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PDBsum entry 4h3b

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Transferase PDB id
4h3b
Jmol
Contents
Protein chains
351 a.a.
Ligands
VAL-VAL-ARG-PRO-
GLY-SER-LEU-ASP-
LEU-PRO
×2
Waters ×445
HEADER    TRANSFERASE                             13-SEP-12   4H3B
TITLE     CRYSTAL STRUCTURE OF JNK3 IN COMPLEX WITH SAB PEPTIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 10;
COMPND   3 CHAIN: A, C;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 46-400);
COMPND   5 SYNONYM: MAP KINASE 10, MAPK 10, MAP KINASE P49 3F12, STRESS-
COMPND   6 ACTIVATED PROTEIN KINASE 1B, SAPK1B, STRESS-ACTIVATED PROTEIN KINASE
COMPND   7 JNK3, C-JUN N-TERMINAL KINASE 3;
COMPND   8 EC: 2.7.11.24;
COMPND   9 ENGINEERED: YES;
COMPND  10 MOL_ID: 2;
COMPND  11 MOLECULE: SH3 DOMAIN-BINDING PROTEIN 5;
COMPND  12 CHAIN: B, D;
COMPND  13 FRAGMENT: UNP RESIDUES 341-350;
COMPND  14 SYNONYM: SH3BP-5, SH3 DOMAIN-BINDING PROTEIN THAT PREFERENTIALLY
COMPND  15 ASSOCIATES WITH BTK;
COMPND  16 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: MAPK10, JNK3, JNK3A, PRKM10, SAPK1B;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 MOL_ID: 2;
SOURCE   9 SYNTHETIC: YES;
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  11 ORGANISM_COMMON: HUMAN;
SOURCE  12 ORGANISM_TAXID: 9606
KEYWDS    SH3BP-5, MAPK, KINASE, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.C.NWACHUKWU,J.D.LAUGHLIN,M.FIGUERA-LOSADA,L.CHERRY,K.W.NETTLES,
AUTHOR   2 P.V.LOGRASSO
REVDAT   3   26-DEC-12 4H3B    1       JRNL
REVDAT   2   28-NOV-12 4H3B    1       JRNL
REVDAT   1   21-NOV-12 4H3B    0
JRNL        AUTH   J.D.LAUGHLIN,J.C.NWACHUKWU,M.FIGUERA-LOSADA,L.CHERRY,
JRNL        AUTH 2 K.W.NETTLES,P.V.LOGRASSO
JRNL        TITL   STRUCTURAL MECHANISMS OF ALLOSTERY AND AUTOINHIBITION IN JNK
JRNL        TITL 2 FAMILY KINASES.
JRNL        REF    STRUCTURE                     V.  20  2174 2012
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   23142346
JRNL        DOI    10.1016/J.STR.2012.09.021
REMARK   2
REMARK   2 RESOLUTION.    2.08 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.08
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.70
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.110
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1
REMARK   3   NUMBER OF REFLECTIONS             : 57512
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) : 0.186
REMARK   3   FREE R VALUE                     : 0.235
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.790
REMARK   3   FREE R VALUE TEST SET COUNT      : 1027
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 36.7055 -  3.9775    0.99     8509   157  0.1623 0.2139
REMARK   3     2  3.9775 -  3.1576    0.99     8509   155  0.1703 0.2044
REMARK   3     3  3.1576 -  2.7587    0.98     8336   166  0.1911 0.2341
REMARK   3     4  2.7587 -  2.5065    0.95     8128   144  0.2149 0.2714
REMARK   3     5  2.5065 -  2.3269    0.92     7899   145  0.2151 0.3036
REMARK   3     6  2.3269 -  2.1897    0.90     7747   134  0.2167 0.2581
REMARK   3     7  2.1897 -  2.0800    0.86     7357   126  0.2653 0.3220
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.10
REMARK   3   SHRINKAGE RADIUS   : 0.86
REMARK   3   K_SOL              : 0.33
REMARK   3   B_SOL              : 44.60
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.620
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) : 0.10390
REMARK   3    B22 (A**2) : 0.10390
REMARK   3    B33 (A**2) : -0.20780
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : -0.00000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.008           6036
REMARK   3   ANGLE     :  1.123           8199
REMARK   3   CHIRALITY :  0.083            912
REMARK   3   PLANARITY :  0.005           1054
REMARK   3   DIHEDRAL  : 13.779           2306
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 30
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: (chain A and resid 45:68)
