longtext: 8dvc-pdb

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HEADER    SIGNALING PROTEIN                       28-JUL-22   8DVC
TITLE     RECEPTOR SHHTL5 FROM STRIGA HERMONTHICA IN COMPLEX WITH STRIGOLACTONE
TITLE    2 AGONIST GR24
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HYPOSENSITIVE TO LIGHT 5;
COMPND   3 CHAIN: A, B, C, D, E;
COMPND   4 SYNONYM: SHHTL5;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;
SOURCE   3 ORGANISM_TAXID: 68872;
SOURCE   4 GENE: SHHTL5;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS    STRIGA HERMONTHICA, STRIGOLACTONE, SIGNALLING, RECEPTOR, SHHTL5,
KEYWDS   2 ALPHA/BETA HYDROLASE, SIGNALLING PROTEIN, RECEPTOR-AGONIST COMPLEX,
KEYWDS   3 SIGNALING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.ARELLANO-SAAB,T.SKARINA,V.YIM,A.SAVCHENKO,P.J.STOGIOS,P.MCCOURT
REVDAT   1   14-JUN-23 8DVC    0
JRNL        AUTH   A.ARELLANO-SAAB,T.SKARINA,Z.XU,C.S.P.MCERLEAN,A.SAVCHENKO,
JRNL        AUTH 2 S.LUMBA,P.J.STOGIOS,P.MCCOURT
JRNL        TITL   STRUCTURAL ANALYSIS OF A HORMONE-BOUND STRIGA STRIGOLACTONE
JRNL        TITL 2 RECEPTOR.
JRNL        REF    NAT.PLANTS                                 2023
JRNL        REFN                   ESSN 2055-0278
JRNL        PMID   37264151
JRNL        DOI    10.1038/S41477-023-01423-Y
REMARK   2
REMARK   2 RESOLUTION.    2.64 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (DEV_3092: ???)
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) : 2.64
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.80
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2
REMARK   3   NUMBER OF REFLECTIONS             : 61813
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187
REMARK   3   R VALUE            (WORKING SET) : 0.185
REMARK   3   FREE R VALUE                     : 0.242
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.230
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998
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 10.0000 -  6.3254    0.95     4469   147  0.1599 0.1993
REMARK   3     2  6.3254 -  5.0345    1.00     4554   153  0.1707 0.1994
REMARK   3     3  5.0345 -  4.4021    1.00     4510   150  0.1432 0.2077
REMARK   3     4  4.4021 -  4.0014    1.00     4484   151  0.1459 0.2142
REMARK   3     5  4.0014 -  3.7156    0.86     3850   128  0.1710 0.2318
REMARK   3     6  3.7156 -  3.4972    0.68     3025   101  0.2177 0.2871
REMARK   3     7  3.4972 -  3.3225    1.00     4445   149  0.2050 0.2982
REMARK   3     8  3.3225 -  3.1782    1.00     4471   150  0.2150 0.2753
REMARK   3     9  3.1782 -  3.0560    1.00     4437   148  0.2276 0.2815
REMARK   3    10  3.0560 -  2.9508    1.00     4445   148  0.2468 0.3446
REMARK   3    11  2.9508 -  2.8586    1.00     4421   148  0.2666 0.2985
REMARK   3    12  2.8586 -  2.7770    1.00     4443   148  0.2643 0.3066
REMARK   3    13  2.7770 -  2.7040    1.00     4413   148  0.2788 0.3483
REMARK   3    14  2.7040 -  2.6381    0.87     3848   129  0.2979 0.3656
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : NULL
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)     : 0.390
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.020
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      :  0.006          10897
REMARK   3   ANGLE     :  1.160          14823
REMARK   3   CHIRALITY :  0.072           1662
REMARK   3   PLANARITY :  0.008           1902
REMARK   3   DIHEDRAL  : 20.646           3919
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 37
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 40 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1164  -8.1057  -3.7224
REMARK   3    T TENSOR
REMARK   3      T11:   0.4531 T22:   0.5486
REMARK   3      T33:   0.8440 T12:  -0.0187
REMARK   3      T13:   0.0507 T23:  -0.3153
REMARK   3    L TENSOR
REMARK   3      L11:   5.2390 L22:   3.8719
REMARK   3      L33:   7.1077 L12:   0.0574
REMARK   3      L13:  -0.8554 L23:  -0.6307
REMARK   3    S TENSOR
REMARK   3      S11:   0.0572 S12:  -0.3858 S13:   0.4328
REMARK   3      S21:   0.2213 S22:  -0.2629 S23:   0.3055
REMARK   3      S31:  -0.1319 S32:  -0.1018 S33:   0.2003
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 41 THROUGH 88 )
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6701  -8.4713  -9.6810
REMARK   3    T TENSOR
REMARK   3      T11:   0.4180 T22:   0.4941
REMARK   3      T33:   0.8330 T12:  -0.0085
REMARK   3      T13:   0.1116 T23:  -0.2030
REMARK   3    L TENSOR
REMARK   3      L11:   1.1833 L22:   2.8095
REMARK   3      L33:   8.0391 L12:   1.4881
REMARK   3      L13:   0.1226 L23:   0.3676
REMARK   3    S TENSOR
REMARK   3      S11:   0.0290 S12:  -0.1703 S13:   0.3057
REMARK   3      S21:   0.0103 S22:   0.0872 S23:  -0.1657
REMARK   3      S31:  -0.2430 S32:   0.3513 S33:  -0.1531
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 89 THROUGH 107 )
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8253 -18.5807  -6.8882
REMARK   3    T TENSOR
REMARK   3      T11:   0.3865 T22:   0.5745
REMARK   3      T33:   0.6069 T12:  -0.0214
REMARK   3      T13:   0.0510 T23:  -0.2477
REMARK   3    L TENSOR
REMARK   3      L11:   3.1763 L22:   4.2620
REMARK   3      L33:   2.4370 L12:  -1.6885
REMARK   3      L13:   0.3562 L23:   1.0957
REMARK   3    S TENSOR
REMARK   3      S11:   0.1280 S12:  -0.9017 S13:   0.1437
REMARK   3      S21:  -0.1297 S22:  -0.0231 S23:  -0.1835
REMARK   3      S31:  -0.2461 S32:  -0.2258 S33:  -0.0954
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 135 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.8449 -26.4683 -11.3105
REMARK   3    T TENSOR
REMARK   3      T11:   0.3924 T22:   0.4135
REMARK   3      T33:   0.7181 T12:   0.0646
REMARK   3      T13:   0.0527 T23:  -0.0570
REMARK   3    L TENSOR
REMARK   3      L11:   5.3307 L22:   6.3835
REMARK   3      L33:   4.5836 L12:   3.9406
REMARK   3      L13:   2.6111 L23:   2.7942
REMARK   3    S TENSOR
REMARK   3      S11:   0.1564 S12:  -0.1265 S13:  -0.1031
REMARK   3      S21:   0.0741 S22:   0.1404 S23:  -0.5166
REMARK   3      S31:   0.5289 S32:   0.5419 S33:  -0.3873
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 136 THROUGH 148 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6613 -23.4130 -31.3324
REMARK   3    T TENSOR
REMARK   3      T11:   0.4904 T22:   0.6641
REMARK   3      T33:   0.9110 T12:  -0.1164
REMARK   3      T13:   0.0747 T23:  -0.1207
REMARK   3    L TENSOR
REMARK   3      L11:   3.0060 L22:   5.6116
REMARK   3      L33:   4.3446 L12:   1.6539
REMARK   3      L13:  -2.2843 L23:  -4.7651
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3300 S12:   0.1468 S13:  -0.1032
REMARK   3      S21:  -0.1346 S22:   0.7401 S23:   1.4971
REMARK   3      S31:   0.1073 S32:  -0.3583 S33:  -0.4059
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 149 THROUGH 162 )
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5335 -16.1068 -25.8669
REMARK   3    T TENSOR
REMARK   3      T11:   0.4403 T22:   0.7883
REMARK   3      T33:   1.0807 T12:  -0.0437
REMARK   3      T13:   0.1863 T23:  -0.1691
REMARK   3    L TENSOR
REMARK   3      L11:   7.7871 L22:   9.7438
