0130 S22:   0.0273 S23:   0.0265
REMARK   3      S31:   0.0604 S32:  -0.0620 S33:  -0.0226
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: (chain A and resid 337:347 )
REMARK   3    ORIGIN FOR THE GROUP (A):  22.2919   4.9750  15.3028
REMARK   3    T TENSOR
REMARK   3      T11:   0.2152 T22:   0.1587
REMARK   3      T33:   0.2159 T12:   0.0352
REMARK   3      T13:  -0.0762 T23:  -0.1029
REMARK   3    L TENSOR
REMARK   3      L11:   7.4549 L22:   6.5248
REMARK   3      L33:   8.0008 L12:   1.9792
REMARK   3      L13:  -5.9674 L23:  -4.9272
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1506 S12:  -0.4618 S13:   0.5574
REMARK   3      S21:   0.4082 S22:  -0.1037 S23:  -0.1289
REMARK   3      S31:  -0.6497 S32:   0.2007 S33:   0.1469
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: (chain B and resid 31:51 )
REMARK   3    ORIGIN FOR THE GROUP (A):  51.2308 -17.8977  10.3426
REMARK   3    T TENSOR
REMARK   3      T11:   0.1881 T22:   0.1297
REMARK   3      T33:   0.1374 T12:   0.0472
REMARK   3      T13:   0.0149 T23:  -0.0236
REMARK   3    L TENSOR
REMARK   3      L11:   7.8084 L22:   9.0047
REMARK   3      L33:   5.8965 L12:   1.5658
REMARK   3      L13:   1.7652 L23:  -2.1860
REMARK   3    S TENSOR
REMARK   3      S11:   0.1701 S12:  -0.3152 S13:  -0.5061
REMARK   3      S21:   0.4826 S22:  -0.1146 S23:  -0.2443
REMARK   3      S31:   0.4345 S32:   0.2696 S33:   0.0120
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: (chain B and resid 52:67 )
REMARK   3    ORIGIN FOR THE GROUP (A):  57.3910 -20.5766  34.5862
REMARK   3    T TENSOR
REMARK   3      T11:   0.1491 T22:   0.1108
REMARK   3      T33:   0.1504 T12:   0.0164
REMARK   3      T13:   0.0008 T23:   0.0030
REMARK   3    L TENSOR
REMARK   3      L11:   4.4225 L22:   6.0955
REMARK   3      L33:   3.5530 L12:   4.9061
REMARK   3      L13:   3.9100 L23:   4.5402
REMARK   3    S TENSOR
REMARK   3      S11:   0.0056 S12:  -0.1412 S13:  -0.2221
REMARK   3      S21:  -0.1858 S22:  -0.0046 S23:  -0.1232
REMARK   3      S31:  -0.0318 S32:  -0.1018 S33:   0.0669
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: (chain B and resid 68:88 )
REMARK   3    ORIGIN FOR THE GROUP (A):  66.6093  -5.9475  26.2656
REMARK   3    T TENSOR
REMARK   3      T11:   0.1250 T22:   0.1185
REMARK   3      T33:   0.2025 T12:   0.0250
REMARK   3      T13:  -0.0498 T23:  -0.0338
REMARK   3    L TENSOR
REMARK   3      L11:   0.5944 L22:   7.6130
REMARK   3      L33:   5.9697 L12:   1.3356
REMARK   3      L13:  -1.1427 L23:  -6.7644
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0188 S12:   0.0359 S13:  -0.1326
REMARK   3      S21:  -0.0007 S22:  -0.1339 S23:  -0.3411
REMARK   3      S31:   0.0757 S32:   0.1778 S33:   0.2772
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: (chain B and resid 89:347 )
REMARK   3    ORIGIN FOR THE GROUP (A):  49.1078   2.2171  25.9104
REMARK   3    T TENSOR
REMARK   3      T11:   0.0973 T22:   0.0754
REMARK   3      T33:   0.0836 T12:   0.0139
REMARK   3      T13:  -0.0060 T23:  -0.0210
REMARK   3    L TENSOR
REMARK   3      L11:   0.8657 L22:   0.6308
REMARK   3      L33:   0.7134 L12:   0.3041
REMARK   3      L13:   0.0975 L23:   0.0443
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0021 S12:  -0.0783 S13:   0.0986
REMARK   3      S21:   0.0673 S22:  -0.0219 S23:   0.0390
REMARK   3      S31:  -0.0965 S32:  -0.0498 S33:   0.0162
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: (chain C and resid 32:51 )
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5195 -50.2268 -44.4056
REMARK   3    T TENSOR
REMARK   3      T11:   0.1190 T22:   0.1436
REMARK   3      T33:   0.1154 T12:   0.0280
REMARK   3      T13:   0.0306 T23:  -0.0107
REMARK   3    L TENSOR
REMARK   3      L11:   7.9831 L22:   8.6636
REMARK   3      L33:   4.6490 L12:   2.3953
REMARK   3      L13:  -0.1831 L23:   1.0563
REMARK   3    S TENSOR
REMARK   3      S11:   0.0282 S12:  -0.4800 S13:  -0.3523
REMARK   3      S21:   0.4356 S22:  -0.0960 S23:  -0.3066
REMARK   3      S31:   0.3744 S32:   0.3310 S33:   0.0500
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: (chain C and resid 52:64 )
REMARK   3    ORIGIN FOR THE GROUP (A):  21.3237 -55.4539 -21.3948
REMARK   3    T TENSOR
REMARK   3      T11:   0.1890 T22:   0.1572
REMARK   3      T33:   0.2076 T12:   0.0519
REMARK   3      T13:   0.0170 T23:  -0.0076
REMARK   3    L TENSOR
REMARK   3      L11:   3.6752 L22:   7.0703
REMARK   3      L33:   5.1446 L12:   4.8815
REMARK   3      L13:   4.3325 L23:   5.9089
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0181 S12:  -0.0631 S13:  -0.1887
REMARK   3      S21:  -0.2040 S22:   0.1013 S23:  -0.3452
REMARK   3      S31:   0.0800 S32:   0.0549 S33:  -0.0880
REMARK   3   TLS GROUP : 11
REMARK   3    SELECTION: (chain C and resid 65:91 )
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7293 -38.8408 -27.6899
REMARK   3    T TENSOR
REMARK   3      T11:   0.1432 T22:   0.1431
REMARK   3      T33:   0.2416 T12:   0.0289
REMARK   3      T13:  -0.0407 T23:  -0.0449
REMARK   3    L TENSOR
REMARK   3      L11:   0.1448 L22:   7.0555
REMARK   3      L33:   6.3180 L12:   0.5333
REMARK   3      L13:  -0.5294 L23:  -6.7078
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1289 S12:  -0.0275 S13:  -0.1112
REMARK   3      S21:   0.2037 S22:  -0.1795 S23:  -0.6146
REMARK   3      S31:  -0.1777 S32:   0.2258 S33:   0.4256
REMARK   3   TLS GROUP : 12
REMARK   3    SELECTION: (chain C and resid 92:347 )
REMARK   3    ORIGIN FOR THE GROUP (A):  12.9913 -31.8589 -27.8200
REMARK   3    T TENSOR
REMARK   3      T11:   0.1168 T22:   0.1051
REMARK   3      T33:   0.1014 T12:   0.0362
REMARK   3      T13:  -0.0049 T23:  -0.0396
REMARK   3    L TENSOR
REMARK   3      L11:   0.8182 L22:   0.6922
REMARK   3      L33:   0.9536 L12:   0.2218
REMARK   3      L13:   0.1326 L23:  -0.0361
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0275 S12:  -0.1349 S13:   0.1059
REMARK   3      S21:   0.1225 S22:  -0.0083 S23:   0.0015
REMARK   3      S31:  -0.1281 S32:  -0.0919 S33:   0.0140
REMARK   3   TLS GROUP : 13
REMARK   3    SELECTION: (chain D and resid 32:51 )
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2760  15.9307 -44.7719
REMARK   3    T TENSOR
REMARK   3      T11:   0.1782 T22:   0.1124
REMARK   3      T33:   0.2077 T12:   0.0518
REMARK   3      T13:  -0.0101 T23:  -0.0326
REMARK   3    L TENSOR
REMARK   3      L11:   7.0013 L22:   8.8552
REMARK   3      L33:   7.9724 L12:   0.4213
REMARK   3      L13:  -0.9198 L23:  -2.7470
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0641 S12:  -0.2989 S13:  -0.4657
REMARK   3      S21:   0.4624 S22:  -0.0860 S23:  -0.2776
REMARK   3      S31:   0.4520 S32:   0.4638 S33:   0.0809
REMARK   3   TLS GROUP : 14
REMARK   3    SELECTION: (chain D and resid 52:90 )
REMARK   3    ORIGIN FOR THE GROUP (A):  30.2358  22.7772 -27.2957
REMARK   3    T TENSOR
REMARK   3      T11:   0.1504 T22:   0.1127
REMARK   3      T33:   0.2171 T12:   0.0362
REMARK   3      T13:  -0.0074 T23:   0.0031
REMARK   3    L TENSOR
REMARK   3      L11:   0.0424 L22:   3.0435
REMARK   3      L33:   2.6148 L12:   0.1819
REMARK   3      L13:  -0.1062 L23:  -2.8204
REMARK   3    S TENSOR
REMARK   3      S11:   0.0161 S12:  -0.0401 S13:  -0.1268
REMARK   3      S21:  -0.0300 S22:  -0.0632 S23:  -0.1153
REMARK   3      S31:   0.0472 S32:   0.1105 S33:   0.0840
REMARK   3   TLS GROUP : 15
REMARK   3    SELECTION: (chain D and resid 91:323 )
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1233  34.2089 -26.5154
REMARK   3    T TENSOR
REMARK   3      T11:   0.1047 T22:   0.0950
REMARK   3      T33:   0.0970 T12:   0.0024
REMARK   3      T13:  -0.0019 T23:  -0.0160
REMARK   3    L TENSOR
REMARK   3      L11:   0.9784 L22:   0.6495
REMARK   3      L33:   0.7262 L12:   0.4257
REMARK   3      L13:   0.3012 L23:   0.0068
REMARK   3    S TENSOR
REMARK   3      S11:   0.0545 S12:  -0.1729 S13:   0.0490
REMARK   3      S21:   0.0829 S22:  -0.0700 S23:   0.0679
REMARK   3      S31:  -0.0244 S32:  -0.1058 S33:   0.0072
REMARK   3   TLS GROUP : 16
REMARK   3    SELECTION: (chain D and resid 324:347 )
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2726  35.1487 -42.0051
REMARK   3    T TENSOR