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6765  -6.6281  10.0817
REMARK   3    T TENSOR
REMARK   3      T11:   0.3197 T22:   0.3715
REMARK   3      T33:   0.2851 T12:   0.0339
REMARK   3      T13:  -0.0357 T23:   0.1079
REMARK   3    L TENSOR
REMARK   3      L11:   2.8828 L22:   1.4379
REMARK   3      L33:   3.0501 L12:   1.3918
REMARK   3      L13:   1.3351 L23:   1.2269
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1933 S12:  -0.2411 S13:  -0.4078
REMARK   3      S21:   0.2925 S22:  -0.0345 S23:   0.0401
REMARK   3      S31:   0.5057 S32:   0.2221 S33:   0.0922
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: (chain A and resid 69:87)
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5391   1.2413   9.6215
REMARK   3    T TENSOR
REMARK   3      T11:   0.2184 T22:   0.4410
REMARK   3      T33:   0.2092 T12:  -0.0129
REMARK   3      T13:  -0.0141 T23:   0.0836
REMARK   3    L TENSOR
REMARK   3      L11:   2.3936 L22:   1.6589
REMARK   3      L33:   3.3850 L12:   0.1675
REMARK   3      L13:   1.3381 L23:   0.5878
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0978 S12:   0.2584 S13:   0.0203
REMARK   3      S21:  -0.0987 S22:  -0.0852 S23:   0.1658
REMARK   3      S31:  -0.0874 S32:  -0.0493 S33:   0.1190
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: (chain A and resid 88:106)
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.9248   1.5459  -3.4658
REMARK   3    T TENSOR
REMARK   3      T11:   0.2568 T22:   0.4105
REMARK   3      T33:   0.2072 T12:  -0.0760
REMARK   3      T13:   0.0001 T23:   0.0278
REMARK   3    L TENSOR
REMARK   3      L11:   0.8008 L22:   0.4830
REMARK   3      L33:   5.6539 L12:  -0.3379
REMARK   3      L13:  -1.1951 L23:  -0.5907
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2081 S12:   0.0814 S13:  -0.2161
REMARK   3      S21:  -0.2809 S22:  -0.0107 S23:   0.0600
REMARK   3      S31:   0.2068 S32:  -0.3920 S33:   0.0726
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: (chain A and resid 107:115)
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8989  10.3317  -4.7921
REMARK   3    T TENSOR
REMARK   3      T11:   0.2328 T22:   0.3958
REMARK   3      T33:   0.2383 T12:   0.0793
REMARK   3      T13:   0.0015 T23:  -0.0067
REMARK   3    L TENSOR
REMARK   3      L11:   2.1490 L22:   6.1100
REMARK   3      L33:   4.6134 L12:  -0.0448
REMARK   3      L13:  -1.7983 L23:   1.1431
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1103 S12:  -0.0284 S13:   0.1333
REMARK   3      S21:  -0.1269 S22:   0.0866 S23:   0.2785
REMARK   3      S31:  -0.0727 S32:  -0.2420 S33:   0.0322
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: (chain A and resid 116:135)
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5334   9.4162   4.1334
REMARK   3    T TENSOR
REMARK   3      T11:   0.2165 T22:   0.4439
REMARK   3      T33:   0.2527 T12:   0.0840
REMARK   3      T13:  -0.0042 T23:   0.0015
REMARK   3    L TENSOR
REMARK   3      L11:   0.7066 L22:   2.0995
REMARK   3      L33:   0.5589 L12:  -0.4047
REMARK   3      L13:   0.0001 L23:   0.0061
REMARK   3    S TENSOR
REMARK   3      S11:   0.0486 S12:  -0.0086 S13:   0.0644
REMARK   3      S21:  -0.1954 S22:  -0.0874 S23:  -0.1625
REMARK   3      S31:   0.0828 S32:   0.2064 S33:   0.0187
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: (chain A and resid 136:148)
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6119  -0.6413   0.4635
REMARK   3    T TENSOR
REMARK   3      T11:   0.2033 T22:   0.3522
REMARK   3      T33:   0.2144 T12:   0.0252
REMARK   3      T13:  -0.0175 T23:   0.0611
REMARK   3    L TENSOR
REMARK   3      L11:   3.5657 L22:   2.3548
REMARK   3      L33:   4.3864 L12:  -0.7406
REMARK   3      L13:  -2.1649 L23:   1.1285
REMARK   3    S TENSOR
REMARK   3      S11:   0.0148 S12:   0.0831 S13:  -0.0474
REMARK   3      S21:  -0.2823 S22:  -0.0062 S23:  -0.0843
REMARK   3      S31:   0.1806 S32:   0.1079 S33:  -0.0197
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: (chain A and resid 149:203)