REMARK   3      L33:   8.0726 L12:   8.5895
REMARK   3      L13:  -6.6457 L23:  -8.0951
REMARK   3    S TENSOR
REMARK   3      S11:  -1.2134 S12:   1.4977 S13:  -0.6908
REMARK   3      S21:  -0.4866 S22:  -0.3223 S23:  -0.2326
REMARK   3      S31:   0.5422 S32:  -0.2645 S33:   1.3587
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 163 THROUGH 182 )
REMARK   3    ORIGIN FOR THE GROUP (A): -18.9774 -10.7968 -18.0271
REMARK   3    T TENSOR
REMARK   3      T11:   0.6061 T22:   0.6223
REMARK   3      T33:   0.9938 T12:   0.1144
REMARK   3      T13:   0.1178 T23:  -0.1591
REMARK   3    L TENSOR
REMARK   3      L11:   4.9186 L22:   4.6673
REMARK   3      L33:   9.3720 L12:   4.7745
REMARK   3      L13:  -6.7698 L23:  -6.6112
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0795 S12:   0.9498 S13:  -0.1323
REMARK   3      S21:   0.4359 S22:   0.5238 S23:   0.0501
REMARK   3      S31:  -0.9565 S32:  -1.4303 S33:  -0.3825
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 214 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6020 -22.5956 -14.6032
REMARK   3    T TENSOR
REMARK   3      T11:   0.3088 T22:   0.5074
REMARK   3      T33:   0.6259 T12:   0.0326
REMARK   3      T13:   0.0736 T23:  -0.1434
REMARK   3    L TENSOR
REMARK   3      L11:   2.7919 L22:   3.9487
REMARK   3      L33:   2.7297 L12:   2.6353
REMARK   3      L13:  -0.0244 L23:  -1.6047
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0133 S12:  -0.1416 S13:   0.2523
REMARK   3      S21:  -0.1326 S22:  -0.0209 S23:  -0.4285
REMARK   3      S31:   0.2135 S32:  -0.0064 S33:   0.0769
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 215 THROUGH 270 )
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8202 -26.3589  -3.9234
REMARK   3    T TENSOR
REMARK   3      T11:   0.3432 T22:   0.5025
REMARK   3      T33:   0.6027 T12:  -0.1397
REMARK   3      T13:   0.1338 T23:  -0.1308
REMARK   3    L TENSOR
REMARK   3      L11:   3.8765 L22:   8.0121
REMARK   3      L33:   5.5770 L12:  -1.5811
REMARK   3      L13:  -0.5855 L23:   1.8494
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0131 S12:  -0.3986 S13:   0.2240
REMARK   3      S21:   0.4732 S22:  -0.2237 S23:   0.2309
REMARK   3      S31:   0.2462 S32:  -0.2042 S33:   0.1924
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 14 )
REMARK   3    ORIGIN FOR THE GROUP (A):  46.8411 -29.3070 -17.2589
REMARK   3    T TENSOR
REMARK   3      T11:   0.5052 T22:   0.9183
REMARK   3      T33:   0.8556 T12:   0.1251
REMARK   3      T13:  -0.0716 T23:   0.0667
REMARK   3    L TENSOR
REMARK   3      L11:   8.7420 L22:   7.0649
REMARK   3      L33:   6.0155 L12:   4.4202
REMARK   3      L13:   1.7336 L23:  -1.6852
REMARK   3    S TENSOR
REMARK   3      S11:  -0.4696 S12:  -0.4655 S13:   1.5581
REMARK   3      S21:   0.0830 S22:   0.0313 S23:  -0.6797
REMARK   3      S31:   1.3855 S32:   1.8025 S33:  -0.0712
REMARK   3   TLS GROUP : 11
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 15 THROUGH 107 )
REMARK   3    ORIGIN FOR THE GROUP (A):  37.1903 -31.5718 -15.6690
REMARK   3    T TENSOR
REMARK   3      T11:   0.3568 T22:   0.6945
REMARK   3      T33:   0.7375 T12:   0.0019
REMARK   3      T13:  -0.0101 T23:  -0.0771
REMARK   3    L TENSOR
REMARK   3      L11:   2.6802 L22:   2.0352
REMARK   3      L33:   2.7909 L12:  -1.2599
REMARK   3      L13:  -0.0593 L23:   0.2591
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0822 S12:  -0.4946 S13:   0.4193
REMARK   3      S21:   0.2821 S22:   0.1030 S23:  -0.2352
REMARK   3      S31:  -0.0792 S32:   0.5561 S33:  -0.0380
REMARK   3   TLS GROUP : 12
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 108 THROUGH 135 )
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0028 -36.6140 -17.0024
REMARK   3    T TENSOR
REMARK   3      T11:   0.3596 T22:   0.6471
REMARK   3      T33:   0.7216 T12:  -0.0627
REMARK   3      T13:   0.1826 T23:   0.0019
REMARK   3    L TENSOR
REMARK   3      L11:   5.5896 L22:   3.9296
REMARK   3      L33:   7.5740 L12:  -2.1066
REMARK   3      L13:   3.5126 L23:  -1.2179
REMARK   3    S TENSOR
REMARK   3      S11:   0.1627 S12:  -0.3457 S13:   0.0798
REMARK   3      S21:   0.0230 S22:   0.0685 S23:   0.4301
REMARK   3      S31:  -0.0785 S32:  -0.3353 S33:  -0.2550
REMARK   3   TLS GROUP : 13
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 136 THROUGH 162 )
REMARK   3    ORIGIN FOR THE GROUP (A):  22.8917 -27.7628 -36.5168
REMARK   3    T TENSOR
REMARK   3      T11:   0.3937 T22:   0.5141
REMARK   3      T33:   0.7738 T12:   0.0574
REMARK   3      T13:  -0.0406 T23:  -0.0315
REMARK   3    L TENSOR
REMARK   3      L11:   6.1453 L22:   5.9486
REMARK   3      L33:   7.8214 L12:   0.1872
REMARK   3      L13:  -3.4070 L23:  -0.1533
REMARK   3    S TENSOR
REMARK   3      S11:   0.2653 S12:   0.3483 S13:   0.3153
REMARK   3      S21:  -0.2405 S22:  -0.4206 S23:   0.2152
REMARK   3      S31:  -0.1653 S32:   0.1218 S33:   0.1419
REMARK   3   TLS GROUP : 14
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 163 THROUGH 182 )
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3410 -16.8493 -28.4482
REMARK   3    T TENSOR
REMARK   3      T11:   0.5207 T22:   0.6505
REMARK   3      T33:   1.0097 T12:  -0.1409
REMARK   3      T13:   0.0190 T23:  -0.0443
REMARK   3    L TENSOR
REMARK   3      L11:   5.6008 L22:   9.0653
REMARK   3      L33:   8.8810 L12:  -6.9641
REMARK   3      L13:  -6.7153 L23:   7.6865
REMARK   3    S TENSOR
REMARK   3      S11:   0.4886 S12:  -0.1325 S13:   1.1676
REMARK   3      S21:   0.1376 S22:   0.1638 S23:  -0.9543
REMARK   3      S31:  -0.4224 S32:   0.1046 S33:  -0.6924
REMARK   3   TLS GROUP : 15
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 183 THROUGH 252 )
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5707 -32.4694 -17.3978
REMARK   3    T TENSOR
REMARK   3      T11:   0.3467 T22:   0.6257
REMARK   3      T33:   0.6817 T12:   0.0462
REMARK   3      T13:   0.0116 T23:  -0.0848
REMARK   3    L TENSOR
REMARK   3      L11:   3.5323 L22:   2.0182
REMARK   3      L33:   1.8525 L12:  -0.9426
REMARK   3      L13:  -0.6321 L23:  -0.5706
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0480 S12:  -0.5340 S13:   0.2411
REMARK   3      S21:   0.1885 S22:   0.0026 S23:   0.0393
REMARK   3      S31:  -0.0738 S32:   0.0720 S33:   0.0557
REMARK   3   TLS GROUP : 16
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 253 THROUGH 270 )
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6083 -23.9345  -3.5192
REMARK   3    T TENSOR
REMARK   3      T11:   0.6333 T22:   1.0791
REMARK   3      T33:   0.8584 T12:  -0.0480
REMARK   3      T13:   0.0061 T23:  -0.2928
REMARK   3    L TENSOR
REMARK   3      L11:   3.6811 L22:   8.3344
REMARK   3      L33:   4.7218 L12:   5.4212
REMARK   3      L13:  -1.9856 L23:  -1.5950
REMARK   3    S TENSOR
REMARK   3      S11:   0.9124 S12:  -1.5620 S13:   0.8348
REMARK   3      S21:   1.1579 S22:  -0.5149 S23:   1.1664
REMARK   3      S31:  -0.0251 S32:   0.8305 S33:  -0.1927
REMARK   3   TLS GROUP : 17
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 58 )
REMARK   3    ORIGIN FOR THE GROUP (A):  37.7797 -75.2527 -13.3541