REMARK   3      T11:   0.0929 T22:   0.0598
REMARK   3      T33:   0.1177 T12:  -0.0281
REMARK   3      T13:  -0.0324 T23:   0.0047
REMARK   3    L TENSOR
REMARK   3      L11:   4.1339 L22:   5.4481
REMARK   3      L33:   3.9165 L12:  -3.3658
REMARK   3      L13:  -1.7029 L23:   2.8553
REMARK   3    S TENSOR
REMARK   3      S11:   0.0615 S12:   0.1703 S13:   0.1270
REMARK   3      S21:  -0.1648 S22:  -0.1287 S23:  -0.0403
REMARK   3      S31:  -0.1473 S32:  -0.1783 S33:   0.0569
REMARK   3   TLS GROUP : 17
REMARK   3    SELECTION: (chain E and resid 32:50 )
REMARK   3    ORIGIN FOR THE GROUP (A):  42.2824 -17.0279  -9.4698
REMARK   3    T TENSOR
REMARK   3      T11:   0.1770 T22:   0.1214
REMARK   3      T33:   0.0982 T12:  -0.0230
REMARK   3      T13:   0.0367 T23:   0.0315
REMARK   3    L TENSOR
REMARK   3      L11:   8.3786 L22:   7.1867
REMARK   3      L33:   8.8409 L12:  -0.2731
REMARK   3      L13:  -0.7737 L23:   3.9194
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1392 S12:   0.3331 S13:  -0.3299
REMARK   3      S21:  -0.2826 S22:  -0.1010 S23:   0.2435
REMARK   3      S31:   0.5083 S32:  -0.2938 S33:   0.1758
REMARK   3   TLS GROUP : 18
REMARK   3    SELECTION: (chain E and resid 51:65 )
REMARK   3    ORIGIN FOR THE GROUP (A):  36.8598 -22.4827 -32.3477
REMARK   3    T TENSOR
REMARK   3      T11:   0.2773 T22:   0.2129
REMARK   3      T33:   0.3005 T12:  -0.0486
REMARK   3      T13:   0.0049 T23:  -0.0346
REMARK   3    L TENSOR
REMARK   3      L11:   5.5945 L22:   4.5036
REMARK   3      L33:   8.0762 L12:  -3.0318
REMARK   3      L13:   5.4924 L23:  -4.9096
REMARK   3    S TENSOR
REMARK   3      S11:   0.3510 S12:  -0.0521 S13:  -0.2273
REMARK   3      S21:   0.1898 S22:  -0.0626 S23:   0.2264
REMARK   3      S31:   0.1358 S32:   0.0437 S33:  -0.2352
REMARK   3   TLS GROUP : 19
REMARK   3    SELECTION: (chain E and resid 66:90 )
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9605  -5.7032 -26.7958
REMARK   3    T TENSOR
REMARK   3      T11:   0.0568 T22:   0.1088
REMARK   3      T33:   0.2231 T12:  -0.0234
REMARK   3      T13:  -0.0203 T23:   0.0173
REMARK   3    L TENSOR
REMARK   3      L11:   0.4336 L22:   6.2474
REMARK   3      L33:   1.9741 L12:  -0.1585
REMARK   3      L13:  -0.1145 L23:   2.2896
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0721 S12:   0.0216 S13:  -0.1375
REMARK   3      S21:  -0.1809 S22:  -0.1330 S23:   0.4051
REMARK   3      S31:   0.0177 S32:  -0.1857 S33:   0.3254
REMARK   3   TLS GROUP : 20
REMARK   3    SELECTION: (chain E and resid 91:347 )
REMARK   3    ORIGIN FOR THE GROUP (A):  47.2348   0.2607 -27.2975
REMARK   3    T TENSOR
REMARK   3      T11:   0.1107 T22:   0.1303
REMARK   3      T33:   0.0943 T12:  -0.0224
REMARK   3      T13:  -0.0004 T23:   0.0378
REMARK   3    L TENSOR
REMARK   3      L11:   0.8019 L22:   0.8966
REMARK   3      L33:   1.2083 L12:  -0.2514
REMARK   3      L13:   0.0345 L23:   0.1325
REMARK   3    S TENSOR
REMARK   3      S11:   0.0143 S12:   0.1571 S13:   0.1009
REMARK   3      S21:  -0.1416 S22:  -0.0274 S23:  -0.0101
REMARK   3      S31:  -0.0882 S32:   0.1603 S33:  -0.0011
REMARK   3   TLS GROUP : 21
REMARK   3    SELECTION: (chain F and resid 32:59 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4628 -57.5098 -29.2331
REMARK   3    T TENSOR
REMARK   3      T11:   0.3254 T22:   0.3297
REMARK   3      T33:   0.2110 T12:  -0.0536
REMARK   3      T13:   0.0476 T23:   0.0845
REMARK   3    L TENSOR
REMARK   3      L11:   1.2282 L22:   4.9817
REMARK   3      L33:   8.0456 L12:  -1.6989
REMARK   3      L13:  -2.2173 L23:   6.2082
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0281 S12:  -0.2089 S13:  -0.3925
REMARK   3      S21:   0.5963 S22:  -0.1723 S23:   0.2314
REMARK   3      S31:   0.9568 S32:  -0.5350 S33:   0.2666
REMARK   3   TLS GROUP : 22
REMARK   3    SELECTION: (chain F and resid 60:89 )
REMARK   3    ORIGIN FOR THE GROUP (A): -21.4679 -60.3979 -44.2188
REMARK   3    T TENSOR
REMARK   3      T11:   0.2373 T22:   0.4186
REMARK   3      T33:   0.4212 T12:  -0.0611
REMARK   3      T13:   0.0198 T23:   0.1969
REMARK   3    L TENSOR
REMARK   3      L11:   7.3712 L22:   7.4225
REMARK   3      L33:   7.9100 L12:  -1.9179
REMARK   3      L13:  -3.6138 L23:   5.3129
REMARK   3    S TENSOR
REMARK   3      S11:   0.1273 S12:  -0.0899 S13:  -0.9735
REMARK   3      S21:   0.4019 S22:   0.2408 S23:   0.0352
REMARK   3      S31:   0.2669 S32:  -0.3332 S33:  -0.0929
REMARK   3   TLS GROUP : 23
REMARK   3    SELECTION: (chain F and resid 90:189 )
REMARK   3    ORIGIN FOR THE GROUP (A): -22.1470 -41.7543 -50.8386
REMARK   3    T TENSOR
REMARK   3      T11:   0.0719 T22:   0.2166
REMARK   3      T33:   0.1554 T12:   0.0093
REMARK   3      T13:   0.0097 T23:   0.0071
REMARK   3    L TENSOR
REMARK   3      L11:   1.7927 L22:   2.2903
REMARK   3      L33:   1.3944 L12:  -0.2204
REMARK   3      L13:  -0.2413 L23:   0.4429
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0532 S12:  -0.0624 S13:   0.1059
REMARK   3      S21:  -0.0493 S22:   0.0444 S23:   0.2602
REMARK   3      S31:  -0.0794 S32:  -0.3312 S33:   0.0148
REMARK   3   TLS GROUP : 24
REMARK   3    SELECTION: (chain F and resid 190:347 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8219 -44.6958 -46.2292
REMARK   3    T TENSOR
REMARK   3      T11:   0.0602 T22:   0.1169
REMARK   3      T33:   0.0804 T12:  -0.0070
REMARK   3      T13:   0.0212 T23:  -0.0083
REMARK   3    L TENSOR
REMARK   3      L11:   0.8394 L22:   0.6518
REMARK   3      L33:   1.0690 L12:  -0.0418
REMARK   3      L13:   0.2356 L23:  -0.1559
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0214 S12:  -0.1047 S13:  -0.0008
REMARK   3      S21:   0.0733 S22:   0.0190 S23:   0.0580
REMARK   3      S31:  -0.0262 S32:  -0.1375 S33:   0.0082
REMARK   3   TLS GROUP : 25
REMARK   3    SELECTION: (chain G and resid 32:59 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.4808   8.4193 -28.0382
REMARK   3    T TENSOR
REMARK   3      T11:   0.4284 T22:   0.3063
REMARK   3      T33:   0.3297 T12:  -0.1569
REMARK   3      T13:  -0.0399 T23:   0.0929
REMARK   3    L TENSOR
REMARK   3      L11:   0.3345 L22:   3.3168
REMARK   3      L33:   1.4710 L12:   0.0720
REMARK   3      L13:   0.1548 L23:   2.1774
REMARK   3    S TENSOR
REMARK   3      S11:   0.1437 S12:  -0.3565 S13:  -0.4158
REMARK   3      S21:   0.2406 S22:  -0.1576 S23:  -0.0243
REMARK   3      S31:   0.6698 S32:  -0.2729 S33:   0.0224
REMARK   3   TLS GROUP : 26
REMARK   3    SELECTION: (chain G and resid 60:91 )
REMARK   3    ORIGIN FOR THE GROUP (A): -20.7602   6.6318 -41.6800
REMARK   3    T TENSOR
REMARK   3      T11:   0.4383 T22:   0.4179
REMARK   3      T33:   0.3905 T12:  -0.2049
REMARK   3      T13:  -0.0099 T23:   0.0152
REMARK   3    L TENSOR
REMARK   3      L11:   2.8005 L22:   5.6845
REMARK   3      L33:   2.3020 L12:  -2.1694
REMARK   3      L13:  -1.9638 L23:   2.2777
REMARK   3    S TENSOR
REMARK   3      S11:   0.0995 S12:  -0.1297 S13:  -0.6181
REMARK   3      S21:   0.6469 S22:  -0.2189 S23:   0.3814
REMARK   3      S31:   0.3088 S32:  -0.3202 S33:   0.0407
REMARK   3   TLS GROUP : 27
REMARK   3    SELECTION: (chain G and resid 92:189 )
REMARK   3    ORIGIN FOR THE GROUP (A): -21.7883  24.0876 -48.5280
REMARK   3    T TENSOR
REMARK   3      T11:   0.0930 T22:   0.2564
REMARK   3      T33:   0.1537 T12:  -0.0207
REMARK   3      T13:   0.0040 T23:  -0.0398
REMARK   3    L TENSOR
REMARK   3      L11:   1.3786 L22:   1.9742
REMARK   3      L33:   1.6121 L12:  -0.1204
REMARK   3      L13:  -0.1080 L23:   0.5973
REMARK   3    S TENSOR
REMARK   3      S11:   0.0154 S12:   0.0297 S13:   0.0073
REMARK   3      S21:   0.0076 S22:  -0.1553 S23:   0.2383
REMARK   3      S31:  -0.0111 S32:  -0.4639 S33:  -0.0171
REMARK   3   TLS GROUP : 28
REMARK   3    SELECTION: (chain G and resid 190:347 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1779  21.4429 -44.9953
REMARK   3    T TENSOR
REMARK   3      T11:   0.0768 T22:   0.1017
REMARK   3      T33:   0.1072 T12:  -0.0315
REMARK   3      T13:  -0.0051 T23:  -0.0054
REMARK   3    L TENSOR
REMARK   3      L11:   1.0450 L22:   0.7795
REMARK   3      L33:   1.1954 L12:  -0.0916
REMARK   3      L13:   0.2596 L23:   0.0136
REMARK   3    S TENSOR