REMARK   3    ORIGIN FOR THE GROUP (A): -12.0728  21.6446   8.4421
REMARK   3    T TENSOR
REMARK   3      T11:   0.2147 T22:   0.4730
REMARK   3      T33:   0.2462 T12:   0.0568
REMARK   3      T13:   0.0203 T23:  -0.0123
REMARK   3    L TENSOR
REMARK   3      L11:   1.1433 L22:   1.2043
REMARK   3      L33:   0.4474 L12:  -0.0882
REMARK   3      L13:   0.0125 L23:  -0.3052
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2027 S12:  -0.4763 S13:  -0.0720
REMARK   3      S21:   0.2524 S22:   0.1554 S23:   0.0301
REMARK   3      S31:  -0.2109 S32:  -0.3418 S33:   0.0506
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: (chain A and resid 204:221)
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2640  10.6507   0.1477
REMARK   3    T TENSOR
REMARK   3      T11:   0.4047 T22:   0.5067
REMARK   3      T33:   0.4917 T12:  -0.0485
REMARK   3      T13:   0.0027 T23:  -0.0126
REMARK   3    L TENSOR
REMARK   3      L11:   1.4626 L22:   2.6243
REMARK   3      L33:   0.0751 L12:   1.9122
REMARK   3      L13:   0.3292 L23:   0.4481
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1388 S12:   0.3002 S13:  -0.4343
REMARK   3      S21:  -0.2514 S22:   0.0141 S23:   0.3118
REMARK   3      S31:   0.4338 S32:  -0.3294 S33:   0.0445
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: (chain A and resid 222:257)
REMARK   3    ORIGIN FOR THE GROUP (A): -17.4510  23.7490  -4.0342
REMARK   3    T TENSOR
REMARK   3      T11:   0.1496 T22:   0.4479
REMARK   3      T33:   0.3041 T12:   0.0757
REMARK   3      T13:   0.0047 T23:   0.0228
REMARK   3    L TENSOR
REMARK   3      L11:   1.1352 L22:   0.8978
REMARK   3      L33:   1.6429 L12:   0.3095
REMARK   3      L13:  -0.6171 L23:   0.0364
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1228 S12:  -0.1772 S13:  -0.0269
REMARK   3      S21:   0.0290 S22:   0.1895 S23:   0.0393
REMARK   3      S31:  -0.0110 S32:  -0.4671 S33:  -0.0248
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: (chain A and resid 258:276)
REMARK   3    ORIGIN FOR THE GROUP (A): -28.0002  23.2809  -5.6730
REMARK   3    T TENSOR
REMARK   3      T11:   0.1232 T22:   0.8536
REMARK   3      T33:   0.2891 T12:   0.1381
REMARK   3      T13:   0.0190 T23:   0.0106
REMARK   3    L TENSOR
REMARK   3      L11:   0.3305 L22:   0.1870
REMARK   3      L33:   0.9090 L12:  -0.1281
REMARK   3      L13:   0.0885 L23:  -0.0642
REMARK   3    S TENSOR
REMARK   3      S11:   0.1244 S12:  -0.0491 S13:  -0.1627
REMARK   3      S21:  -0.0550 S22:   0.0253 S23:   0.1518
REMARK   3      S31:   0.0406 S32:  -0.2545 S33:   0.2330
REMARK   3   TLS GROUP : 11
REMARK   3    SELECTION: (chain A and resid 277:319)
REMARK   3    ORIGIN FOR THE GROUP (A): -26.7778  33.8538  -9.7219
REMARK   3    T TENSOR
REMARK   3      T11:   0.1237 T22:   1.0336
REMARK   3      T33:   0.3086 T12:   0.5673
REMARK   3      T13:   0.1235 T23:   0.0016
REMARK   3    L TENSOR
REMARK   3      L11:   0.1451 L22:   0.0708
REMARK   3      L33:   0.0503 L12:  -0.0620
REMARK   3      L13:  -0.0753 L23:   0.0179
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2133 S12:  -0.1461 S13:   0.1870
REMARK   3      S21:   0.1757 S22:   0.1442 S23:   0.0535
REMARK   3      S31:  -0.2687 S32:  -0.4015 S33:  -0.2950
REMARK   3   TLS GROUP : 12
REMARK   3    SELECTION: (chain A and resid 325:362)
REMARK   3    ORIGIN FOR THE GROUP (A): -15.1910  36.2024   5.4512
REMARK   3    T TENSOR
REMARK   3      T11:   0.4643 T22:   0.4425
REMARK   3      T33:   0.3787 T12:   0.2427
REMARK   3      T13:   0.0389 T23:  -0.0929
REMARK   3    L TENSOR
REMARK   3      L11:   0.9841 L22:   0.7165
REMARK   3      L33:   0.6630 L12:   0.1417
REMARK   3      L13:   0.3716 L23:   0.2004
REMARK   3    S TENSOR
REMARK   3      S11:   0.0011 S12:  -0.2168 S13:   0.4479
REMARK   3      S21:   0.2423 S22:   0.1080 S23:   0.2479
REMARK   3      S31:  -0.6409 S32:  -0.2880 S33:  -0.1474
REMARK   3   TLS GROUP : 13
REMARK   3    SELECTION: (chain A and resid 363:370)