REMARK   3    T TENSOR
REMARK   3      T11:   0.6284 T22:   0.9282
REMARK   3      T33:   0.7420 T12:   0.1368
REMARK   3      T13:  -0.0457 T23:   0.3395
REMARK   3    L TENSOR
REMARK   3      L11:   3.4649 L22:   5.0636
REMARK   3      L33:   4.2133 L12:   1.1522
REMARK   3      L13:  -1.2050 L23:   2.2520
REMARK   3    S TENSOR
REMARK   3      S11:   0.0723 S12:  -0.9126 S13:  -0.6430
REMARK   3      S21:   0.6524 S22:  -0.2998 S23:  -0.9967
REMARK   3      S31:   0.5850 S32:   0.5869 S33:   0.1561
REMARK   3   TLS GROUP : 18
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 59 THROUGH 195 )
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8739 -70.0993 -23.3654
REMARK   3    T TENSOR
REMARK   3      T11:   0.4899 T22:   0.5278
REMARK   3      T33:   0.4984 T12:   0.1303
REMARK   3      T13:  -0.0360 T23:   0.1112
REMARK   3    L TENSOR
REMARK   3      L11:   0.9902 L22:   3.0990
REMARK   3      L33:   5.7131 L12:   1.3010
REMARK   3      L13:  -0.7102 L23:  -1.0385
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0262 S12:  -0.1794 S13:  -0.2661
REMARK   3      S21:   0.0401 S22:  -0.2640 S23:  -0.1390
REMARK   3      S31:  -0.1020 S32:  -0.1621 S33:   0.3081
REMARK   3   TLS GROUP : 19
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 196 THROUGH 270 )
REMARK   3    ORIGIN FOR THE GROUP (A):  27.6332 -58.6983 -13.0719
REMARK   3    T TENSOR
REMARK   3      T11:   0.6427 T22:   0.5207
REMARK   3      T33:   0.3970 T12:  -0.0325
REMARK   3      T13:  -0.1042 T23:   0.0882
REMARK   3    L TENSOR
REMARK   3      L11:   7.6561 L22:   5.1503
REMARK   3      L33:   2.4345 L12:   1.0107
REMARK   3      L13:   1.7165 L23:  -0.2997
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2950 S12:  -0.2600 S13:   0.4895
REMARK   3      S21:   0.5298 S22:  -0.2532 S23:  -0.2648
REMARK   3      S31:  -0.5510 S32:   0.2389 S33:   0.5324
REMARK   3   TLS GROUP : 20
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 58 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4976 -88.3391  -3.1167
REMARK   3    T TENSOR
REMARK   3      T11:   0.8608 T22:   0.5947
REMARK   3      T33:   0.5557 T12:   0.1213
REMARK   3      T13:   0.2434 T23:   0.1912
REMARK   3    L TENSOR
REMARK   3      L11:   7.2396 L22:   4.0645
REMARK   3      L33:   5.9527 L12:  -0.1152
REMARK   3      L13:   3.5608 L23:  -1.0122
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2617 S12:  -0.7174 S13:  -0.5838
REMARK   3      S21:   0.5762 S22:   0.0735 S23:   0.0452
REMARK   3      S31:   0.4235 S32:  -0.0386 S33:   0.1822
REMARK   3   TLS GROUP : 21
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 59 THROUGH 88 )
REMARK   3    ORIGIN FOR THE GROUP (A): -19.5726 -79.4483  -6.6850
REMARK   3    T TENSOR
REMARK   3      T11:   0.7084 T22:   0.6403
REMARK   3      T33:   0.5255 T12:   0.1259
REMARK   3      T13:   0.1921 T23:   0.0337
REMARK   3    L TENSOR
REMARK   3      L11:   5.9808 L22:   3.3804
REMARK   3      L33:   9.3259 L12:   0.5377
REMARK   3      L13:   2.7035 L23:  -3.2521
REMARK   3    S TENSOR
REMARK   3      S11:  -0.6150 S12:  -0.6696 S13:  -0.0896
REMARK   3      S21:   0.7103 S22:   0.4773 S23:   0.4295
REMARK   3      S31:  -0.4596 S32:  -0.8884 S33:   0.0900
REMARK   3   TLS GROUP : 22
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 89 THROUGH 107 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.8497 -75.1410  -4.8343
REMARK   3    T TENSOR
REMARK   3      T11:   0.8304 T22:   0.6485
REMARK   3      T33:   0.3686 T12:   0.0856
REMARK   3      T13:   0.0547 T23:   0.1355
REMARK   3    L TENSOR
REMARK   3      L11:   1.1728 L22:   1.1502
REMARK   3      L33:   4.2318 L12:   0.6017
REMARK   3      L13:   1.0371 L23:  -1.1418
REMARK   3    S TENSOR
REMARK   3      S11:  -0.6488 S12:  -1.5272 S13:  -0.6227
REMARK   3      S21:   1.2170 S22:   0.5694 S23:   0.2936
REMARK   3      S31:   0.0845 S32:   0.5901 S33:   0.1029
REMARK   3   TLS GROUP : 23
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 108 THROUGH 135 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.0528 -69.8579 -10.9279
REMARK   3    T TENSOR
REMARK   3      T11:   0.6311 T22:   0.3446
REMARK   3      T33:   0.5130 T12:  -0.0231
REMARK   3      T13:  -0.0422 T23:   0.0095
REMARK   3    L TENSOR
REMARK   3      L11:   9.1303 L22:   4.8160
REMARK   3      L33:   5.6704 L12:   1.2024
REMARK   3      L13:  -2.3098 L23:   0.4372
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3243 S12:  -0.0461 S13:   0.8819
REMARK   3      S21:   0.1372 S22:   0.4715 S23:   0.0720
REMARK   3      S31:  -0.7188 S32:   0.3647 S33:  -0.1726
REMARK   3   TLS GROUP : 24
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 136 THROUGH 162 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0814 -79.7618 -29.9336
REMARK   3    T TENSOR
REMARK   3      T11:   0.7481 T22:   0.6737
REMARK   3      T33:   0.6707 T12:  -0.0510
REMARK   3      T13:   0.1361 T23:   0.1447
REMARK   3    L TENSOR
REMARK   3      L11:   2.4839 L22:   2.3069
REMARK   3      L33:   5.0976 L12:  -0.6936
REMARK   3      L13:   1.1510 L23:   2.6754
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2057 S12:   0.5124 S13:   0.0087
REMARK   3      S21:  -0.5357 S22:  -0.0375 S23:  -0.0330
REMARK   3      S31:   0.2923 S32:  -0.5583 S33:   0.2265
REMARK   3   TLS GROUP : 25
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 163 THROUGH 182 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0034 -91.9645 -21.2798
REMARK   3    T TENSOR
REMARK   3      T11:   0.8512 T22:   0.5290
REMARK   3      T33:   0.7867 T12:   0.0258
REMARK   3      T13:   0.1686 T23:   0.1697
REMARK   3    L TENSOR
REMARK   3      L11:   3.7338 L22:   2.5147
REMARK   3      L33:   3.9266 L12:   3.0531
REMARK   3      L13:   2.4568 L23:   1.9385
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1203 S12:   0.4308 S13:  -2.3585
REMARK   3      S21:   0.0440 S22:   0.2727 S23:  -0.4647
REMARK   3      S31:   0.3782 S32:   0.3227 S33:  -0.0924
REMARK   3   TLS GROUP : 26
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 183 THROUGH 214 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.3869 -72.0105 -13.0292
REMARK   3    T TENSOR
REMARK   3      T11:   0.5886 T22:   0.5094
REMARK   3      T33:   0.4851 T12:   0.0459
REMARK   3      T13:   0.0150 T23:   0.0636
REMARK   3    L TENSOR
REMARK   3      L11:   4.8441 L22:   3.3471
REMARK   3      L33:   3.9800 L12:   2.2059
REMARK   3      L13:   2.1560 L23:   2.8815
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3677 S12:  -0.1850 S13:   0.4474
REMARK   3      S21:   0.0380 S22:  -0.3196 S23:   0.3316
REMARK   3      S31:  -0.2090 S32:  -0.4268 S33:   0.7417
REMARK   3   TLS GROUP : 27
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 215 THROUGH 231 )
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0737 -69.4337 -13.8002
REMARK   3    T TENSOR
REMARK   3      T11:   0.9055 T22:   0.7311
REMARK   3      T33:   0.8009 T12:  -0.1868
REMARK   3      T13:  -0.0964 T23:   0.0532
REMARK   3    L TENSOR
REMARK   3      L11:   4.6508 L22:   6.8629
REMARK   3      L33:   3.3392 L12:  -5.0287