REMARK   3      S11:   0.0307 S12:  -0.0801 S13:  -0.0711
REMARK   3      S21:   0.0640 S22:  -0.0058 S23:  -0.0291
REMARK   3      S31:   0.0559 S32:  -0.1347 S33:  -0.0381
REMARK   3   TLS GROUP : 29
REMARK   3    SELECTION: (chain H and resid 32:60 )
REMARK   3    ORIGIN FOR THE GROUP (A):  66.0903 -27.4711 -24.7844
REMARK   3    T TENSOR
REMARK   3      T11:   0.3766 T22:   0.3255
REMARK   3      T33:   0.2167 T12:   0.1485
REMARK   3      T13:   0.0094 T23:  -0.0802
REMARK   3    L TENSOR
REMARK   3      L11:   4.1257 L22:   6.3564
REMARK   3      L33:   5.1564 L12:   2.3928
REMARK   3      L13:  -3.6560 L23:  -3.6339
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0958 S12:  -0.0167 S13:  -0.5400
REMARK   3      S21:  -0.0367 S22:  -0.3139 S23:  -0.3311
REMARK   3      S31:   0.7335 S32:   0.5750 S33:   0.4082
REMARK   3   TLS GROUP : 30
REMARK   3    SELECTION: (chain H and resid 61:87 )
REMARK   3    ORIGIN FOR THE GROUP (A):  79.6419 -31.1396 -10.0252
REMARK   3    T TENSOR
REMARK   3      T11:   0.3681 T22:   0.4322
REMARK   3      T33:   0.4398 T12:   0.2187
REMARK   3      T13:  -0.0132 T23:  -0.0389
REMARK   3    L TENSOR
REMARK   3      L11:   7.6387 L22:   4.1364
REMARK   3      L33:   3.9181 L12:   1.3537
REMARK   3      L13:  -2.2872 L23:  -0.5592
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0462 S12:   0.0172 S13:  -1.0013
REMARK   3      S21:  -0.3167 S22:  -0.1003 S23:  -0.4502
REMARK   3      S31:   0.5716 S32:   0.2951 S33:   0.1701
REMARK   3   TLS GROUP : 31
REMARK   3    SELECTION: (chain H and resid 88:189 )
REMARK   3    ORIGIN FOR THE GROUP (A):  82.5480 -11.7464  -5.7687
REMARK   3    T TENSOR
REMARK   3      T11:   0.1338 T22:   0.3442
REMARK   3      T33:   0.2174 T12:   0.0325
REMARK   3      T13:  -0.0021 T23:   0.0121
REMARK   3    L TENSOR
REMARK   3      L11:   2.1041 L22:   2.8122
REMARK   3      L33:   1.5738 L12:   0.1856
REMARK   3      L13:  -0.5001 L23:  -0.7095
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0359 S12:  -0.0280 S13:   0.0762
REMARK   3      S21:   0.0662 S22:  -0.0682 S23:  -0.4314
REMARK   3      S31:  -0.0036 S32:   0.4898 S33:   0.0848
REMARK   3   TLS GROUP : 32
REMARK   3    SELECTION: (chain H and resid 190:347 )
REMARK   3    ORIGIN FOR THE GROUP (A):  65.8388 -13.2111  -9.0775
REMARK   3    T TENSOR
REMARK   3      T11:   0.1174 T22:   0.2052
REMARK   3      T33:   0.1084 T12:   0.0560
REMARK   3      T13:   0.0089 T23:  -0.0099
REMARK   3    L TENSOR
REMARK   3      L11:   0.8321 L22:   0.7762
REMARK   3      L33:   1.1704 L12:  -0.0656
REMARK   3      L13:   0.2176 L23:  -0.0174
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0113 S12:   0.0507 S13:  -0.0248
REMARK   3      S21:  -0.0167 S22:   0.0260 S23:  -0.0884
REMARK   3      S31:   0.0944 S32:   0.2189 S33:  -0.0112
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 4Q3O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085563.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-13
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 272067
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.740
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.720
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : 3.000
REMARK 200  R MERGE                    (I) : 0.05600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 21.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.39200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.PHASER)
REMARK 200 STARTING MODEL: PDB ENTRY 3FAK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 20% PEG10K.
REMARK 280  CRYROPROTECTANT: 12% GLYCEROL THEN PARATON-N OIL, PH 6.0, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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       94.72700
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       65.69850
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       94.72700
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       65.69850
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 569  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 700  LIES ON A SPECIAL POSITION.
REMARK 375      HOH H 714  LIES ON A SPECIAL POSITION.
REMARK 450
REMARK 450 SOURCE
REMARK 450 The sample has been obtained from Lake Matapan deep-sea and
REMARK 450 identified using the technique metagenome library
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     1
REMARK 465     HIS A     2
REMARK 465     ARG A     3
REMARK 465     TYR A     4
REMARK 465     GLY A     5
REMARK 465     LEU A     6
REMARK 465     LEU A     7
REMARK 465     VAL A     8
REMARK 465     PHE A     9
REMARK 465     CYS A    10
REMARK 465     SER A    11
REMARK 465     LEU A    12
REMARK 465     VAL A    13
REMARK 465     ILE A    14
REMARK 465     LEU A    15
REMARK 465     MET A    16
REMARK 465     VAL A    17
REMARK 465     GLN A    18
REMARK 465     GLY A    19
REMARK 465     VAL A    20
REMARK 465     ASN A    21
REMARK 465     LYS A    22
REMARK 465     ALA A    23
REMARK 465     VAL A    24
REMARK 465     ALA A    25
REMARK 465     GLY A    26
REMARK 465     GLU A    27
REMARK 465     GLN A    28
REMARK 465     ALA A    29
REMARK 465     LYS A    30
REMARK 465     ASN A   348
REMARK 465     MET B     1
REMARK 465     HIS B     2
REMARK 465     ARG B     3
REMARK 465     TYR B     4
REMARK 465     GLY B     5
REMARK 465     LEU B     6
REMARK 465     LEU B     7
REMARK 465     VAL B     8
REMARK 465     PHE B     9
REMARK 465     CYS B    10
REMARK 465     SER B    11
REMARK 465     LEU B    12
REMARK 465     VAL B    13
REMARK 465     ILE B    14
REMARK 465     LEU B    15
REMARK 465     MET B    16
REMARK 465     VAL B    17
REMARK 465     GLN B    18
REMARK 465     GLY B    19
REMARK 465     VAL B    20
REMARK 465     ASN B    21
REMARK 465     LYS B    22
REMARK 465     ALA B    23
REMARK 465     VAL B    24
REMARK 465     ALA B    25
REMARK 465     GLY B    26
REMARK 465     GLU B    27
REMARK 465     GLN B    28
REMARK 465     ALA B    29
REMARK 465     LYS B    30
REMARK 465     ASN B   348
REMARK 465     MET C     1
REMARK 465     HIS C     2
REMARK 465     ARG C     3
REMARK 465     TYR C     4
REMARK 465     GLY C     5
REMARK 465     LEU C     6
REMARK 465     LEU C     7
REMARK 465     VAL C     8
REMARK 465     PHE C     9
REMARK 465     CYS C    10
REMARK 465     SER C    11
REMARK 465     LEU C    12
REMARK 465     VAL C    13
REMARK 465     ILE C    14
REMARK 465     LEU C    15
REMARK 465     MET C    16
REMARK 465     VAL C    17
REMARK 465     GLN C    18
REMARK 465     GLY C    19
REMARK 465     VAL C    20
REMARK 465     ASN C    21
REMARK 465     LYS C    22
REMARK 465     ALA C    23
REMARK 465     VAL C    24
REMARK 465     ALA C    25
REMARK 465     GLY C    26
REMARK 465     GLU C    27
REMARK 465     GLN C    28
REMARK 465     ALA C    29
REMARK 465     LYS C    30
REMARK 465     GLU C    31
REMARK 465     ASN C   348
REMARK 465     MET D     1
REMARK 465     HIS D     2
REMARK 465     ARG D     3
REMARK 465     TYR D     4
REMARK 465     GLY D     5
REMARK 465     LEU D     6
REMARK 465     LEU D     7
REMARK 465     VAL D     8
REMARK 465     PHE D     9
REMARK 465     CYS D    10
REMARK 465     SER D    11
REMARK 465     LEU D    12
REMARK 465     VAL D    13
REMARK 465     ILE D    14
REMARK 465     LEU D    15
REMARK 465     MET D    16
REMARK 465     VAL D    17
REMARK 465     GLN D    18
REMARK 465     GLY D    19
REMARK 465     VAL D    20
REMARK 465     ASN D    21
REMARK 465     LYS D    22
REMARK 465     ALA D    23
REMARK 465     VAL D    24
REMARK 465     ALA D    25
REMARK 465     GLY D    26
REMARK 465     GLU D    27
REMARK 465     GLN D    28
REMARK 465     ALA D    29
REMARK 465     LYS D    30
REMARK 465     GLU D    31
REMARK 465     ASN D   348
REMARK 465     MET E     1
REMARK 465     HIS E     2
REMARK 465     ARG E     3
REMARK 465     TYR E     4
REMARK 465     GLY E     5
REMARK 465     LEU E     6
REMARK 465     LEU E     7
REMARK 465     VAL E     8
REMARK 465     PHE E     9
REMARK 465     CYS E    10
REMARK 465     SER E    11
REMARK 465     LEU E    12
REMARK 465     VAL E    13
REMARK 465     ILE E    14
REMARK 465     LEU E    15
REMARK 465     MET E    16
REMARK 465     VAL E    17