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8490  31.5405  10.5409
REMARK   3    T TENSOR
REMARK   3      T11:   0.4331 T22:   0.4723
REMARK   3      T33:   0.4140 T12:  -0.0414
REMARK   3      T13:  -0.0801 T23:  -0.0770
REMARK   3    L TENSOR
REMARK   3      L11:   5.5548 L22:   5.8554
REMARK   3      L33:   5.2966 L12:  -0.5504
REMARK   3      L13:  -0.1399 L23:   1.6560
REMARK   3    S TENSOR
REMARK   3      S11:   0.1368 S12:   0.1628 S13:   0.2587
REMARK   3      S21:  -0.2110 S22:   0.0130 S23:  -0.1831
REMARK   3      S31:  -0.3469 S32:   0.0891 S33:  -0.1120
REMARK   3   TLS GROUP : 14
REMARK   3    SELECTION: (chain A and resid 371:382)
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6627  19.3761  -7.6136
REMARK   3    T TENSOR
REMARK   3      T11:   0.4182 T22:   0.6889
REMARK   3      T33:   0.4007 T12:  -0.0227
REMARK   3      T13:   0.0431 T23:  -0.0192
REMARK   3    L TENSOR
REMARK   3      L11:   2.4698 L22:   3.6612
REMARK   3      L33:   6.2260 L12:   0.0566
REMARK   3      L13:   0.0687 L23:   2.4499
REMARK   3    S TENSOR
REMARK   3      S11:   0.1580 S12:  -0.1040 S13:   0.1394
REMARK   3      S21:  -0.4360 S22:  -0.0040 S23:  -0.0286
REMARK   3      S31:   0.1861 S32:   0.1439 S33:  -0.0735
REMARK   3   TLS GROUP : 15
REMARK   3    SELECTION: (chain A and resid 383:400)
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2947   3.4761 -10.3739
REMARK   3    T TENSOR
REMARK   3      T11:   0.3022 T22:   0.4449
REMARK   3      T33:   0.2503 T12:  -0.0083
REMARK   3      T13:   0.0982 T23:  -0.0291
REMARK   3    L TENSOR
REMARK   3      L11:   3.3075 L22:   2.6583
REMARK   3      L33:   6.0877 L12:   0.0299
REMARK   3      L13:   0.9172 L23:  -0.1331
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3130 S12:  -0.0220 S13:   0.1104
REMARK   3      S21:  -0.1147 S22:   0.0562 S23:  -0.2540
REMARK   3      S31:  -0.0605 S32:   0.3318 S33:   0.1277
REMARK   3   TLS GROUP : 16
REMARK   3    SELECTION: (chain C and resid 45:68)
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.4517  44.8967 -10.5414
REMARK   3    T TENSOR
REMARK   3      T11:   0.3434 T22:   0.3584
REMARK   3      T33:   0.2788 T12:   0.0385
REMARK   3      T13:  -0.0982 T23:  -0.0359
REMARK   3    L TENSOR
REMARK   3      L11:   0.7295 L22:   3.0749
REMARK   3      L33:   3.2043 L12:   0.6234
REMARK   3      L13:   0.0554 L23:  -1.6165
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0805 S12:   0.3052 S13:  -0.1459
REMARK   3      S21:  -0.1577 S22:  -0.0821 S23:   0.3333
REMARK   3      S31:   0.1157 S32:  -0.5975 S33:   0.0918
REMARK   3   TLS GROUP : 17
REMARK   3    SELECTION: (chain C and resid 69:87)
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8538  44.6481 -10.1584
REMARK   3    T TENSOR
REMARK   3      T11:   0.3750 T22:   0.2762
REMARK   3      T33:   0.2182 T12:   0.0995
REMARK   3      T13:  -0.0949 T23:  -0.0363
REMARK   3    L TENSOR
REMARK   3      L11:   1.6479 L22:   2.3334
REMARK   3      L33:   2.9949 L12:  -0.2988
REMARK   3      L13:   0.1750 L23:  -1.2471
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1810 S12:  -0.1565 S13:  -0.0958
REMARK   3      S21:   0.2179 S22:  -0.0291 S23:  -0.0484
REMARK   3      S31:  -0.0153 S32:   0.0228 S33:   0.1194
REMARK   3   TLS GROUP : 18
REMARK   3    SELECTION: (chain C and resid 88:105)
REMARK   3    ORIGIN FOR THE GROUP (A):   2.5329  46.6568   2.3391
REMARK   3    T TENSOR
REMARK   3      T11:   0.4547 T22:   0.2091
REMARK   3      T33:   0.1912 T12:   0.0308
REMARK   3      T13:  -0.0162 T23:  -0.0198
REMARK   3    L TENSOR
REMARK   3      L11:   0.5853 L22:   0.3997
REMARK   3      L33:   4.6973 L12:  -0.2801
REMARK   3      L13:   0.1931 L23:   0.9558
REMARK   3    S TENSOR
REMARK   3      S11:   0.0360 S12:  -0.1052 S13:  -0.1484
REMARK   3      S21:   0.2574 S22:  -0.1787 S23:   0.1397
REMARK   3      S31:   0.4300 S32:  -0.0081 S33:   0.0321
REMARK   3   TLS GROUP : 19
REMARK   3    SELECTION: (chain C and resid 106:125)