REMARK   3      L13:  -2.9484 L23:   1.8349
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1110 S12:   0.2491 S13:   1.3209
REMARK   3      S21:  -0.7785 S22:   0.0308 S23:  -0.8492
REMARK   3      S31:  -1.3639 S32:   0.3579 S33:  -0.0654
REMARK   3   TLS GROUP : 28
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 232 THROUGH 270 )
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7017 -78.8925  -4.6056
REMARK   3    T TENSOR
REMARK   3      T11:   0.6511 T22:   0.8136
REMARK   3      T33:   0.5456 T12:   0.1941
REMARK   3      T13:   0.0295 T23:   0.2215
REMARK   3    L TENSOR
REMARK   3      L11:   4.7837 L22:   9.2977
REMARK   3      L33:   1.3513 L12:  -0.5926
REMARK   3      L13:  -0.2457 L23:  -3.5049
REMARK   3    S TENSOR
REMARK   3      S11:  -0.7817 S12:  -0.6074 S13:  -0.3371
REMARK   3      S21:   1.1480 S22:   0.2916 S23:  -0.3827
REMARK   3      S31:   0.2310 S32:   0.9169 S33:   0.4499
REMARK   3   TLS GROUP : 29
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 14 )
REMARK   3    ORIGIN FOR THE GROUP (A): -40.0332 -39.9628   2.5881
REMARK   3    T TENSOR
REMARK   3      T11:   1.1301 T22:   0.7834
REMARK   3      T33:   0.5901 T12:   0.0429
REMARK   3      T13:   0.3305 T23:   0.0211
REMARK   3    L TENSOR
REMARK   3      L11:   9.4213 L22:   0.7959
REMARK   3      L33:   4.2876 L12:  -0.1405
REMARK   3      L13:   4.6568 L23:   0.5371
REMARK   3    S TENSOR
REMARK   3      S11:  -0.9830 S12:   0.1324 S13:  -0.1683
REMARK   3      S21:   2.4473 S22:   0.7810 S23:   1.5041
REMARK   3      S31:  -1.8314 S32:  -1.6202 S33:   0.0003
REMARK   3   TLS GROUP : 30
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 15 THROUGH 58 )
REMARK   3    ORIGIN FOR THE GROUP (A): -34.6518 -48.9089   2.4016
REMARK   3    T TENSOR
REMARK   3      T11:   0.8397 T22:   0.8008
REMARK   3      T33:   0.6347 T12:  -0.1466
REMARK   3      T13:   0.2673 T23:  -0.1192
REMARK   3    L TENSOR
REMARK   3      L11:   5.2200 L22:   6.7632
REMARK   3      L33:   3.1002 L12:  -0.9568
REMARK   3      L13:   2.1410 L23:  -2.1700
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2117 S12:  -0.9524 S13:   0.1560
REMARK   3      S21:   1.3088 S22:   0.0983 S23:   0.1721
REMARK   3      S31:   0.0490 S32:  -0.8434 S33:   0.1065
REMARK   3   TLS GROUP : 31
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 59 THROUGH 107 )
REMARK   3    ORIGIN FOR THE GROUP (A): -28.7965 -38.0397  -3.3276
REMARK   3    T TENSOR
REMARK   3      T11:   0.5736 T22:   0.4719
REMARK   3      T33:   0.6296 T12:  -0.0776
REMARK   3      T13:   0.1254 T23:  -0.1700
REMARK   3    L TENSOR
REMARK   3      L11:   3.7391 L22:   3.9225
REMARK   3      L33:   9.0786 L12:  -1.5758
REMARK   3      L13:   2.0235 L23:  -0.5376
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2980 S12:  -0.4372 S13:   0.4769
REMARK   3      S21:   0.8736 S22:  -0.1450 S23:   0.1834
REMARK   3      S31:  -0.1320 S32:  -0.7695 S33:   0.4196
REMARK   3   TLS GROUP : 32
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 108 THROUGH 135 )
REMARK   3    ORIGIN FOR THE GROUP (A): -17.8622 -47.2948  -7.8400
REMARK   3    T TENSOR
REMARK   3      T11:   0.5412 T22:   0.4927
REMARK   3      T33:   0.6563 T12:  -0.0372
REMARK   3      T13:  -0.0210 T23:   0.1206
REMARK   3    L TENSOR
REMARK   3      L11:   5.7384 L22:   7.1324
REMARK   3      L33:   9.0442 L12:  -1.2600
REMARK   3      L13:  -2.1509 L23:   4.7305
REMARK   3    S TENSOR
REMARK   3      S11:   0.0804 S12:   0.4518 S13:   0.6121
REMARK   3      S21:   0.7592 S22:  -0.3385 S23:  -0.7916
REMARK   3      S31:   0.3837 S32:   0.0606 S33:   0.1804
REMARK   3   TLS GROUP : 33
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 136 THROUGH 148 )
REMARK   3    ORIGIN FOR THE GROUP (A): -26.2722 -47.8077 -27.3441
REMARK   3    T TENSOR
REMARK   3      T11:   0.5242 T22:   0.7845
REMARK   3      T33:   0.7625 T12:   0.0053
REMARK   3      T13:   0.0339 T23:   0.1968
REMARK   3    L TENSOR
REMARK   3      L11:   2.1725 L22:   2.1118
REMARK   3      L33:   2.1397 L12:  -0.8729
REMARK   3      L13:  -0.1056 L23:  -1.0735
REMARK   3    S TENSOR
REMARK   3      S11:   0.0265 S12:   0.3201 S13:  -1.0720
REMARK   3      S21:  -0.0212 S22:  -0.8080 S23:  -0.9960
REMARK   3      S31:   0.1065 S32:   0.4927 S33:   0.8006
REMARK   3   TLS GROUP : 34
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 149 THROUGH 182 )
REMARK   3    ORIGIN FOR THE GROUP (A): -37.7365 -56.3934 -16.9277
REMARK   3    T TENSOR
REMARK   3      T11:   0.5248 T22:   0.7004
REMARK   3      T33:   0.7406 T12:  -0.2214
REMARK   3      T13:   0.1240 T23:  -0.0496
REMARK   3    L TENSOR
REMARK   3      L11:   3.1526 L22:   4.2192
REMARK   3      L33:   5.4175 L12:  -3.2860
REMARK   3      L13:   2.0644 L23:  -0.7102
REMARK   3    S TENSOR
REMARK   3      S11:   0.0160 S12:  -0.2686 S13:   0.1755
REMARK   3      S21:   0.0393 S22:   0.1461 S23:   0.2494
REMARK   3      S31:   0.6015 S32:  -0.9599 S33:  -0.2090
REMARK   3   TLS GROUP : 35
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 183 THROUGH 207 )
REMARK   3    ORIGIN FOR THE GROUP (A): -22.6384 -41.7302 -12.6686
REMARK   3    T TENSOR
REMARK   3      T11:   0.4690 T22:   0.4311
REMARK   3      T33:   0.7232 T12:  -0.0978
REMARK   3      T13:  -0.0578 T23:  -0.0344
REMARK   3    L TENSOR
REMARK   3      L11:   8.5417 L22:   2.8150
REMARK   3      L33:   6.0147 L12:   0.4354
REMARK   3      L13:   6.0050 L23:   0.9462
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2807 S12:   0.0694 S13:   1.5138
REMARK   3      S21:   0.2877 S22:  -0.2467 S23:  -0.3813
REMARK   3      S31:  -0.2408 S32:   0.4344 S33:   0.6253
REMARK   3   TLS GROUP : 36
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 208 THROUGH 241 )
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6335 -54.6959  -4.9937
REMARK   3    T TENSOR
REMARK   3      T11:   0.7945 T22:   0.4799
REMARK   3      T33:   0.5733 T12:   0.1205
REMARK   3      T13:  -0.0547 T23:   0.0400
REMARK   3    L TENSOR
REMARK   3      L11:   2.4169 L22:   4.8270
REMARK   3      L33:   8.8124 L12:  -0.2946
REMARK   3      L13:  -0.0429 L23:   3.9956
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2094 S12:  -0.0924 S13:   0.3121
REMARK   3      S21:   1.0075 S22:  -0.2243 S23:  -0.1186
REMARK   3      S31:   0.8214 S32:   0.2294 S33:   0.3634
REMARK   3   TLS GROUP : 37
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 242 THROUGH 270 )
REMARK   3    ORIGIN FOR THE GROUP (A): -24.6295 -59.3160   1.7624
REMARK   3    T TENSOR
REMARK   3      T11:   0.9085 T22:   0.6789
REMARK   3      T33:   0.5149 T12:  -0.0583
REMARK   3      T13:   0.2037 T23:   0.0353
REMARK   3    L TENSOR
REMARK   3      L11:   5.9151 L22:   8.5992
REMARK   3      L33:   8.1726 L12:  -1.8992
REMARK   3      L13:   1.5392 L23:   1.8425
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2914 S12:  -0.4239 S13:  -0.2704
REMARK   3      S21:   1.1880 S22:  -0.0520 S23:   0.1946
REMARK   3      S31:   1.2830 S32:   0.3545 S33:   0.2967
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 8DVC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-22.