REMARK 465     GLN E    18
REMARK 465     GLY E    19
REMARK 465     VAL E    20
REMARK 465     ASN E    21
REMARK 465     LYS E    22
REMARK 465     ALA E    23
REMARK 465     VAL E    24
REMARK 465     ALA E    25
REMARK 465     GLY E    26
REMARK 465     GLU E    27
REMARK 465     GLN E    28
REMARK 465     ALA E    29
REMARK 465     LYS E    30
REMARK 465     GLU E    31
REMARK 465     ASN E   348
REMARK 465     MET F     1
REMARK 465     HIS F     2
REMARK 465     ARG F     3
REMARK 465     TYR F     4
REMARK 465     GLY F     5
REMARK 465     LEU F     6
REMARK 465     LEU F     7
REMARK 465     VAL F     8
REMARK 465     PHE F     9
REMARK 465     CYS F    10
REMARK 465     SER F    11
REMARK 465     LEU F    12
REMARK 465     VAL F    13
REMARK 465     ILE F    14
REMARK 465     LEU F    15
REMARK 465     MET F    16
REMARK 465     VAL F    17
REMARK 465     GLN F    18
REMARK 465     GLY F    19
REMARK 465     VAL F    20
REMARK 465     ASN F    21
REMARK 465     LYS F    22
REMARK 465     ALA F    23
REMARK 465     VAL F    24
REMARK 465     ALA F    25
REMARK 465     GLY F    26
REMARK 465     GLU F    27
REMARK 465     GLN F    28
REMARK 465     ALA F    29
REMARK 465     LYS F    30
REMARK 465     GLU F    31
REMARK 465     ASN F   348
REMARK 465     MET G     1
REMARK 465     HIS G     2
REMARK 465     ARG G     3
REMARK 465     TYR G     4
REMARK 465     GLY G     5
REMARK 465     LEU G     6
REMARK 465     LEU G     7
REMARK 465     VAL G     8
REMARK 465     PHE G     9
REMARK 465     CYS G    10
REMARK 465     SER G    11
REMARK 465     LEU G    12
REMARK 465     VAL G    13
REMARK 465     ILE G    14
REMARK 465     LEU G    15
REMARK 465     MET G    16
REMARK 465     VAL G    17
REMARK 465     GLN G    18
REMARK 465     GLY G    19
REMARK 465     VAL G    20
REMARK 465     ASN G    21
REMARK 465     LYS G    22
REMARK 465     ALA G    23
REMARK 465     VAL G    24
REMARK 465     ALA G    25
REMARK 465     GLY G    26
REMARK 465     GLU G    27
REMARK 465     GLN G    28
REMARK 465     ALA G    29
REMARK 465     LYS G    30
REMARK 465     GLU G    31
REMARK 465     ASN G   348
REMARK 465     MET H     1
REMARK 465     HIS H     2
REMARK 465     ARG H     3
REMARK 465     TYR H     4
REMARK 465     GLY H     5
REMARK 465     LEU H     6
REMARK 465     LEU H     7
REMARK 465     VAL H     8
REMARK 465     PHE H     9
REMARK 465     CYS H    10
REMARK 465     SER H    11
REMARK 465     LEU H    12
REMARK 465     VAL H    13
REMARK 465     ILE H    14
REMARK 465     LEU H    15
REMARK 465     MET H    16
REMARK 465     VAL H    17
REMARK 465     GLN H    18
REMARK 465     GLY H    19
REMARK 465     VAL H    20
REMARK 465     ASN H    21
REMARK 465     LYS H    22
REMARK 465     ALA H    23
REMARK 465     VAL H    24
REMARK 465     ALA H    25
REMARK 465     GLY H    26
REMARK 465     GLU H    27
REMARK 465     GLN H    28
REMARK 465     ALA H    29
REMARK 465     LYS H    30
REMARK 465     GLU H    31
REMARK 465     ASN H   348
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    PHE A 132       30.68     75.57
REMARK 500    ASP A 184      139.52     84.30
REMARK 500    SER A 194     -126.73     61.67
REMARK 500    THR A 222       59.07     34.14
REMARK 500    ILE A 245      -54.64     66.76
REMARK 500    SER A 326       76.33   -114.46
REMARK 500    GLN A 328       57.44    -97.12
REMARK 500    PHE B 132       28.06     84.60
REMARK 500    ASP B 184      134.26     84.80
REMARK 500    SER B 194     -127.77     66.11
REMARK 500    THR B 222       60.64     37.62
REMARK 500    ILE B 245      -50.53     66.72
REMARK 500    GLN B 328       47.18   -100.22
REMARK 500    ASP C 184      147.30     82.79
REMARK 500    SER C 194     -127.75     61.71
REMARK 500    THR C 222       59.09     38.95
REMARK 500    ILE C 245      -48.86     62.27
REMARK 500    GLN C 328       54.03    -94.61
REMARK 500    PHE D 132       24.95     80.25
REMARK 500    ASP D 184      136.80     79.65
REMARK 500    SER D 194     -128.69     61.04
REMARK 500    THR D 222       62.73     33.52
REMARK 500    ILE D 245      -47.68     68.00
REMARK 500    GLN D 328       50.73    -99.65
REMARK 500    PHE E 165      136.30    -38.08
REMARK 500    ASP E 184      134.86     85.11
REMARK 500    SER E 194     -127.98     64.07
REMARK 500    THR E 222       58.13     38.35
REMARK 500    ILE E 245      -48.98     66.42
REMARK 500    GLN E 328       51.49    -96.31
REMARK 500    PHE F 132       33.64     77.24
REMARK 500    ASP F 184      134.74     86.01
REMARK 500    SER F 194     -123.67     58.07
REMARK 500    THR F 222       61.91     31.19
REMARK 500    ILE F 245      -52.10     66.11
REMARK 500    ASP F 248       36.85    -88.84
REMARK 500    THR F 286     -165.67   -160.21
REMARK 500    SER F 326       78.33   -119.40
REMARK 500    GLN F 328       53.58    -97.47
REMARK 500    ASP G 184      135.15     83.69
REMARK 500    SER G 194     -124.10     60.22
REMARK 500    THR G 222       58.28     36.53
REMARK 500    ILE G 245      -53.60     67.45
REMARK 500    ASP G 248       34.35    -91.27
REMARK 500    SER G 326       76.03   -118.37
REMARK 500    GLN G 328       52.96    -95.82
REMARK 500    ASP H 184      141.47     84.10
REMARK 500    SER H 194     -127.52     62.96
REMARK 500    THR H 222       58.92     34.49
REMARK 500    ILE H 245      -52.09     63.73
REMARK 500
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 PHE A   60     VAL A   61                 -148.91
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 F 854        DISTANCE =  6.06 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES G 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES H 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES H 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Q3K   RELATED DB: PDB
REMARK 900 RELATED ID: 4Q3L   RELATED DB: PDB
REMARK 900 RELATED ID: 4Q3M   RELATED DB: PDB
REMARK 900 RELATED ID: 4Q3N   RELATED DB: PDB
DBREF  4Q3O A    1   348  PDB    4Q3O     4Q3O             1    348
DBREF  4Q3O B    1   348  PDB    4Q3O     4Q3O             1    348
DBREF  4Q3O C    1   348  PDB    4Q3O     4Q3O             1    348
DBREF  4Q3O D    1   348  PDB    4Q3O     4Q3O             1    348
DBREF  4Q3O E    1   348  PDB    4Q3O     4Q3O             1    348
DBREF  4Q3O F    1   348  PDB    4Q3O     4Q3O             1    348
DBREF  4Q3O G    1   348  PDB    4Q3O     4Q3O             1    348
DBREF  4Q3O H    1   348  PDB    4Q3O     4Q3O             1    348
SEQRES   1 A  348  MET HIS ARG TYR GLY LEU LEU VAL PHE CYS SER LEU VAL
SEQRES   2 A  348  ILE LEU MET VAL GLN GLY VAL ASN LYS ALA VAL ALA GLY
SEQRES   3 A  348  GLU GLN ALA LYS GLU VAL PRO ILE PRO GLN SER ILE SER
SEQRES   4 A  348  ALA GLU PHE LYS ALA ALA LEU ALA GLN TYR PRO THR PRO
SEQRES   5 A  348  SER VAL GLU GLU ALA ARG SER PHE VAL PRO THR THR ALA
SEQRES   6 A  348  ALA GLN TRP ARG ASP TYR VAL GLN ALA THR ASN LYS MET
SEQRES   7 A  348  GLN LYS THR LYS ILE LYS ASN MET ARG LYS HIS TYR GLY
SEQRES   8 A  348  VAL THR VAL GLU LEU LEU ASP ILE LYS GLY VAL THR VAL
SEQRES   9 A  348  ARG LYS ILE THR PRO LYS SER LEU SER PRO GLU PHE LYS
SEQRES  10 A  348  ASP HIS VAL TYR ILE ASP ILE HIS GLY GLY ALA TYR VAL
SEQRES  11 A  348  LEU PHE ALA GLY LEU PRO SER ILE GLU GLU GLY ILE LEU
SEQRES  12 A  348  ILE ALA HIS ARG LEU GLY ILE VAL VAL TYR SER VAL ASP
SEQRES  13 A  348  TYR ARG MET PRO PRO ALA TYR PRO PHE PRO ALA ALA LEU
SEQRES  14 A  348  ASP ASP VAL LYS HIS VAL TYR ARG VAL LEU SER GLN GLN
SEQRES  15 A  348  TYR ASP ALA ASN HIS ILE PHE MET GLY GLY THR SER ALA
SEQRES  16 A  348  GLY GLY GLY LEU LEU LEU ALA PHE VAL GLN GLY LEU ILE
SEQRES  17 A  348  GLU ASN GLY VAL ALA THR PRO ARG ALA ILE TYR ALA GLY
SEQRES  18 A  348  THR PRO TRP ALA ASP LEU THR LYS THR GLY ASP SER LEU
SEQRES  19 A  348  TYR THR ASN GLU GLY ILE ASP ARG ILE LEU ILE THR TYR
SEQRES  20 A  348  ASP GLY THR LEU GLY ALA SER ALA ARG LEU TYR ALA GLY
SEQRES  21 A  348  ASN THR PRO LEU THR HIS PRO LYS LEU SER PRO ILE TYR
SEQRES  22 A  348  GLY ASP PHE THR ASP PHE PRO PRO THR PHE LEU VAL THR
SEQRES  23 A  348  GLY THR ARG ASP MET PHE LEU SER ASP THR VAL ARG VAL
SEQRES  24 A  348  ASN ARG LYS MET ARG ASP ALA GLY VAL THR THR VAL LEU
SEQRES  25 A  348  ASP VAL TYR GLU GLY LEU SER HIS ALA ASP TYR LEU VAL