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4254  56.5073  -0.0062
REMARK   3    T TENSOR
REMARK   3      T11:   0.3093 T22:   0.3227
REMARK   3      T33:   0.2492 T12:   0.1098
REMARK   3      T13:  -0.0122 T23:   0.0093
REMARK   3    L TENSOR
REMARK   3      L11:   2.7323 L22:   0.3801
REMARK   3      L33:   2.8347 L12:   0.1699
REMARK   3      L13:  -2.4282 L23:   0.3624
REMARK   3    S TENSOR
REMARK   3      S11:   0.0890 S12:  -0.0619 S13:  -0.0864
REMARK   3      S21:   0.0469 S22:  -0.1352 S23:  -0.0250
REMARK   3      S31:   0.0158 S32:  -0.0084 S33:   0.0404
REMARK   3   TLS GROUP : 20
REMARK   3    SELECTION: (chain C and resid 126:148)
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.6516  51.8508  -1.8038
REMARK   3    T TENSOR
REMARK   3      T11:   0.2868 T22:   0.3192
REMARK   3      T33:   0.2239 T12:   0.0826
REMARK   3      T13:  -0.0285 T23:  -0.0208
REMARK   3    L TENSOR
REMARK   3      L11:   1.2212 L22:   2.0975
REMARK   3      L33:   2.2323 L12:  -0.2111
REMARK   3      L13:  -0.0651 L23:   0.1916
REMARK   3    S TENSOR
REMARK   3      S11:   0.1647 S12:  -0.2097 S13:   0.2438
REMARK   3      S21:   0.1344 S22:  -0.0184 S23:   0.1599
REMARK   3      S31:  -0.1556 S32:  -0.4347 S33:  -0.0517
REMARK   3   TLS GROUP : 21
REMARK   3    SELECTION: (chain C and resid 149:203)
REMARK   3    ORIGIN FOR THE GROUP (A):  24.8806  48.7125  -9.2561
REMARK   3    T TENSOR
REMARK   3      T11:   0.3448 T22:   0.3348
REMARK   3      T33:   0.2417 T12:   0.1456
REMARK   3      T13:   0.0179 T23:  -0.0167
REMARK   3    L TENSOR
REMARK   3      L11:   0.8918 L22:   1.2479
REMARK   3      L33:   0.2375 L12:   0.0725
REMARK   3      L13:   0.3179 L23:  -0.0240
REMARK   3    S TENSOR
REMARK   3      S11:   0.1580 S12:   0.4418 S13:  -0.0585
REMARK   3      S21:  -0.2113 S22:  -0.1659 S23:   0.0436
REMARK   3      S31:   0.2369 S32:   0.4130 S33:   0.0371
REMARK   3   TLS GROUP : 22
REMARK   3    SELECTION: (chain C and resid 204:221)
REMARK   3    ORIGIN FOR THE GROUP (A):  14.3548  45.2216  -0.6609
REMARK   3    T TENSOR
REMARK   3      T11:   0.4952 T22:   0.3884
REMARK   3      T33:   0.4896 T12:   0.0305
REMARK   3      T13:   0.0034 T23:  -0.0037
REMARK   3    L TENSOR
REMARK   3      L11:   0.9486 L22:   2.8253
REMARK   3      L33:   0.1012 L12:   1.6360
REMARK   3      L13:  -0.2698 L23:  -0.4666
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0068 S12:  -0.1591 S13:  -0.4205
REMARK   3      S21:   0.2856 S22:  -0.0731 S23:   0.1840
REMARK   3      S31:   0.4236 S32:  -0.2534 S33:   0.0239
REMARK   3   TLS GROUP : 23
REMARK   3    SELECTION: (chain C and resid 222:256)
REMARK   3    ORIGIN FOR THE GROUP (A):  29.1250  45.6714   3.8233
REMARK   3    T TENSOR
REMARK   3      T11:   0.3168 T22:   0.2851
REMARK   3      T33:   0.3029 T12:   0.1577
REMARK   3      T13:  -0.0097 T23:  -0.0214
REMARK   3    L TENSOR
REMARK   3      L11:   0.8558 L22:   1.3274
REMARK   3      L33:   1.7970 L12:  -0.1570
REMARK   3      L13:  -0.3269 L23:   0.0964
REMARK   3    S TENSOR
REMARK   3      S11:   0.1697 S12:   0.2040 S13:  -0.0055
REMARK   3      S21:  -0.0370 S22:  -0.1355 S23:  -0.0555
REMARK   3      S31:   0.4545 S32:   0.2370 S33:  -0.0205
REMARK   3   TLS GROUP : 24
REMARK   3    SELECTION: (chain C and resid 257:267)
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2863  35.6317  -0.4950
REMARK   3    T TENSOR
REMARK   3      T11:   0.6582 T22:   0.4646
REMARK   3      T33:   0.3164 T12:   0.3924
REMARK   3      T13:  -0.0175 T23:  -0.0915
REMARK   3    L TENSOR
REMARK   3      L11:   1.2861 L22:   0.4511
REMARK   3      L33:   2.8808 L12:  -0.6625
REMARK   3      L13:  -1.2004 L23:   1.0541
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0593 S12:  -0.2105 S13:  -0.0955
REMARK   3      S21:   0.1654 S22:   0.1703 S23:  -0.1223
REMARK   3      S31:   0.3457 S32:   0.1420 S33:   0.1773
REMARK   3   TLS GROUP : 25
REMARK   3    SELECTION: (chain C and resid 268:292)