REMARK 100 THE DEPOSITION ID IS D_1000267348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-16
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 21-ID-D
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97903
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61856
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.630
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1
REMARK 200  DATA REDUNDANCY                : 5.100
REMARK 200  R MERGE                    (I) : 0.08400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.68
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.88900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 0.890
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 5CBK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 66.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 0.1 M BIS-TRIS,
REMARK 280  PH 5.5, 8 MM GR24, 1% DMSO, 1% ISOPROPANOL, CRYOPROTECTANT:
REMARK 280  ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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       62.49400
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.49400
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       49.63450
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      176.48350
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       49.63450
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      176.48350
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       62.49400
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       49.63450
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      176.48350
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       62.49400
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       49.63450
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      176.48350
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     SER A     2
REMARK 465     ASP A   271
REMARK 465     ASP B   271
REMARK 465     ASP C   271
REMARK 465     ASP D   271
REMARK 465     MET E     1
REMARK 465     ASP E   271
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    TRP A  33       30.55    -99.11
REMARK 500    ALA A  95     -112.89     56.66
REMARK 500    ARG A 123      129.68   -174.77
REMARK 500    ASN A 149       85.75   -152.86
REMARK 500    PRO A 242       80.10    -68.25
REMARK 500    ALA A 252       57.84   -149.81
REMARK 500    ALA B  95      -99.02     56.23
REMARK 500    ASN B 149       75.88   -161.85
REMARK 500    SER B 236      141.51   -176.00
REMARK 500    ASP B 267     -161.11   -102.22
REMARK 500    ALA C  95     -114.68     54.48
REMARK 500    ASP C 129      -18.02     96.38
REMARK 500    ASN C 149       85.97   -155.94
REMARK 500    LYS C 216       41.39   -143.50
REMARK 500    PRO C 242       99.71    -66.21
REMARK 500    THR C 243      149.22   -173.91
REMARK 500    ALA D  95     -107.31     51.64
REMARK 500    ARG D 123      122.17   -170.61
REMARK 500    ASP D 267     -164.52   -105.47
REMARK 500    THR E  28     -165.12   -124.61
REMARK 500    ALA E  95     -105.14     45.84
REMARK 500    TYR E 130      107.92   -164.17
REMARK 500    ASN E 149       78.85   -161.20
REMARK 500    LYS E 216       44.81   -142.13
REMARK 500    ASP E 267     -155.51   -115.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH C 431        DISTANCE =  6.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TZU A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TZU B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TZU C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TZU D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TZU E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO E 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO E 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6DVA   RELATED DB: PDB
REMARK 900 RELATED ID: 5CBK   RELATED DB: PDB
DBREF1 8DVC A    1   271  UNP                  A0A0M5I297_STRHE
DBREF2 8DVC A     A0A0M5I297                          1         271
DBREF1 8DVC B    1   271  UNP                  A0A0M5I297_STRHE
DBREF2 8DVC B     A0A0M5I297                          1         271
DBREF1 8DVC C    1   271  UNP                  A0A0M5I297_STRHE
DBREF2 8DVC C     A0A0M5I297                          1         271
DBREF1 8DVC D    1   271  UNP                  A0A0M5I297_STRHE
DBREF2 8DVC D     A0A0M5I297                          1         271
DBREF1 8DVC E    1   271  UNP                  A0A0M5I297_STRHE
DBREF2 8DVC E     A0A0M5I297                          1         271
SEQADV 8DVC ALA A   95  UNP  A0A0M5I29 SER    95 ENGINEERED MUTATION
SEQADV 8DVC ALA B   95  UNP  A0A0M5I29 SER    95 ENGINEERED MUTATION
SEQADV 8DVC ALA C   95  UNP  A0A0M5I29 SER    95 ENGINEERED MUTATION
SEQADV 8DVC ALA D   95  UNP  A0A0M5I29 SER    95 ENGINEERED MUTATION
SEQADV 8DVC ALA E   95  UNP  A0A0M5I29 SER    95 ENGINEERED MUTATION
SEQRES   1 A  271  MET SER THR VAL GLY SER ALA HIS ASN VAL THR VAL LEU
SEQRES   2 A  271  GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS GLY PHE
SEQRES   3 A  271  GLY THR ASP GLN SER VAL TRP LYS TYR LEU VAL PRO HIS
SEQRES   4 A  271  LEU THR ASP ASP TYR ARG VAL LEU LEU TYR ASP ASN MET
SEQRES   5 A  271  GLY ALA GLY THR THR ASP PRO ASN LEU TYR ASP PHE GLU
SEQRES   6 A  271  ARG TYR SER SER LEU GLU GLY HIS SER GLN ASP LEU ILE
SEQRES   7 A  271  ALA ILE LEU GLU GLU PHE HIS VAL THR LYS CYS ILE PHE
SEQRES   8 A  271  VAL GLY HIS ALA LEU SER SER MET VAL GLY ALA VAL SER
SEQRES   9 A  271  SER ILE PHE ARG PRO ASP LEU PHE ARG LYS ILE VAL MET
SEQRES  10 A  271  ILE SER ALA CYS PRO ARG VAL ALA ASN ALA ASP ASP TYR
SEQRES  11 A  271  TYR GLY GLY PHE GLU GLU GLU ASP VAL ASN GLN LEU TYR
SEQRES  12 A  271  GLY ALA MET GLU GLU ASN PHE GLN THR MET MET THR GLY
SEQRES  13 A  271  TYR ALA PRO ILE VAL VAL GLY GLY ASP LEU GLU SER GLU
SEQRES  14 A  271  ALA MET GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES  15 A  271  PRO ASP ILE ALA LEU SER ILE CYS ARG MET ILE SER GLY
SEQRES  16 A  271  TYR ASP LEU ARG PRO TYR LEU GLY LEU VAL VAL ILE PRO
SEQRES  17 A  271  CYS HIS ILE ILE GLN SER SER LYS ASP LYS LEU VAL PRO