SEQRES  26 A  348  SER HIS GLN THR PRO GLU SER GLN SER VAL TYR ARG GLN
SEQRES  27 A  348  LEU LYS ARG PHE LEU VAL GLY PHE THR ASN
SEQRES   1 B  348  MET HIS ARG TYR GLY LEU LEU VAL PHE CYS SER LEU VAL
SEQRES   2 B  348  ILE LEU MET VAL GLN GLY VAL ASN LYS ALA VAL ALA GLY
SEQRES   3 B  348  GLU GLN ALA LYS GLU VAL PRO ILE PRO GLN SER ILE SER
SEQRES   4 B  348  ALA GLU PHE LYS ALA ALA LEU ALA GLN TYR PRO THR PRO
SEQRES   5 B  348  SER VAL GLU GLU ALA ARG SER PHE VAL PRO THR THR ALA
SEQRES   6 B  348  ALA GLN TRP ARG ASP TYR VAL GLN ALA THR ASN LYS MET
SEQRES   7 B  348  GLN LYS THR LYS ILE LYS ASN MET ARG LYS HIS TYR GLY
SEQRES   8 B  348  VAL THR VAL GLU LEU LEU ASP ILE LYS GLY VAL THR VAL
SEQRES   9 B  348  ARG LYS ILE THR PRO LYS SER LEU SER PRO GLU PHE LYS
SEQRES  10 B  348  ASP HIS VAL TYR ILE ASP ILE HIS GLY GLY ALA TYR VAL
SEQRES  11 B  348  LEU PHE ALA GLY LEU PRO SER ILE GLU GLU GLY ILE LEU
SEQRES  12 B  348  ILE ALA HIS ARG LEU GLY ILE VAL VAL TYR SER VAL ASP
SEQRES  13 B  348  TYR ARG MET PRO PRO ALA TYR PRO PHE PRO ALA ALA LEU
SEQRES  14 B  348  ASP ASP VAL LYS HIS VAL TYR ARG VAL LEU SER GLN GLN
SEQRES  15 B  348  TYR ASP ALA ASN HIS ILE PHE MET GLY GLY THR SER ALA
SEQRES  16 B  348  GLY GLY GLY LEU LEU LEU ALA PHE VAL GLN GLY LEU ILE
SEQRES  17 B  348  GLU ASN GLY VAL ALA THR PRO ARG ALA ILE TYR ALA GLY
SEQRES  18 B  348  THR PRO TRP ALA ASP LEU THR LYS THR GLY ASP SER LEU
SEQRES  19 B  348  TYR THR ASN GLU GLY ILE ASP ARG ILE LEU ILE THR TYR
SEQRES  20 B  348  ASP GLY THR LEU GLY ALA SER ALA ARG LEU TYR ALA GLY
SEQRES  21 B  348  ASN THR PRO LEU THR HIS PRO LYS LEU SER PRO ILE TYR
SEQRES  22 B  348  GLY ASP PHE THR ASP PHE PRO PRO THR PHE LEU VAL THR
SEQRES  23 B  348  GLY THR ARG ASP MET PHE LEU SER ASP THR VAL ARG VAL
SEQRES  24 B  348  ASN ARG LYS MET ARG ASP ALA GLY VAL THR THR VAL LEU
SEQRES  25 B  348  ASP VAL TYR GLU GLY LEU SER HIS ALA ASP TYR LEU VAL
SEQRES  26 B  348  SER HIS GLN THR PRO GLU SER GLN SER VAL TYR ARG GLN
SEQRES  27 B  348  LEU LYS ARG PHE LEU VAL GLY PHE THR ASN
SEQRES   1 C  348  MET HIS ARG TYR GLY LEU LEU VAL PHE CYS SER LEU VAL
SEQRES   2 C  348  ILE LEU MET VAL GLN GLY VAL ASN LYS ALA VAL ALA GLY
SEQRES   3 C  348  GLU GLN ALA LYS GLU VAL PRO ILE PRO GLN SER ILE SER
SEQRES   4 C  348  ALA GLU PHE LYS ALA ALA LEU ALA GLN TYR PRO THR PRO
SEQRES   5 C  348  SER VAL GLU GLU ALA ARG SER PHE VAL PRO THR THR ALA
SEQRES   6 C  348  ALA GLN TRP ARG ASP TYR VAL GLN ALA THR ASN LYS MET
SEQRES   7 C  348  GLN LYS THR LYS ILE LYS ASN MET ARG LYS HIS TYR GLY
SEQRES   8 C  348  VAL THR VAL GLU LEU LEU ASP ILE LYS GLY VAL THR VAL
SEQRES   9 C  348  ARG LYS ILE THR PRO LYS SER LEU SER PRO GLU PHE LYS
SEQRES  10 C  348  ASP HIS VAL TYR ILE ASP ILE HIS GLY GLY ALA TYR VAL
SEQRES  11 C  348  LEU PHE ALA GLY LEU PRO SER ILE GLU GLU GLY ILE LEU
SEQRES  12 C  348  ILE ALA HIS ARG LEU GLY ILE VAL VAL TYR SER VAL ASP
SEQRES  13 C  348  TYR ARG MET PRO PRO ALA TYR PRO PHE PRO ALA ALA LEU
SEQRES  14 C  348  ASP ASP VAL LYS HIS VAL TYR ARG VAL LEU SER GLN GLN
SEQRES  15 C  348  TYR ASP ALA ASN HIS ILE PHE MET GLY GLY THR SER ALA
SEQRES  16 C  348  GLY GLY GLY LEU LEU LEU ALA PHE VAL GLN GLY LEU ILE
SEQRES  17 C  348  GLU ASN GLY VAL ALA THR PRO ARG ALA ILE TYR ALA GLY
SEQRES  18 C  348  THR PRO TRP ALA ASP LEU THR LYS THR GLY ASP SER LEU
SEQRES  19 C  348  TYR THR ASN GLU GLY ILE ASP ARG ILE LEU ILE THR TYR
SEQRES  20 C  348  ASP GLY THR LEU GLY ALA SER ALA ARG LEU TYR ALA GLY
SEQRES  21 C  348  ASN THR PRO LEU THR HIS PRO LYS LEU SER PRO ILE TYR
SEQRES  22 C  348  GLY ASP PHE THR ASP PHE PRO PRO THR PHE LEU VAL THR
SEQRES  23 C  348  GLY THR ARG ASP MET PHE LEU SER ASP THR VAL ARG VAL
SEQRES  24 C  348  ASN ARG LYS MET ARG ASP ALA GLY VAL THR THR VAL LEU
SEQRES  25 C  348  ASP VAL TYR GLU GLY LEU SER HIS ALA ASP TYR LEU VAL
SEQRES  26 C  348  SER HIS GLN THR PRO GLU SER GLN SER VAL TYR ARG GLN
SEQRES  27 C  348  LEU LYS ARG PHE LEU VAL GLY PHE THR ASN
SEQRES   1 D  348  MET HIS ARG TYR GLY LEU LEU VAL PHE CYS SER LEU VAL
SEQRES   2 D  348  ILE LEU MET VAL GLN GLY VAL ASN LYS ALA VAL ALA GLY
SEQRES   3 D  348  GLU GLN ALA LYS GLU VAL PRO ILE PRO GLN SER ILE SER
SEQRES   4 D  348  ALA GLU PHE LYS ALA ALA LEU ALA GLN TYR PRO THR PRO
SEQRES   5 D  348  SER VAL GLU GLU ALA ARG SER PHE VAL PRO THR THR ALA
SEQRES   6 D  348  ALA GLN TRP ARG ASP TYR VAL GLN ALA THR ASN LYS MET
SEQRES   7 D  348  GLN LYS THR LYS ILE LYS ASN MET ARG LYS HIS TYR GLY
SEQRES   8 D  348  VAL THR VAL GLU LEU LEU ASP ILE LYS GLY VAL THR VAL
SEQRES   9 D  348  ARG LYS ILE THR PRO LYS SER LEU SER PRO GLU PHE LYS
SEQRES  10 D  348  ASP HIS VAL TYR ILE ASP ILE HIS GLY GLY ALA TYR VAL
SEQRES  11 D  348  LEU PHE ALA GLY LEU PRO SER ILE GLU GLU GLY ILE LEU
SEQRES  12 D  348  ILE ALA HIS ARG LEU GLY ILE VAL VAL TYR SER VAL ASP
SEQRES  13 D  348  TYR ARG MET PRO PRO ALA TYR PRO PHE PRO ALA ALA LEU
SEQRES  14 D  348  ASP ASP VAL LYS HIS VAL TYR ARG VAL LEU SER GLN GLN
SEQRES  15 D  348  TYR ASP ALA ASN HIS ILE PHE MET GLY GLY THR SER ALA
SEQRES  16 D  348  GLY GLY GLY LEU LEU LEU ALA PHE VAL GLN GLY LEU ILE
SEQRES  17 D  348  GLU ASN GLY VAL ALA THR PRO ARG ALA ILE TYR ALA GLY
SEQRES  18 D  348  THR PRO TRP ALA ASP LEU THR LYS THR GLY ASP SER LEU
SEQRES  19 D  348  TYR THR ASN GLU GLY ILE ASP ARG ILE LEU ILE THR TYR
SEQRES  20 D  348  ASP GLY THR LEU GLY ALA SER ALA ARG LEU TYR ALA GLY
SEQRES  21 D  348  ASN THR PRO LEU THR HIS PRO LYS LEU SER PRO ILE TYR
SEQRES  22 D  348  GLY ASP PHE THR ASP PHE PRO PRO THR PHE LEU VAL THR
SEQRES  23 D  348  GLY THR ARG ASP MET PHE LEU SER ASP THR VAL ARG VAL
SEQRES  24 D  348  ASN ARG LYS MET ARG ASP ALA GLY VAL THR THR VAL LEU
SEQRES  25 D  348  ASP VAL TYR GLU GLY LEU SER HIS ALA ASP TYR LEU VAL
SEQRES  26 D  348  SER HIS GLN THR PRO GLU SER GLN SER VAL TYR ARG GLN
SEQRES  27 D  348  LEU LYS ARG PHE LEU VAL GLY PHE THR ASN
SEQRES   1 E  348  MET HIS ARG TYR GLY LEU LEU VAL PHE CYS SER LEU VAL
SEQRES   2 E  348  ILE LEU MET VAL GLN GLY VAL ASN LYS ALA VAL ALA GLY
SEQRES   3 E  348  GLU GLN ALA LYS GLU VAL PRO ILE PRO GLN SER ILE SER
SEQRES   4 E  348  ALA GLU PHE LYS ALA ALA LEU ALA GLN TYR PRO THR PRO
SEQRES   5 E  348  SER VAL GLU GLU ALA ARG SER PHE VAL PRO THR THR ALA
SEQRES   6 E  348  ALA GLN TRP ARG ASP TYR VAL GLN ALA THR ASN LYS MET
SEQRES   7 E  348  GLN LYS THR LYS ILE LYS ASN MET ARG LYS HIS TYR GLY
SEQRES   8 E  348  VAL THR VAL GLU LEU LEU ASP ILE LYS GLY VAL THR VAL
SEQRES   9 E  348  ARG LYS ILE THR PRO LYS SER LEU SER PRO GLU PHE LYS
SEQRES  10 E  348  ASP HIS VAL TYR ILE ASP ILE HIS GLY GLY ALA TYR VAL
SEQRES  11 E  348  LEU PHE ALA GLY LEU PRO SER ILE GLU GLU GLY ILE LEU
SEQRES  12 E  348  ILE ALA HIS ARG LEU GLY ILE VAL VAL TYR SER VAL ASP
SEQRES  13 E  348  TYR ARG MET PRO PRO ALA TYR PRO PHE PRO ALA ALA LEU
SEQRES  14 E  348  ASP ASP VAL LYS HIS VAL TYR ARG VAL LEU SER GLN GLN
SEQRES  15 E  348  TYR ASP ALA ASN HIS ILE PHE MET GLY GLY THR SER ALA
SEQRES  16 E  348  GLY GLY GLY LEU LEU LEU ALA PHE VAL GLN GLY LEU ILE
SEQRES  17 E  348  GLU ASN GLY VAL ALA THR PRO ARG ALA ILE TYR ALA GLY
SEQRES  18 E  348  THR PRO TRP ALA ASP LEU THR LYS THR GLY ASP SER LEU
SEQRES  19 E  348  TYR THR ASN GLU GLY ILE ASP ARG ILE LEU ILE THR TYR
SEQRES  20 E  348  ASP GLY THR LEU GLY ALA SER ALA ARG LEU TYR ALA GLY
SEQRES  21 E  348  ASN THR PRO LEU THR HIS PRO LYS LEU SER PRO ILE TYR
SEQRES  22 E  348  GLY ASP PHE THR ASP PHE PRO PRO THR PHE LEU VAL THR
SEQRES  23 E  348  GLY THR ARG ASP MET PHE LEU SER ASP THR VAL ARG VAL
SEQRES  24 E  348  ASN ARG LYS MET ARG ASP ALA GLY VAL THR THR VAL LEU
SEQRES  25 E  348  ASP VAL TYR GLU GLY LEU SER HIS ALA ASP TYR LEU VAL
SEQRES  26 E  348  SER HIS GLN THR PRO GLU SER GLN SER VAL TYR ARG GLN
SEQRES  27 E  348  LEU LYS ARG PHE LEU VAL GLY PHE THR ASN
SEQRES   1 F  348  MET HIS ARG TYR GLY LEU LEU VAL PHE CYS SER LEU VAL
SEQRES   2 F  348  ILE LEU MET VAL GLN GLY VAL ASN LYS ALA VAL ALA GLY
SEQRES   3 F  348  GLU GLN ALA LYS GLU VAL PRO ILE PRO GLN SER ILE SER
SEQRES   4 F  348  ALA GLU PHE LYS ALA ALA LEU ALA GLN TYR PRO THR PRO
SEQRES   5 F  348  SER VAL GLU GLU ALA ARG SER PHE VAL PRO THR THR ALA
SEQRES   6 F  348  ALA GLN TRP ARG ASP TYR VAL GLN ALA THR ASN LYS MET