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2192  42.9382  12.8219
REMARK   3    T TENSOR
REMARK   3      T11:   0.4437 T22:   0.5399
REMARK   3      T33:   0.3472 T12:   0.3992
REMARK   3      T13:   0.0155 T23:  -0.0470
REMARK   3    L TENSOR
REMARK   3      L11:   0.7066 L22:   0.4118
REMARK   3      L33:   0.1541 L12:  -0.3677
REMARK   3      L13:  -0.3184 L23:   0.1783
REMARK   3    S TENSOR
REMARK   3      S11:   0.1095 S12:   0.0544 S13:   0.1017
REMARK   3      S21:   0.0684 S22:   0.0047 S23:  -0.2088
REMARK   3      S31:   0.1035 S32:   0.2959 S33:  -0.0568
REMARK   3   TLS GROUP : 26
REMARK   3    SELECTION: (chain C and resid 293:314)
REMARK   3    ORIGIN FOR THE GROUP (A):  43.4782  40.1181  10.3514
REMARK   3    T TENSOR
REMARK   3      T11:   0.4935 T22:   0.8390
REMARK   3      T33:   0.3362 T12:   0.8070
REMARK   3      T13:   0.0361 T23:  -0.0570
REMARK   3    L TENSOR
REMARK   3      L11:   0.0014 L22:  -0.0040
REMARK   3      L33:  -0.0002 L12:  -0.0171
REMARK   3      L13:  -0.0027 L23:   0.0028
REMARK   3    S TENSOR
REMARK   3      S11:   0.0744 S12:   0.2430 S13:   0.0027
REMARK   3      S21:  -0.0289 S22:  -0.0951 S23:  -0.1321
REMARK   3      S31:   0.1671 S32:   0.2363 S33:  -0.0685
REMARK   3   TLS GROUP : 27
REMARK   3    SELECTION: (chain C and resid 315:354)
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0930  50.7009  -5.5628
REMARK   3    T TENSOR
REMARK   3      T11:   0.2466 T22:   0.6778
REMARK   3      T33:   0.3681 T12:   0.1412
REMARK   3      T13:   0.0913 T23:   0.0284
REMARK   3    L TENSOR
REMARK   3      L11:   0.9779 L22:   1.3185
REMARK   3      L33:   0.3102 L12:  -0.3773
REMARK   3      L13:  -0.5244 L23:   0.1177
REMARK   3    S TENSOR
REMARK   3      S11:   0.0949 S12:   0.2498 S13:   0.0208
REMARK   3      S21:  -0.2475 S22:  -0.0379 S23:  -0.4350
REMARK   3      S31:   0.0171 S32:   0.7246 S33:  -0.1993
REMARK   3   TLS GROUP : 28
REMARK   3    SELECTION: (chain C and resid 355:370)
REMARK   3    ORIGIN FOR THE GROUP (A):  32.0684  61.0617 -11.9322
REMARK   3    T TENSOR
REMARK   3      T11:   0.4468 T22:   0.6053
REMARK   3      T33:   0.3777 T12:   0.0403
REMARK   3      T13:   0.1001 T23:   0.1015
REMARK   3    L TENSOR
REMARK   3      L11:   2.9850 L22:   1.3498
REMARK   3      L33:   0.1172 L12:  -1.7145
REMARK   3      L13:   0.1822 L23:  -0.2965
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1174 S12:   0.0310 S13:   0.3488
REMARK   3      S21:  -0.0715 S22:   0.1932 S23:  -0.1334
REMARK   3      S31:  -0.2993 S32:   0.4178 S33:  -0.0560
REMARK   3   TLS GROUP : 29
REMARK   3    SELECTION: (chain C and resid 371:382)
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4181  62.5334   7.0721
REMARK   3    T TENSOR
REMARK   3      T11:   0.6021 T22:   0.4332
REMARK   3      T33:   0.4024 T12:   0.0881
REMARK   3      T13:   0.0337 T23:  -0.0239
REMARK   3    L TENSOR
REMARK   3      L11:   3.4483 L22:   2.2650
REMARK   3      L33:   5.0770 L12:   0.7415
REMARK   3      L13:  -1.7364 L23:  -0.6076
REMARK   3    S TENSOR
REMARK   3      S11:   0.2227 S12:  -0.4018 S13:   0.0771
REMARK   3      S21:  -0.0092 S22:  -0.0903 S23:  -0.0711
REMARK   3      S31:   0.0044 S32:  -0.2341 S33:  -0.0533
REMARK   3   TLS GROUP : 30
REMARK   3    SELECTION: (chain C and resid 383:400)
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.1379  57.7128   9.8362
REMARK   3    T TENSOR
REMARK   3      T11:   0.4261 T22:   0.3421
REMARK   3      T33:   0.2562 T12:   0.0497
REMARK   3      T13:   0.0562 T23:  -0.0707
REMARK   3    L TENSOR
REMARK   3      L11:   2.7178 L22:   3.4211
REMARK   3      L33:   6.7918 L12:  -0.4070
REMARK   3      L13:   0.6033 L23:  -1.3220
REMARK   3    S TENSOR
REMARK   3      S11:   0.0065 S12:   0.1646 S13:   0.2522
REMARK   3      S21:   0.0639 S22:  -0.3243 S23:   0.0269
REMARK   3      S31:  -0.3827 S32:  -0.1247 S33:   0.1823
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 4H3B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-12.