SEQRES  18 A  271  VAL ALA VAL ALA GLU TYR LEU HIS ARG ASN PHE GLY GLY
SEQRES  19 A  271  LYS SER VAL VAL GLU LEU ILE PRO THR GLU GLY HIS LEU
SEQRES  20 A  271  PRO HIS LEU SER ALA PRO ASP ILE THR ILE PRO VAL LEU
SEQRES  21 A  271  ILE ARG HIS ILE ASN GLN ASP ILE ALA ASP ASP
SEQRES   1 B  271  MET SER THR VAL GLY SER ALA HIS ASN VAL THR VAL LEU
SEQRES   2 B  271  GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS GLY PHE
SEQRES   3 B  271  GLY THR ASP GLN SER VAL TRP LYS TYR LEU VAL PRO HIS
SEQRES   4 B  271  LEU THR ASP ASP TYR ARG VAL LEU LEU TYR ASP ASN MET
SEQRES   5 B  271  GLY ALA GLY THR THR ASP PRO ASN LEU TYR ASP PHE GLU
SEQRES   6 B  271  ARG TYR SER SER LEU GLU GLY HIS SER GLN ASP LEU ILE
SEQRES   7 B  271  ALA ILE LEU GLU GLU PHE HIS VAL THR LYS CYS ILE PHE
SEQRES   8 B  271  VAL GLY HIS ALA LEU SER SER MET VAL GLY ALA VAL SER
SEQRES   9 B  271  SER ILE PHE ARG PRO ASP LEU PHE ARG LYS ILE VAL MET
SEQRES  10 B  271  ILE SER ALA CYS PRO ARG VAL ALA ASN ALA ASP ASP TYR
SEQRES  11 B  271  TYR GLY GLY PHE GLU GLU GLU ASP VAL ASN GLN LEU TYR
SEQRES  12 B  271  GLY ALA MET GLU GLU ASN PHE GLN THR MET MET THR GLY
SEQRES  13 B  271  TYR ALA PRO ILE VAL VAL GLY GLY ASP LEU GLU SER GLU
SEQRES  14 B  271  ALA MET GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES  15 B  271  PRO ASP ILE ALA LEU SER ILE CYS ARG MET ILE SER GLY
SEQRES  16 B  271  TYR ASP LEU ARG PRO TYR LEU GLY LEU VAL VAL ILE PRO
SEQRES  17 B  271  CYS HIS ILE ILE GLN SER SER LYS ASP LYS LEU VAL PRO
SEQRES  18 B  271  VAL ALA VAL ALA GLU TYR LEU HIS ARG ASN PHE GLY GLY
SEQRES  19 B  271  LYS SER VAL VAL GLU LEU ILE PRO THR GLU GLY HIS LEU
SEQRES  20 B  271  PRO HIS LEU SER ALA PRO ASP ILE THR ILE PRO VAL LEU
SEQRES  21 B  271  ILE ARG HIS ILE ASN GLN ASP ILE ALA ASP ASP
SEQRES   1 C  271  MET SER THR VAL GLY SER ALA HIS ASN VAL THR VAL LEU
SEQRES   2 C  271  GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS GLY PHE
SEQRES   3 C  271  GLY THR ASP GLN SER VAL TRP LYS TYR LEU VAL PRO HIS
SEQRES   4 C  271  LEU THR ASP ASP TYR ARG VAL LEU LEU TYR ASP ASN MET
SEQRES   5 C  271  GLY ALA GLY THR THR ASP PRO ASN LEU TYR ASP PHE GLU
SEQRES   6 C  271  ARG TYR SER SER LEU GLU GLY HIS SER GLN ASP LEU ILE
SEQRES   7 C  271  ALA ILE LEU GLU GLU PHE HIS VAL THR LYS CYS ILE PHE
SEQRES   8 C  271  VAL GLY HIS ALA LEU SER SER MET VAL GLY ALA VAL SER
SEQRES   9 C  271  SER ILE PHE ARG PRO ASP LEU PHE ARG LYS ILE VAL MET
SEQRES  10 C  271  ILE SER ALA CYS PRO ARG VAL ALA ASN ALA ASP ASP TYR
SEQRES  11 C  271  TYR GLY GLY PHE GLU GLU GLU ASP VAL ASN GLN LEU TYR
SEQRES  12 C  271  GLY ALA MET GLU GLU ASN PHE GLN THR MET MET THR GLY
SEQRES  13 C  271  TYR ALA PRO ILE VAL VAL GLY GLY ASP LEU GLU SER GLU
SEQRES  14 C  271  ALA MET GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES  15 C  271  PRO ASP ILE ALA LEU SER ILE CYS ARG MET ILE SER GLY
SEQRES  16 C  271  TYR ASP LEU ARG PRO TYR LEU GLY LEU VAL VAL ILE PRO
SEQRES  17 C  271  CYS HIS ILE ILE GLN SER SER LYS ASP LYS LEU VAL PRO
SEQRES  18 C  271  VAL ALA VAL ALA GLU TYR LEU HIS ARG ASN PHE GLY GLY
SEQRES  19 C  271  LYS SER VAL VAL GLU LEU ILE PRO THR GLU GLY HIS LEU
SEQRES  20 C  271  PRO HIS LEU SER ALA PRO ASP ILE THR ILE PRO VAL LEU
SEQRES  21 C  271  ILE ARG HIS ILE ASN GLN ASP ILE ALA ASP ASP
SEQRES   1 D  271  MET SER THR VAL GLY SER ALA HIS ASN VAL THR VAL LEU
SEQRES   2 D  271  GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS GLY PHE
SEQRES   3 D  271  GLY THR ASP GLN SER VAL TRP LYS TYR LEU VAL PRO HIS
SEQRES   4 D  271  LEU THR ASP ASP TYR ARG VAL LEU LEU TYR ASP ASN MET
SEQRES   5 D  271  GLY ALA GLY THR THR ASP PRO ASN LEU TYR ASP PHE GLU
SEQRES   6 D  271  ARG TYR SER SER LEU GLU GLY HIS SER GLN ASP LEU ILE
SEQRES   7 D  271  ALA ILE LEU GLU GLU PHE HIS VAL THR LYS CYS ILE PHE
SEQRES   8 D  271  VAL GLY HIS ALA LEU SER SER MET VAL GLY ALA VAL SER
SEQRES   9 D  271  SER ILE PHE ARG PRO ASP LEU PHE ARG LYS ILE VAL MET
SEQRES  10 D  271  ILE SER ALA CYS PRO ARG VAL ALA ASN ALA ASP ASP TYR
SEQRES  11 D  271  TYR GLY GLY PHE GLU GLU GLU ASP VAL ASN GLN LEU TYR
SEQRES  12 D  271  GLY ALA MET GLU GLU ASN PHE GLN THR MET MET THR GLY
SEQRES  13 D  271  TYR ALA PRO ILE VAL VAL GLY GLY ASP LEU GLU SER GLU
SEQRES  14 D  271  ALA MET GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES  15 D  271  PRO ASP ILE ALA LEU SER ILE CYS ARG MET ILE SER GLY
SEQRES  16 D  271  TYR ASP LEU ARG PRO TYR LEU GLY LEU VAL VAL ILE PRO
SEQRES  17 D  271  CYS HIS ILE ILE GLN SER SER LYS ASP LYS LEU VAL PRO
SEQRES  18 D  271  VAL ALA VAL ALA GLU TYR LEU HIS ARG ASN PHE GLY GLY
SEQRES  19 D  271  LYS SER VAL VAL GLU LEU ILE PRO THR GLU GLY HIS LEU
SEQRES  20 D  271  PRO HIS LEU SER ALA PRO ASP ILE THR ILE PRO VAL LEU
SEQRES  21 D  271  ILE ARG HIS ILE ASN GLN ASP ILE ALA ASP ASP
SEQRES   1 E  271  MET SER THR VAL GLY SER ALA HIS ASN VAL THR VAL LEU
SEQRES   2 E  271  GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS GLY PHE
SEQRES   3 E  271  GLY THR ASP GLN SER VAL TRP LYS TYR LEU VAL PRO HIS
SEQRES   4 E  271  LEU THR ASP ASP TYR ARG VAL LEU LEU TYR ASP ASN MET
SEQRES   5 E  271  GLY ALA GLY THR THR ASP PRO ASN LEU TYR ASP PHE GLU
SEQRES   6 E  271  ARG TYR SER SER LEU GLU GLY HIS SER GLN ASP LEU ILE
SEQRES   7 E  271  ALA ILE LEU GLU GLU PHE HIS VAL THR LYS CYS ILE PHE
SEQRES   8 E  271  VAL GLY HIS ALA LEU SER SER MET VAL GLY ALA VAL SER
SEQRES   9 E  271  SER ILE PHE ARG PRO ASP LEU PHE ARG LYS ILE VAL MET
SEQRES  10 E  271  ILE SER ALA CYS PRO ARG VAL ALA ASN ALA ASP ASP TYR
SEQRES  11 E  271  TYR GLY GLY PHE GLU GLU GLU ASP VAL ASN GLN LEU TYR
SEQRES  12 E  271  GLY ALA MET GLU GLU ASN PHE GLN THR MET MET THR GLY
SEQRES  13 E  271  TYR ALA PRO ILE VAL VAL GLY GLY ASP LEU GLU SER GLU
SEQRES  14 E  271  ALA MET GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES  15 E  271  PRO ASP ILE ALA LEU SER ILE CYS ARG MET ILE SER GLY
SEQRES  16 E  271  TYR ASP LEU ARG PRO TYR LEU GLY LEU VAL VAL ILE PRO
SEQRES  17 E  271  CYS HIS ILE ILE GLN SER SER LYS ASP LYS LEU VAL PRO