SEQRES   7 F  348  GLN LYS THR LYS ILE LYS ASN MET ARG LYS HIS TYR GLY
SEQRES   8 F  348  VAL THR VAL GLU LEU LEU ASP ILE LYS GLY VAL THR VAL
SEQRES   9 F  348  ARG LYS ILE THR PRO LYS SER LEU SER PRO GLU PHE LYS
SEQRES  10 F  348  ASP HIS VAL TYR ILE ASP ILE HIS GLY GLY ALA TYR VAL
SEQRES  11 F  348  LEU PHE ALA GLY LEU PRO SER ILE GLU GLU GLY ILE LEU
SEQRES  12 F  348  ILE ALA HIS ARG LEU GLY ILE VAL VAL TYR SER VAL ASP
SEQRES  13 F  348  TYR ARG MET PRO PRO ALA TYR PRO PHE PRO ALA ALA LEU
SEQRES  14 F  348  ASP ASP VAL LYS HIS VAL TYR ARG VAL LEU SER GLN GLN
SEQRES  15 F  348  TYR ASP ALA ASN HIS ILE PHE MET GLY GLY THR SER ALA
SEQRES  16 F  348  GLY GLY GLY LEU LEU LEU ALA PHE VAL GLN GLY LEU ILE
SEQRES  17 F  348  GLU ASN GLY VAL ALA THR PRO ARG ALA ILE TYR ALA GLY
SEQRES  18 F  348  THR PRO TRP ALA ASP LEU THR LYS THR GLY ASP SER LEU
SEQRES  19 F  348  TYR THR ASN GLU GLY ILE ASP ARG ILE LEU ILE THR TYR
SEQRES  20 F  348  ASP GLY THR LEU GLY ALA SER ALA ARG LEU TYR ALA GLY
SEQRES  21 F  348  ASN THR PRO LEU THR HIS PRO LYS LEU SER PRO ILE TYR
SEQRES  22 F  348  GLY ASP PHE THR ASP PHE PRO PRO THR PHE LEU VAL THR
SEQRES  23 F  348  GLY THR ARG ASP MET PHE LEU SER ASP THR VAL ARG VAL
SEQRES  24 F  348  ASN ARG LYS MET ARG ASP ALA GLY VAL THR THR VAL LEU
SEQRES  25 F  348  ASP VAL TYR GLU GLY LEU SER HIS ALA ASP TYR LEU VAL
SEQRES  26 F  348  SER HIS GLN THR PRO GLU SER GLN SER VAL TYR ARG GLN
SEQRES  27 F  348  LEU LYS ARG PHE LEU VAL GLY PHE THR ASN
SEQRES   1 G  348  MET HIS ARG TYR GLY LEU LEU VAL PHE CYS SER LEU VAL
SEQRES   2 G  348  ILE LEU MET VAL GLN GLY VAL ASN LYS ALA VAL ALA GLY
SEQRES   3 G  348  GLU GLN ALA LYS GLU VAL PRO ILE PRO GLN SER ILE SER
SEQRES   4 G  348  ALA GLU PHE LYS ALA ALA LEU ALA GLN TYR PRO THR PRO
SEQRES   5 G  348  SER VAL GLU GLU ALA ARG SER PHE VAL PRO THR THR ALA
SEQRES   6 G  348  ALA GLN TRP ARG ASP TYR VAL GLN ALA THR ASN LYS MET
SEQRES   7 G  348  GLN LYS THR LYS ILE LYS ASN MET ARG LYS HIS TYR GLY
SEQRES   8 G  348  VAL THR VAL GLU LEU LEU ASP ILE LYS GLY VAL THR VAL
SEQRES   9 G  348  ARG LYS ILE THR PRO LYS SER LEU SER PRO GLU PHE LYS
SEQRES  10 G  348  ASP HIS VAL TYR ILE ASP ILE HIS GLY GLY ALA TYR VAL
SEQRES  11 G  348  LEU PHE ALA GLY LEU PRO SER ILE GLU GLU GLY ILE LEU
SEQRES  12 G  348  ILE ALA HIS ARG LEU GLY ILE VAL VAL TYR SER VAL ASP
SEQRES  13 G  348  TYR ARG MET PRO PRO ALA TYR PRO PHE PRO ALA ALA LEU
SEQRES  14 G  348  ASP ASP VAL LYS HIS VAL TYR ARG VAL LEU SER GLN GLN
SEQRES  15 G  348  TYR ASP ALA ASN HIS ILE PHE MET GLY GLY THR SER ALA
SEQRES  16 G  348  GLY GLY GLY LEU LEU LEU ALA PHE VAL GLN GLY LEU ILE
SEQRES  17 G  348  GLU ASN GLY VAL ALA THR PRO ARG ALA ILE TYR ALA GLY
SEQRES  18 G  348  THR PRO TRP ALA ASP LEU THR LYS THR GLY ASP SER LEU
SEQRES  19 G  348  TYR THR ASN GLU GLY ILE ASP ARG ILE LEU ILE THR TYR
SEQRES  20 G  348  ASP GLY THR LEU GLY ALA SER ALA ARG LEU TYR ALA GLY
SEQRES  21 G  348  ASN THR PRO LEU THR HIS PRO LYS LEU SER PRO ILE TYR
SEQRES  22 G  348  GLY ASP PHE THR ASP PHE PRO PRO THR PHE LEU VAL THR
SEQRES  23 G  348  GLY THR ARG ASP MET PHE LEU SER ASP THR VAL ARG VAL
SEQRES  24 G  348  ASN ARG LYS MET ARG ASP ALA GLY VAL THR THR VAL LEU
SEQRES  25 G  348  ASP VAL TYR GLU GLY LEU SER HIS ALA ASP TYR LEU VAL
SEQRES  26 G  348  SER HIS GLN THR PRO GLU SER GLN SER VAL TYR ARG GLN
SEQRES  27 G  348  LEU LYS ARG PHE LEU VAL GLY PHE THR ASN
SEQRES   1 H  348  MET HIS ARG TYR GLY LEU LEU VAL PHE CYS SER LEU VAL
SEQRES   2 H  348  ILE LEU MET VAL GLN GLY VAL ASN LYS ALA VAL ALA GLY
SEQRES   3 H  348  GLU GLN ALA LYS GLU VAL PRO ILE PRO GLN SER ILE SER
SEQRES   4 H  348  ALA GLU PHE LYS ALA ALA LEU ALA GLN TYR PRO THR PRO
SEQRES   5 H  348  SER VAL GLU GLU ALA ARG SER PHE VAL PRO THR THR ALA
SEQRES   6 H  348  ALA GLN TRP ARG ASP TYR VAL GLN ALA THR ASN LYS MET
SEQRES   7 H  348  GLN LYS THR LYS ILE LYS ASN MET ARG LYS HIS TYR GLY
SEQRES   8 H  348  VAL THR VAL GLU LEU LEU ASP ILE LYS GLY VAL THR VAL
SEQRES   9 H  348  ARG LYS ILE THR PRO LYS SER LEU SER PRO GLU PHE LYS
SEQRES  10 H  348  ASP HIS VAL TYR ILE ASP ILE HIS GLY GLY ALA TYR VAL
SEQRES  11 H  348  LEU PHE ALA GLY LEU PRO SER ILE GLU GLU GLY ILE LEU
SEQRES  12 H  348  ILE ALA HIS ARG LEU GLY ILE VAL VAL TYR SER VAL ASP
SEQRES  13 H  348  TYR ARG MET PRO PRO ALA TYR PRO PHE PRO ALA ALA LEU
SEQRES  14 H  348  ASP ASP VAL LYS HIS VAL TYR ARG VAL LEU SER GLN GLN
SEQRES  15 H  348  TYR ASP ALA ASN HIS ILE PHE MET GLY GLY THR SER ALA
SEQRES  16 H  348  GLY GLY GLY LEU LEU LEU ALA PHE VAL GLN GLY LEU ILE
SEQRES  17 H  348  GLU ASN GLY VAL ALA THR PRO ARG ALA ILE TYR ALA GLY
SEQRES  18 H  348  THR PRO TRP ALA ASP LEU THR LYS THR GLY ASP SER LEU
SEQRES  19 H  348  TYR THR ASN GLU GLY ILE ASP ARG ILE LEU ILE THR TYR
SEQRES  20 H  348  ASP GLY THR LEU GLY ALA SER ALA ARG LEU TYR ALA GLY
SEQRES  21 H  348  ASN THR PRO LEU THR HIS PRO LYS LEU SER PRO ILE TYR
SEQRES  22 H  348  GLY ASP PHE THR ASP PHE PRO PRO THR PHE LEU VAL THR
SEQRES  23 H  348  GLY THR ARG ASP MET PHE LEU SER ASP THR VAL ARG VAL
SEQRES  24 H  348  ASN ARG LYS MET ARG ASP ALA GLY VAL THR THR VAL LEU
SEQRES  25 H  348  ASP VAL TYR GLU GLY LEU SER HIS ALA ASP TYR LEU VAL
SEQRES  26 H  348  SER HIS GLN THR PRO GLU SER GLN SER VAL TYR ARG GLN
SEQRES  27 H  348  LEU LYS ARG PHE LEU VAL GLY PHE THR ASN
HET     CL  A 401       1
HET     CL  A 402       1
HET    MES  A 403      12
HET    MES  A 404      12
HET    GOL  A 405       6
HET    GOL  A 406       6
HET    GOL  A 407       6
HET     CL  B 401       1
HET    MES  B 402      12
HET    GOL  B 403       6
HET     CL  C 401       1
HET    MES  C 402      12
HET    MES  C 403      12
HET    GOL  C 404       6
HET    GOL  C 405       6
HET    GOL  C 406       6
HET    MES  D 401      12
HET     CL  C 407       1
HET    GOL  D 402       6
HET    GOL  D 403       6
HET    GOL  D 404       6
HET    GOL  D 405       6
HET    GOL  D 406       6
HET     CL  E 401       1
HET     CL  E 402       1
HET     CL  D 407       1
HET    GOL  E 403       6
HET    GOL  E 404       6
HET     CL  F 401       1
HET    GOL  F 402       6
HET    GOL  F 403       6
HET     CL  G 401       1
HET    MES  G 402      12
HET    MES  G 403      12
HET    GOL  G 404       6
HET    MES  H 401      12
HET    MES  H 402      12
HETNAM      CL CHLORIDE ION
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   9   CL    10(CL 1-)
FORMUL  11  MES    10(C6 H13 N O4 S)
FORMUL  13  GOL    17(C3 H8 O3)
FORMUL  46  HOH   *3085(H2 O)
HELIX    1   1 SER A   39  TYR A   49  1                                  11
HELIX    2   2 SER A   53  PHE A   60  1                                   8
HELIX    3   3 THR A   64  GLY A   91  1                                  28
HELIX    4   4 SER A  113  LYS A  117  5                                   5
HELIX    5   5 GLY A  134  SER A  137  5                                   4
HELIX    6   6 ILE A  138  GLY A  149  1                                  12
HELIX    7   7 PRO A  166  ASP A  184  1                                  19
HELIX    8   8 SER A  194  ASN A  210  1                                  17
HELIX    9   9 GLY A  231  ASN A  237  1                                   7
HELIX   10  10 GLY A  249  GLY A  260  1                                  12
HELIX   11  11 SER A  270  GLY A  274  5                                   5
HELIX   12  12 PHE A  292  ALA A  306  1                                  15
HELIX   13  13 ALA A  321  SER A  326  1                                   6
HELIX   14  14 THR A  329  GLY A  345  1                                  17
HELIX   15  15 SER B   39  TYR B   49  1                                  11
HELIX   16  16 SER B   53  PHE B   60  1                                   8
HELIX   17  17 THR B   64  GLY B   91  1                                  28
HELIX   18  18 SER B  113  LYS B  117  5                                   5
HELIX   19  19 GLY B  134  SER B  137  5                                   4
HELIX   20  20 ILE B  138  GLY B  149  1                                  12
HELIX   21  21 PRO B  166  ASP B  184  1                                  19
HELIX   22  22 SER B  194  ASN B  210  1                                  17
HELIX   23  23 GLY B  231  ASN B  237  1                                   7