REMARK 100 THE RCSB ID CODE IS RCSB074965.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-JAN-11
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 5.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL11-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.17
REMARK 200  MONOCHROMATOR                  : SIDE SCATTERING BENT-CUBE I-BEAM
REMARK 200                                   SINGLE CRYSTAL, ASYMMETRIC CUT
REMARK 200                                   4.965 DEGREES
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73519
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.721
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.196
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 5.500
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 33.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK 200 STARTING MODEL: PDB ENTRY 1JNK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CHLORIDE, 0.1 M BIS-TRIS,
REMARK 280  28-31% PEG3350, PH 5.5, VAPOR DIFFUSION, TEMPERATURE 294.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.41667
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       84.83333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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: 1150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ALA A   320
REMARK 465     ASP A   321
REMARK 465     SER A   322
REMARK 465     GLU A   323
REMARK 465     HIS A   324
REMARK 465     ALA C   320
REMARK 465     ASP C   321
REMARK 465     SER C   322
REMARK 465     GLU C   323
REMARK 465     HIS C   324
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     LYS A 134    CG   CD   CE   NZ
REMARK 470     ARG A 212    CG   CD   NE   CZ   NH1  NH2
REMARK 470     THR A 213    OG1  CG2
REMARK 470     LYS A 260    CD   CE   NZ
REMARK 470     LYS A 326    CD   CE   NZ
REMARK 470     GLN A 379    CG   CD   OE1  NE2
REMARK 470     GLU A 382    CG   CD   OE1  OE2
REMARK 470     LYS C 134    CG   CD   CE   NZ
REMARK 470     ARG C 212    CG   CD   NE   CZ   NH1  NH2
REMARK 470     THR C 213    OG1  CG2
REMARK 470     LYS C 260    CD   CE   NZ
REMARK 470     LYS C 326    CD   CE   NZ
REMARK 470     GLN C 379    CG   CD   OE1  NE2
REMARK 470     GLU C 382    CG   CD   OE1  OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH C   623     O    HOH C   625              1.84
REMARK 500   O    HOH A   608     O    HOH A   629              1.88
REMARK 500   O    HOH A   690     O    HOH A   702              1.91
REMARK 500   O    HOH C   708     O    HOH C   712              1.92
REMARK 500   O    HOH C   696     O    HOH C   709              1.93
REMARK 500   O    HOH C   675     O    HOH C   689              1.94
REMARK 500   O    HOH D   405     O    HOH D   406              1.98
REMARK 500   O    HOH A   663     O    HOH A   675              1.99
REMARK 500   OD1  ASP A   141     O    HOH A   584              2.05
REMARK 500   O    HOH C   631     O    HOH C   632              2.05
REMARK 500   OE1  GLU A   392     O    HOH A   658              2.09
REMARK 500   OE1  GLN A   102     O    HOH A   596              2.09
REMARK 500   O    HOH A   617     O    HOH A   709              2.09
REMARK 500   O    HOH C   695     O    HOH C   697              2.10
REMARK 500   N    ARG B   343     O    HOH B   403              2.12
REMARK 500   O    HOH C   673     O    HOH C   692              2.12
REMARK 500   O    HOH A   655     O    HOH A   661              2.13
REMARK 500   OE2  GLU C   111     O    HOH C   716              2.13
REMARK 500   OE1  GLN C    75     O    HOH C   682              2.13
REMARK 500   NH1  ARG A    97     OE1  GLN A   100              2.14
REMARK 500   O    HOH C   638     O    HOH C   687              2.15
REMARK 500   O    HOH C   538     O    HOH C   702              2.15
REMARK 500   O    HOH A   558     O    HOH A   686              2.16
REMARK 500   O    HOH C   680     O    HOH C   713              2.16
REMARK 500   O    HOH C   581     O    HOH C   679              2.17
REMARK 500   OD1  ASN C    66     O    HOH C   641              2.18
REMARK 500   O    HOH C   558     O    HOH C   670              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A 119       85.39   -155.78
REMARK 500    GLN A 140      -39.79   -139.13