SEQRES  18 E  271  VAL ALA VAL ALA GLU TYR LEU HIS ARG ASN PHE GLY GLY
SEQRES  19 E  271  LYS SER VAL VAL GLU LEU ILE PRO THR GLU GLY HIS LEU
SEQRES  20 E  271  PRO HIS LEU SER ALA PRO ASP ILE THR ILE PRO VAL LEU
SEQRES  21 E  271  ILE ARG HIS ILE ASN GLN ASP ILE ALA ASP ASP
HET    TZU  A 301      22
HET    SO4  A 302       5
HET    SO4  A 303       5
HET    SO4  A 304       5
HET    SO4  A 305       5
HET    EDO  A 306       4
HET    EDO  A 307       4
HET     CL  A 308       1
HET     CL  A 309       1
HET    TZU  B 301      22
HET    SO4  B 302       5
HET    SO4  B 303       5
HET    SO4  B 304       5
HET    EDO  B 305       4
HET     CL  B 306       1
HET    TZU  C 301      22
HET    SO4  C 302       5
HET    EDO  C 303       4
HET    EDO  C 304       4
HET    EDO  C 305       4
HET    EDO  C 306       4
HET    TZU  D 301      22
HET    SO4  D 302       5
HET    SO4  D 303       5
HET    SO4  D 304       5
HET     CL  D 305       1
HET     CL  D 306       1
HET    TZU  E 301      22
HET    SO4  E 302       5
HET    SO4  E 303       5
HET    EDO  E 304       4
HET    EDO  E 305       4
HET     CL  E 306       1
HETNAM     TZU (3R,3AR,8BS)-3-({[(2R)-4-METHYL-5-OXO-2,5-DIHYDROFURAN-
HETNAM   2 TZU  2-YL]OXY}METHYL)-3,3A,4,8B-TETRAHYDRO-2H-INDENO[1,2-
HETNAM   3 TZU  B]FURAN-2-ONE
HETNAM     SO4 SULFATE ION
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM      CL CHLORIDE ION
HETSYN     TZU GR24
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   6  TZU    5(C17 H16 O5)
FORMUL   7  SO4    13(O4 S 2-)
FORMUL  11  EDO    9(C2 H6 O2)
FORMUL  13   CL    6(CL 1-)
FORMUL  39  HOH   *212(H2 O)
HELIX    1 AA1 THR A    3  HIS A    8  1                                   6
HELIX    2 AA2 ASP A   29  LYS A   34  5                                   6
HELIX    3 AA3 LEU A   36  LEU A   40  5                                   5
HELIX    4 AA4 ASP A   58  TYR A   62  5                                   5
HELIX    5 AA5 GLU A   65  SER A   68  5                                   4
HELIX    6 AA6 SER A   69  PHE A   84  1                                  16
HELIX    7 AA7 ALA A   95  ARG A  108  1                                  14
HELIX    8 AA8 GLU A  136  ASN A  149  1                                  14
HELIX    9 AA9 ASN A  149  GLY A  163  1                                  15
HELIX   10 AB1 SER A  168  PHE A  179  1                                  12
HELIX   11 AB2 ARG A  182  TYR A  196  1                                  15
HELIX   12 AB3 LEU A  198  VAL A  205  5                                   8
HELIX   13 AB4 PRO A  221  PHE A  232  1                                  12
HELIX   14 AB5 LEU A  247  ALA A  252  1                                   6
HELIX   15 AB6 ALA A  252  GLN A  266  1                                  15
HELIX   16 AB7 THR B    3  HIS B    8  1                                   6
HELIX   17 AB8 ASP B   29  LYS B   34  5                                   6
HELIX   18 AB9 LEU B   36  LEU B   40  5                                   5
HELIX   19 AC1 ASP B   58  TYR B   62  5                                   5
HELIX   20 AC2 ASP B   63  SER B   68  1                                   6
HELIX   21 AC3 SER B   69  PHE B   84  1                                  16
HELIX   22 AC4 ALA B   95  ARG B  108  1                                  14
HELIX   23 AC5 GLU B  135  ASN B  149  1                                  15
HELIX   24 AC6 ASN B  149  GLY B  163  1                                  15
HELIX   25 AC7 SER B  168  PHE B  179  1                                  12
HELIX   26 AC8 ARG B  182  TYR B  196  1                                  15
HELIX   27 AC9 LEU B  198  VAL B  205  5                                   8
HELIX   28 AD1 PRO B  221  PHE B  232  1                                  12
HELIX   29 AD2 LEU B  247  ALA B  252  1                                   6
HELIX   30 AD3 ALA B  252  GLN B  266  1                                  15
HELIX   31 AD4 ASP C   29  LYS C   34  5                                   6
HELIX   32 AD5 LEU C   36  LEU C   40  5                                   5
HELIX   33 AD6 ASP C   58  TYR C   62  5                                   5
HELIX   34 AD7 ASP C   63  SER C   68  1                                   6
HELIX   35 AD8 LEU C   70  PHE C   84  1                                  15
HELIX   36 AD9 ALA C   95  ARG C  108  1                                  14
HELIX   37 AE1 GLU C  135  ASN C  149  1                                  15
HELIX   38 AE2 ASN C  149  GLY C  163  1                                  15
HELIX   39 AE3 SER C  168  PHE C  179  1                                  12
HELIX   40 AE4 ARG C  182  SER C  194  1                                  13
HELIX   41 AE5 LEU C  198  VAL C  205  5                                   8
HELIX   42 AE6 PRO C  221  ARG C  230  1                                  10
HELIX   43 AE7 LEU C  247  ALA C  252  1                                   6
HELIX   44 AE8 ALA C  252  GLN C  266  1                                  15
HELIX   45 AE9 THR D    3  HIS D    8  1                                   6
HELIX   46 AF1 ASP D   29  LYS D   34  5                                   6
HELIX   47 AF2 LEU D   36  LEU D   40  5                                   5
HELIX   48 AF3 ASP D   58  TYR D   62  5                                   5
HELIX   49 AF4 GLU D   65  SER D   69  5                                   5
HELIX   50 AF5 LEU D   70  PHE D   84  1                                  15
HELIX   51 AF6 ALA D   95  ARG D  108  1                                  14
HELIX   52 AF7 GLU D  135  ASN D  149  1                                  15
HELIX   53 AF8 ASN D  149  GLY D  163  1                                  15
HELIX   54 AF9 SER D  168  MET D  181  1                                  14
HELIX   55 AG1 ARG D  182  TYR D  196  1                                  15
HELIX   56 AG2 LEU D  198  VAL D  205  5                                   8
HELIX   57 AG3 PRO D  221  PHE D  232  1                                  12
HELIX   58 AG4 LEU D  247  ALA D  252  1                                   6