HELIX   24  24 GLY B  249  GLY B  260  1                                  12
HELIX   25  25 SER B  270  GLY B  274  5                                   5
HELIX   26  26 PHE B  292  ALA B  306  1                                  15
HELIX   27  27 ALA B  321  SER B  326  1                                   6
HELIX   28  28 THR B  329  GLY B  345  1                                  17
HELIX   29  29 SER C   39  TYR C   49  1                                  11
HELIX   30  30 SER C   53  PHE C   60  1                                   8
HELIX   31  31 THR C   64  GLY C   91  1                                  28
HELIX   32  32 SER C  113  LYS C  117  5                                   5
HELIX   33  33 GLY C  134  SER C  137  5                                   4
HELIX   34  34 ILE C  138  GLY C  149  1                                  12
HELIX   35  35 PRO C  166  TYR C  183  1                                  18
HELIX   36  36 ASP C  184  ASN C  186  5                                   3
HELIX   37  37 SER C  194  ASN C  210  1                                  17
HELIX   38  38 GLY C  231  ASN C  237  1                                   7
HELIX   39  39 GLY C  249  GLY C  260  1                                  12
HELIX   40  40 SER C  270  GLY C  274  5                                   5
HELIX   41  41 PHE C  292  ALA C  306  1                                  15
HELIX   42  42 ALA C  321  SER C  326  1                                   6
HELIX   43  43 THR C  329  GLY C  345  1                                  17
HELIX   44  44 SER D   39  TYR D   49  1                                  11
HELIX   45  45 SER D   53  PHE D   60  1                                   8
HELIX   46  46 THR D   64  GLY D   91  1                                  28
HELIX   47  47 SER D  113  LYS D  117  5                                   5
HELIX   48  48 GLY D  134  SER D  137  5                                   4
HELIX   49  49 ILE D  138  GLY D  149  1                                  12
HELIX   50  50 PRO D  166  ASP D  184  1                                  19
HELIX   51  51 SER D  194  ASN D  210  1                                  17
HELIX   52  52 GLY D  231  ASN D  237  1                                   7
HELIX   53  53 GLY D  249  GLY D  260  1                                  12
HELIX   54  54 SER D  270  GLY D  274  5                                   5
HELIX   55  55 PHE D  292  ALA D  306  1                                  15
HELIX   56  56 ALA D  321  SER D  326  1                                   6
HELIX   57  57 THR D  329  GLY D  345  1                                  17
HELIX   58  58 SER E   39  TYR E   49  1                                  11
HELIX   59  59 SER E   53  PHE E   60  1                                   8
HELIX   60  60 THR E   64  GLY E   91  1                                  28
HELIX   61  61 SER E  113  LYS E  117  5                                   5
HELIX   62  62 GLY E  134  SER E  137  5                                   4
HELIX   63  63 ILE E  138  GLY E  149  1                                  12
HELIX   64  64 PRO E  166  ASP E  184  1                                  19
HELIX   65  65 SER E  194  ASN E  210  1                                  17
HELIX   66  66 ASP E  232  ASN E  237  1                                   6
HELIX   67  67 GLY E  249  GLY E  260  1                                  12
HELIX   68  68 SER E  270  GLY E  274  5                                   5
HELIX   69  69 PHE E  292  ALA E  306  1                                  15
HELIX   70  70 ALA E  321  SER E  326  1                                   6
HELIX   71  71 THR E  329  GLY E  345  1                                  17
HELIX   72  72 SER F   39  TYR F   49  1                                  11
HELIX   73  73 SER F   53  PHE F   60  1                                   8
HELIX   74  74 THR F   64  GLY F   91  1                                  28
HELIX   75  75 SER F  113  LYS F  117  5                                   5
HELIX   76  76 GLY F  134  SER F  137  5                                   4
HELIX   77  77 ILE F  138  GLY F  149  1                                  12
HELIX   78  78 PRO F  166  ASP F  184  1                                  19
HELIX   79  79 SER F  194  ASN F  210  1                                  17
HELIX   80  80 GLY F  231  ASN F  237  1                                   7
HELIX   81  81 GLY F  249  GLY F  260  1                                  12
HELIX   82  82 SER F  270  GLY F  274  5                                   5
HELIX   83  83 PHE F  292  ALA F  306  1                                  15
HELIX   84  84 ALA F  321  SER F  326  1                                   6
HELIX   85  85 THR F  329  GLY F  345  1                                  17
HELIX   86  86 SER G   39  TYR G   49  1                                  11
HELIX   87  87 SER G   53  PHE G   60  1                                   8
HELIX   88  88 THR G   64  GLY G   91  1                                  28
HELIX   89  89 SER G  113  LYS G  117  5                                   5
HELIX   90  90 GLY G  134  SER G  137  5                                   4
HELIX   91  91 ILE G  138  GLY G  149  1                                  12
HELIX   92  92 PRO G  166  ASP G  184  1                                  19
HELIX   93  93 SER G  194  ASN G  210  1                                  17
HELIX   94  94 ASP G  232  ASN G  237  1                                   6
HELIX   95  95 GLY G  249  GLY G  260  1                                  12
HELIX   96  96 SER G  270  GLY G  274  5                                   5
HELIX   97  97 PHE G  292  ALA G  306  1                                  15
HELIX   98  98 ALA G  321  SER G  326  1                                   6
HELIX   99  99 THR G  329  GLY G  345  1                                  17
HELIX  100 100 SER H   39  TYR H   49  1                                  11
HELIX  101 101 SER H   53  PHE H   60  1                                   8
HELIX  102 102 THR H   64  MET H   86  1                                  23
HELIX  103 103 ARG H   87  HIS H   89  5                                   3
HELIX  104 104 SER H  113  LYS H  117  5                                   5
HELIX  105 105 GLY H  134  SER H  137  5                                   4
HELIX  106 106 ILE H  138  GLY H  149  1                                  12
HELIX  107 107 PRO H  166  ASP H  184  1                                  19
HELIX  108 108 SER H  194  ASN H  210  1                                  17
HELIX  109 109 GLY H  231  ASN H  237  1                                   7
HELIX  110 110 GLY H  249  GLY H  260  1                                  12
HELIX  111 111 SER H  270  GLY H  274  5                                   5
HELIX  112 112 PHE H  292  ALA H  306  1                                  15
HELIX  113 113 ALA H  321  SER H  326  1                                   6
HELIX  114 114 THR H  329  GLY H  345  1                                  17
SHEET    1   A 8 THR A  93  ILE A  99  0
SHEET    2   A 8 VAL A 102  THR A 108 -1  O  VAL A 104   N  LEU A  97
SHEET    3   A 8 VAL A 151  ASP A 156 -1  O  VAL A 152   N  ILE A 107
SHEET    4   A 8 VAL A 120  ILE A 124  1  N  TYR A 121   O  TYR A 153
SHEET    5   A 8 ILE A 188  THR A 193  1  O  PHE A 189   N  VAL A 120
SHEET    6   A 8 ALA A 217  GLY A 221  1  O  GLY A 221   N  GLY A 192
SHEET    7   A 8 THR A 282  GLY A 287  1  O  PHE A 283   N  ALA A 220
SHEET    8   A 8 THR A 310  TYR A 315  1  O  VAL A 311   N  LEU A 284
SHEET    1   B 8 THR B  93  ILE B  99  0
SHEET    2   B 8 VAL B 102  THR B 108 -1  O  VAL B 104   N  LEU B  97
SHEET    3   B 8 VAL B 151  ASP B 156 -1  O  VAL B 152   N  ILE B 107
SHEET    4   B 8 VAL B 120  ILE B 124  1  N  TYR B 121   O  TYR B 153
SHEET    5   B 8 ILE B 188  THR B 193  1  O  PHE B 189   N  VAL B 120
SHEET    6   B 8 ALA B 217  GLY B 221  1  O  GLY B 221   N  GLY B 192
SHEET    7   B 8 THR B 282  GLY B 287  1  O  PHE B 283   N  ALA B 220
SHEET    8   B 8 THR B 310  TYR B 315  1  O  VAL B 311   N  LEU B 284
SHEET    1   C 8 THR C  93  ILE C  99  0
SHEET    2   C 8 VAL C 102  THR C 108 -1  O  VAL C 102   N  ILE C  99
SHEET    3   C 8 VAL C 152  ASP C 156 -1  O  VAL C 152   N  ILE C 107
SHEET    4   C 8 VAL C 120  ILE C 124  1  N  TYR C 121   O  TYR C 153
SHEET    5   C 8 ILE C 188  THR C 193  1  O  PHE C 189   N  ILE C 122
SHEET    6   C 8 ALA C 217  GLY C 221  1  O  GLY C 221   N  GLY C 192
SHEET    7   C 8 THR C 282  GLY C 287  1  O  PHE C 283   N  ALA C 220
SHEET    8   C 8 THR C 310  TYR C 315  1  O  ASP C 313   N  LEU C 284
SHEET    1   D 8 THR D  93  ILE D  99  0
SHEET    2   D 8 VAL D 102  THR D 108 -1  O  VAL D 104   N  LEU D  97
SHEET    3   D 8 VAL D 151  ASP D 156 -1  O  VAL D 152   N  ILE D 107
SHEET    4   D 8 VAL D 120  ILE D 124  1  N  TYR D 121   O  TYR D 153
SHEET    5   D 8 ILE D 188  THR D 193  1  O  PHE D 189   N  ILE D 122
SHEET    6   D 8 ALA D 217  GLY D 221  1  O  GLY D 221   N  GLY D 192
SHEET    7   D 8 THR D 282  GLY D 287  1  O  PHE D 283   N  ALA D 220
SHEET    8   D 8 THR D 310  TYR D 315  1  O  VAL D 311   N  LEU D 284
SHEET    1   E 8 THR E  93  ILE E  99  0
SHEET    2   E 8 VAL E 102  THR E 108 -1  O  LYS E 106   N  GLU E  95
SHEET    3   E 8 VAL E 151  ASP E 156 -1  O  VAL E 152   N  ILE E 107
SHEET    4   E 8 VAL E 120  ILE E 124  1  N  TYR E 121   O  TYR E 153
SHEET    5   E 8 ILE E 188  THR E 193  1  O  PHE E 189   N  ILE E 122
SHEET    6   E 8 ALA E 217  GLY E 221  1  O  GLY E 221   N  GLY E 192
SHEET    7   E 8 THR E 282  GLY E 287  1  O  PHE E 283   N  ALA E 220
SHEET    8   E 8 THR E 310  TYR E 315  1  O  VAL E 311   N  LEU E 284
SHEET    1   F 8 THR F  93  ILE F  99  0
SHEET    2   F 8 VAL F 102  THR F 108 -1  O  VAL F 104   N  LEU F  97
SHEET    3   F 8 VAL F 151  ASP F 156 -1  O  VAL F 152   N  ILE F 107
SHEET    4   F 8 VAL F 120  ILE F 124  1  N  TYR F 121   O  TYR F 153
SHEET    5   F 8 ILE F 188  THR F 193  1  O  PHE F 189   N  ILE F 122
SHEET    6   F 8 ALA F 217  GLY F 221  1  O  GLY F 221   N  GLY F 192
SHEET    7   F 8 THR F 282  GLY F 287  1  O  PHE F 283   N  ALA F 220
SHEET    8   F 8 THR F 310  TYR F 315  1  O  VAL F 311   N  LEU F 284
SHEET    1   G 8 THR G  93  ILE G  99  0
SHEET    2   G 8 VAL G 102  THR G 108 -1  O  VAL G 102   N  ILE G  99
SHEET    3   G 8 VAL G 151  ASP G 156 -1  O  VAL G 152   N  ILE G 107
SHEET    4   G 8 VAL G 120  ILE G 124  1  N  TYR G 121   O  TYR G 153
SHEET    5   G 8 ILE G 188  THR G 193  1  O  PHE G 189   N  VAL G 120
SHEET    6   G 8 ALA G 217  GLY G 221  1  O  GLY G 221   N  GLY G 192
SHEET    7   G 8 THR G 282  GLY G 287  1  O  PHE G 283   N  ALA G 220
SHEET    8   G 8 THR G 310  TYR G 315  1  O  VAL G 311   N  LEU G 284
SHEET    1   H 8 VAL H  92  ILE H  99  0
SHEET    2   H 8 VAL H 102  PRO H 109 -1  O  VAL H 104   N  LEU H  97
SHEET    3   H 8 VAL H 151  ASP H 156 -1  O  VAL H 152   N  ILE H 107
SHEET    4   H 8 VAL H 120  ILE H 124  1  N  TYR H 121   O  TYR H 153
SHEET    5   H 8 ILE H 188  THR H 193  1  O  PHE H 189   N  ILE H 122
SHEET    6   H 8 ALA H 217  GLY H 221  1  O  GLY H 221   N  GLY H 192
SHEET    7   H 8 THR H 282  GLY H 287  1  O  PHE H 283   N  ALA H 220
SHEET    8   H 8 THR H 310  TYR H 315  1  O  VAL H 311   N  LEU H 284
CISPEP   1 PRO A  160    PRO A  161          0         2.73
CISPEP   2 PHE A  165    PRO A  166          0         8.42
CISPEP   3 PRO B  160    PRO B  161          0         5.85
CISPEP   4 PHE B  165    PRO B  166          0         9.91
CISPEP   5 PRO C  160    PRO C  161          0         3.47
CISPEP   6 PHE C  165    PRO C  166          0         5.48
CISPEP   7 PRO D  160    PRO D  161          0         5.22
CISPEP   8 PHE D  165    PRO D  166          0         8.82
CISPEP   9 PRO E  160    PRO E  161          0         5.33
CISPEP  10 PHE E  165    PRO E  166          0         2.28
CISPEP  11 PRO F  160    PRO F  161          0         5.50
CISPEP  12 PHE F  165    PRO F  166          0         8.43
CISPEP  13 PRO G  160    PRO G  161          0        -0.60
CISPEP  14 PHE G  165    PRO G  166          0         4.30
CISPEP  15 PRO H  160    PRO H  161          0         2.67
CISPEP  16 PHE H  165    PRO H  166          0         3.15
SITE     1 AC1  4 GLY A 127  ALA A 128  SER A 194  HOH A 859
SITE     1 AC2  5 ARG A 304  LEU A 312  HOH A 681  ARG B 304
SITE     2 AC2  5 LEU B 312
SITE     1 AC3  7 SER A  37  SER A  39  HOH A 664  HOH A 743
SITE     2 AC3  7 HOH A 867  ARG B 298  HOH B 530
SITE     1 AC4 12 ARG A 298  LYS A 302  HOH A 517  HOH A 562
SITE     2 AC4 12 HOH A 611  HOH A 683  HOH A 710  GLN B  36
SITE     3 AC4 12 SER B  37  ALA E  40  HOH E 591  HOH E 669
SITE     1 AC5  6 ARG A  87  VAL A  94  LEU A  96  ARG A 105
SITE     2 AC5  6 LEU A 135  HOH A 822
SITE     1 AC6  6 HIS A  89  TYR A  90  ARG A 147  GLN A 328
SITE     2 AC6  6 GLN A 333  HOH A 541
SITE     1 AC7  8 GLN A 205  GLU A 209  PRO A 267  LYS A 268
SITE     2 AC7  8 ASP A 275  HOH A 547  HOH A 727  GLN E 328
SITE     1 AC8  4 GLY B 127  ALA B 128  SER B 194  HOH B 920
SITE     1 AC9  4 HIS B 146  GLN B 333  LYS B 340  HOH B 548
SITE     1 BC1  6 THR B 103  ALA B 133  ASP B 156  TYR B 157
SITE     2 BC1  6 ARG B 158  HOH B 563
SITE     1 BC2  4 GLY C 127  ALA C 128  SER C 194  HOH C 739
SITE     1 BC3  8 ILE C 272  ARG C 298  LYS C 302  HOH C 532
SITE     2 BC3  8 HOH C 646  HOH C 860  SER F  37  SER F  39
SITE     1 BC4  7 HIS C 146  ARG C 147  GLN C 333  LYS C 340
SITE     2 BC4  7 HOH C 506  HOH C 549  HOH C 891
SITE     1 BC5  8 VAL C  94  GLU C  95  LEU C  96  HOH C 818
SITE     2 BC5  8 HOH C 862  PRO E  52  GLU E  56  PHE E  60
SITE     1 BC6  9 THR C 103  ALA C 133  ASP C 156  TYR C 157
SITE     2 BC6  9 HOH C 557  HOH C 612  HOH C 641  HOH C 762
SITE     3 BC6  9 HOH C 886
SITE     1 BC7  7 ARG C 158  PRO C 166  ALA C 167  ASP C 170
SITE     2 BC7  7 HOH C 593  HOH C 702  HOH C 825
SITE     1 BC8  6 ARG C 304  VAL C 311  LEU C 312  ARG F 304
SITE     2 BC8  6 LEU F 312  HOH F 685
SITE     1 BC9  6 HIS D 146  GLN D 333  LYS D 340  GOL D 402
SITE     2 BC9  6 HOH D 527  HOH D 566
SITE     1 CC1  6 SER D 111  SER D 113  HIS D 146  MES D 401
SITE     2 CC1  6 HOH D 520  HOH D 821
SITE     1 CC2  4 GLY D 127  ALA D 128  SER D 194  HIS D 320
SITE     1 CC3  6 HIS D  89  TYR D  90  LYS D 110  HIS D 146
SITE     2 CC3  6 HOH D 678  ASP G 278
SITE     1 CC4  4 LYS D 173  ASN D 210  HOH D 824  ARG H 158
SITE     1 CC5  8 GLN D 205  GLU D 209  PRO D 267  LYS D 268
SITE     2 CC5  8 GLY D 274  ASP D 275  HOH D 560  HOH D 840
SITE     1 CC6  5 ARG D 304  LEU D 312  HOH D 891  ARG G 304
SITE     2 CC6  5 LEU G 312
SITE     1 CC7  4 GLY E 127  ALA E 128  SER E 194  HOH E 827
SITE     1 CC8  5 ARG E 304  LEU E 312  HOH E 661  ARG H 304
SITE     2 CC8  5 LEU H 312
SITE     1 CC9  2 HOH E 601  HOH E 686
SITE     1 DC1  6 PRO D  52  GLU D  56  VAL E  94  GLU E  95
SITE     2 DC1  6 LEU E  96  HOH E 776
SITE     1 DC2  5 GLY F 127  ALA F 128  SER F 194  HIS F 320
SITE     2 DC2  5 HOH F 584
SITE     1 DC3  6 PRO B 166  LYS B 173  HOH B 643  HOH B 822
SITE     2 DC3  6 ALA F 162  TYR F 163
SITE     1 DC4  7 GLN C 328  GLN F 205  GLU F 209  PRO F 267
SITE     2 DC4  7 LYS F 268  ASP F 275  HOH F 537
SITE     1 DC5  4 GLY G 127  ALA G 128  SER G 194  HOH G 783
SITE     1 DC6  8 SER D  37  SER D  39  ARG G 298  LYS G 302
SITE     2 DC6  8 HOH G 581  HOH G 650  HOH G 797  HOH G 851
SITE     1 DC7  7 ARG D 298  HOH D 528  SER G  37  SER G  39
SITE     2 DC7  7 GLU G 331  HOH G 504  HOH G 798
SITE     1 DC8  9 GLN D 328  GLN G 205  GLU G 209  PRO G 267
SITE     2 DC8  9 LYS G 268  GLY G 274  ASP G 275  HOH G 527
SITE     3 DC8  9 HOH G 607
SITE     1 DC9  9 SER E  37  SER E  39  ARG H 298  LYS H 302
SITE     2 DC9  9 HOH H 586  HOH H 613  HOH H 647  HOH H 768
SITE     3 DC9  9 HOH H 831
SITE     1 EC1  7 ARG E 298  HOH E 577  HOH E 730  SER H  37
SITE     2 EC1  7 SER H  39  HOH H 706  HOH H 807
CRYST1  189.454  131.397  112.441  90.00 103.55  90.00 C 1 2 1      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      0.005278  0.000000  0.001272        0.00000
SCALE2      0.000000  0.007611  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009148        0.00000
TER    2502      THR A 347
TER    4992      THR B 347
TER    7479      THR C 347
TER    9978      THR D 347
TER   12469      THR E 347
TER   14947      THR F 347
TER   17435      THR G 347
TER   19907      THR H 347
MASTER     1263    0   37  114   64    0   69    623063    8  222  216
END