HELIX   59 AG5 ALA D  252  GLN D  266  1                                  15
HELIX   60 AG6 THR E    3  HIS E    8  1                                   6
HELIX   61 AG7 ASP E   29  LYS E   34  5                                   6
HELIX   62 AG8 LEU E   36  LEU E   40  5                                   5
HELIX   63 AG9 ASP E   58  TYR E   62  5                                   5
HELIX   64 AH1 GLU E   65  SER E   68  5                                   4
HELIX   65 AH2 SER E   69  PHE E   84  1                                  16
HELIX   66 AH3 ALA E   95  ARG E  108  1                                  14
HELIX   67 AH4 GLU E  135  ASN E  149  1                                  15
HELIX   68 AH5 ASN E  149  GLY E  163  1                                  15
HELIX   69 AH6 SER E  168  PHE E  179  1                                  12
HELIX   70 AH7 ARG E  182  TYR E  196  1                                  15
HELIX   71 AH8 TYR E  201  VAL E  205  5                                   5
HELIX   72 AH9 PRO E  221  PHE E  232  1                                  12
HELIX   73 AI1 LEU E  247  ALA E  252  1                                   6
HELIX   74 AI2 ALA E  252  GLN E  266  1                                  15
SHEET    1 AA1 7 THR A  11  GLY A  14  0
SHEET    2 AA1 7 ARG A  45  LEU A  48 -1  O  VAL A  46   N  LEU A  13
SHEET    3 AA1 7 THR A  19  GLY A  23  1  N  VAL A  20   O  ARG A  45
SHEET    4 AA1 7 CYS A  89  HIS A  94  1  O  VAL A  92   N  VAL A  21
SHEET    5 AA1 7 PHE A 112  ILE A 118  1  O  ARG A 113   N  CYS A  89
SHEET    6 AA1 7 CYS A 209  LYS A 216  1  O  HIS A 210   N  ILE A 115
SHEET    7 AA1 7 SER A 236  GLU A 244  1  O  VAL A 237   N  ILE A 211
SHEET    1 AA2 2 ALA A 125  ASN A 126  0
SHEET    2 AA2 2 PHE A 134  GLU A 135  1  O  PHE A 134   N  ASN A 126
SHEET    1 AA3 7 THR B  11  GLY B  14  0
SHEET    2 AA3 7 ARG B  45  TYR B  49 -1  O  LEU B  48   N  THR B  11
SHEET    3 AA3 7 THR B  19  GLY B  23  1  N  VAL B  20   O  ARG B  45
SHEET    4 AA3 7 CYS B  89  HIS B  94  1  O  VAL B  92   N  VAL B  21
SHEET    5 AA3 7 PHE B 112  ILE B 118  1  O  VAL B 116   N  PHE B  91
SHEET    6 AA3 7 CYS B 209  LYS B 216  1  O  HIS B 210   N  ILE B 115
SHEET    7 AA3 7 SER B 236  GLU B 244  1  O  ILE B 241   N  GLN B 213
SHEET    1 AA4 7 THR C  11  GLY C  14  0
SHEET    2 AA4 7 ARG C  45  LEU C  48 -1  O  LEU C  48   N  THR C  11
SHEET    3 AA4 7 THR C  19  GLY C  23  1  N  VAL C  20   O  LEU C  47
SHEET    4 AA4 7 CYS C  89  HIS C  94  1  O  ILE C  90   N  THR C  19
SHEET    5 AA4 7 PHE C 112  ILE C 118  1  O  ARG C 113   N  CYS C  89
SHEET    6 AA4 7 CYS C 209  LYS C 216  1  O  HIS C 210   N  ILE C 115
SHEET    7 AA4 7 SER C 236  GLU C 244  1  O  VAL C 237   N  ILE C 211
SHEET    1 AA5 7 THR D  11  GLY D  14  0
SHEET    2 AA5 7 ARG D  45  LEU D  48 -1  O  VAL D  46   N  LEU D  13
SHEET    3 AA5 7 THR D  19  LEU D  22  1  N  VAL D  20   O  LEU D  47
SHEET    4 AA5 7 CYS D  89  HIS D  94  1  O  VAL D  92   N  VAL D  21
SHEET    5 AA5 7 PHE D 112  ILE D 118  1  O  ARG D 113   N  CYS D  89
SHEET    6 AA5 7 CYS D 209  LYS D 216  1  O  ILE D 212   N  MET D 117
SHEET    7 AA5 7 SER D 236  GLU D 244  1  O  VAL D 237   N  ILE D 211
SHEET    1 AA6 7 THR E  11  GLY E  14  0
SHEET    2 AA6 7 ARG E  45  LEU E  48 -1  O  VAL E  46   N  LEU E  13
SHEET    3 AA6 7 THR E  19  GLY E  23  1  N  VAL E  20   O  LEU E  47
SHEET    4 AA6 7 CYS E  89  HIS E  94  1  O  VAL E  92   N  VAL E  21
SHEET    5 AA6 7 PHE E 112  ILE E 118  1  O  ARG E 113   N  CYS E  89
SHEET    6 AA6 7 CYS E 209  LYS E 216  1  O  HIS E 210   N  MET E 117
SHEET    7 AA6 7 SER E 236  GLU E 244  1  O  VAL E 237   N  ILE E 211
SITE     1 AC1 11 PHE A  26  ALA A  95  LEU A  96  VAL A 139
SITE     2 AC1 11 TYR A 143  TYR A 157  CYS A 190  ILE A 193
SITE     3 AC1 11 LEU A 219  HIS A 246  EDO A 307
SITE     1 AC2  3 ALA A 127  ASP A 128  ARG A 199
SITE     1 AC3  2 SER A 168  GLU A 169
SITE     1 AC4  2 ARG A 176  ASN A 180
SITE     1 AC5  2 ARG A  66  GLN A  75
SITE     1 AC6  4 LEU A  70  GLU A  71  TYR A 196  HOH A 408
SITE     1 AC7  4 PHE A 134  LEU A 142  LEU A 219  TZU A 301
SITE     1 AC8  1 PHE A  64
SITE     1 AC9  1 ARG A 262
SITE     1 AD1  9 GLY B  25  PHE B  26  ALA B  95  LEU B  96
SITE     2 AD1  9 VAL B 139  TYR B 143  MET B 146  CYS B 190
SITE     3 AD1  9 HIS B 246
SITE     1 AD2  3 ALA B 127  ASP B 128  ARG B 199
SITE     1 AD3  1 HIS B 229
SITE     1 AD4  2 PRO B 258  ARG B 262
SITE     1 AD5  3 SER B  69  LEU B  70  TYR B 196
SITE     1 AD6  1 ARG B 176
SITE     1 AD7 10 PHE C  26  HIS C  94  ALA C  95  LEU C  96
SITE     2 AD7 10 VAL C 124  VAL C 139  LEU C 142  TYR C 143
SITE     3 AD7 10 MET C 146  HIS C 246
SITE     1 AD8  1 ASN C 180
SITE     1 AD9  2 ASP C  63  PHE C  64
SITE     1 AE1  3 SER C  69  LEU C  70  LEU C 198
SITE     1 AE2  3 ASP C 128  ASP C 129  ARG C 199
SITE     1 AE3  8 HIS C  24  GLY C  25  GLY C  27  THR C  28
SITE     2 AE3  8 ASN C  51  LEU C  96  MET C 181  HOH C 406
SITE     1 AE4  8 PHE D  26  ALA D  95  LEU D  96  VAL D 139
SITE     2 AE4  8 TYR D 143  CYS D 190  ILE D 193  HIS D 246
SITE     1 AE5  3 HIS C  85  THR C  87  SER D   6
SITE     1 AE6  3 ALA D 127  ASP D 128  ARG D 199
SITE     1 AE7  3 ASP D  63  PHE D  64  GLU D  65
SITE     1 AE8  1 ARG D 176
SITE     1 AE9  8 PHE E  26  ALA E  95  LEU E  96  VAL E 139
SITE     2 AE9  8 TYR E 143  MET E 146  ILE E 193  HIS E 246
SITE     1 AF1  4 ALA E 127  ASP E 128  ARG E 199  HOH E 401
SITE     1 AF2  2 ARG E 176  ASN E 180
SITE     1 AF3  3 GLU E  71  TYR E 196  ASP E 197
SITE     1 AF4  1 GLN E  75
CRYST1   99.269  352.967  124.988  90.00  90.00  90.00 C 2 2 21     40
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      0.010074  0.000000  0.000000        0.00000
SCALE2      0.000000  0.002833  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008001        0.00000
TER    2082      ASP A 270
TER    4178      ASP B 270
TER    6274      ASP C 270
TER    8370      ASP D 270
TER   10458      ASP E 270
MASTER      999    0   33   74   37    0   40    610882    5  211  105
END