REMARK 500    ARG A 188      -32.39     76.60
REMARK 500    ARG A 212       63.10    -65.86
REMARK 500    THR A 213      -35.35   -170.82
REMARK 500    SER A 316      -34.49    -36.99
REMARK 500    ASN C 119       85.75   -153.19
REMARK 500    GLN C 140      -36.63   -140.91
REMARK 500    ARG C 188      -31.66     77.50
REMARK 500    THR C 213      -31.10   -157.61
REMARK 500    LEU C 327       86.55     -4.43
REMARK 500    LYS C 328      -40.48    171.00
REMARK 500    VAL D 342      105.60     43.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4H36   RELATED DB: PDB
REMARK 900 JNK3 COMPLEXED WITH ATF2 PEPTIDE
REMARK 900 RELATED ID: 4H39   RELATED DB: PDB
REMARK 900 JNK3 COMPLEXED WITH JIP1 PEPTIDE
DBREF  4H3B A   46   400  UNP    P53779   MK10_HUMAN      46    400
DBREF  4H3B B  341   350  UNP    O60239   3BP5_HUMAN     341    350
DBREF  4H3B C   46   400  UNP    P53779   MK10_HUMAN      46    400
DBREF  4H3B D  341   350  UNP    O60239   3BP5_HUMAN     341    350
SEQADV 4H3B ALA A   45  UNP  P53779              EXPRESSION TAG
SEQADV 4H3B ALA C   45  UNP  P53779              EXPRESSION TAG
SEQRES   1 A  356  ALA ASN GLN PHE TYR SER VAL GLU VAL GLY ASP SER THR
SEQRES   2 A  356  PHE THR VAL LEU LYS ARG TYR GLN ASN LEU LYS PRO ILE
SEQRES   3 A  356  GLY SER GLY ALA GLN GLY ILE VAL CYS ALA ALA TYR ASP
SEQRES   4 A  356  ALA VAL LEU ASP ARG ASN VAL ALA ILE LYS LYS LEU SER
SEQRES   5 A  356  ARG PRO PHE GLN ASN GLN THR HIS ALA LYS ARG ALA TYR
SEQRES   6 A  356  ARG GLU LEU VAL LEU MET LYS CYS VAL ASN HIS LYS ASN
SEQRES   7 A  356  ILE ILE SER LEU LEU ASN VAL PHE THR PRO GLN LYS THR
SEQRES   8 A  356  LEU GLU GLU PHE GLN ASP VAL TYR LEU VAL MET GLU LEU
SEQRES   9 A  356  MET ASP ALA ASN LEU CYS GLN VAL ILE GLN MET GLU LEU
SEQRES  10 A  356  ASP HIS GLU ARG MET SER TYR LEU LEU TYR GLN MET LEU
SEQRES  11 A  356  CYS GLY ILE LYS HIS LEU HIS SER ALA GLY ILE ILE HIS
SEQRES  12 A  356  ARG ASP LEU LYS PRO SER ASN ILE VAL VAL LYS SER ASP
SEQRES  13 A  356  CYS THR LEU LYS ILE LEU ASP PHE GLY LEU ALA ARG THR
SEQRES  14 A  356  ALA GLY THR SER PHE MET MET THR PRO TYR VAL VAL THR
SEQRES  15 A  356  ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU GLY MET GLY
SEQRES  16 A  356  TYR LYS GLU ASN VAL ASP ILE TRP SER VAL GLY CYS ILE
SEQRES  17 A  356  MET GLY GLU MET VAL ARG HIS LYS ILE LEU PHE PRO GLY
SEQRES  18 A  356  ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL ILE GLU GLN
SEQRES  19 A  356  LEU GLY THR PRO CYS PRO GLU PHE MET LYS LYS LEU GLN
SEQRES  20 A  356  PRO THR VAL ARG ASN TYR VAL GLU ASN ARG PRO LYS TYR
SEQRES  21 A  356  ALA GLY LEU THR PHE PRO LYS LEU PHE PRO ASP SER LEU
SEQRES  22 A  356  PHE PRO ALA ASP SER GLU HIS ASN LYS LEU LYS ALA SER
SEQRES  23 A  356  GLN ALA ARG ASP LEU LEU SER LYS MET LEU VAL ILE ASP
SEQRES  24 A  356  PRO ALA LYS ARG ILE SER VAL ASP ASP ALA LEU GLN HIS
SEQRES  25 A  356  PRO TYR ILE ASN VAL TRP TYR ASP PRO ALA GLU VAL GLU
SEQRES  26 A  356  ALA PRO PRO PRO GLN ILE TYR ASP LYS GLN LEU ASP GLU
SEQRES  27 A  356  ARG GLU HIS THR ILE GLU GLU TRP LYS GLU LEU ILE TYR
SEQRES  28 A  356  LYS GLU VAL MET ASN
SEQRES   1 B   10  VAL VAL ARG PRO GLY SER LEU ASP LEU PRO
SEQRES   1 C  356  ALA ASN GLN PHE TYR SER VAL GLU VAL GLY ASP SER THR
SEQRES   2 C  356  PHE THR VAL LEU LYS ARG TYR GLN ASN LEU LYS PRO ILE
SEQRES   3 C  356  GLY SER GLY ALA GLN GLY ILE VAL CYS ALA ALA TYR ASP
SEQRES   4 C  356  ALA VAL LEU ASP ARG ASN VAL ALA ILE LYS LYS LEU SER
SEQRES   5 C  356  ARG PRO PHE GLN ASN GLN THR HIS ALA LYS ARG ALA TYR
SEQRES   6 C  356  ARG GLU LEU VAL LEU MET LYS CYS VAL ASN HIS LYS ASN
SEQRES   7 C  356  ILE ILE SER LEU LEU ASN VAL PHE THR PRO GLN LYS THR
SEQRES   8 C  356  LEU GLU GLU PHE GLN ASP VAL TYR LEU VAL MET GLU LEU
SEQRES   9 C  356  MET ASP ALA ASN LEU CYS GLN VAL ILE GLN MET GLU LEU
SEQRES  10 C  356  ASP HIS GLU ARG MET SER TYR LEU LEU TYR GLN MET LEU
SEQRES  11 C  356  CYS GLY ILE LYS HIS LEU HIS SER ALA GLY ILE ILE HIS
SEQRES  12 C  356  ARG ASP LEU LYS PRO SER ASN ILE VAL VAL LYS SER ASP
SEQRES  13 C  356  CYS THR LEU LYS ILE LEU ASP PHE GLY LEU ALA ARG THR
SEQRES  14 C  356  ALA GLY THR SER PHE MET MET THR PRO TYR VAL VAL THR
SEQRES  15 C  356  ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU GLY MET GLY
SEQRES  16 C  356  TYR LYS GLU ASN VAL ASP ILE TRP SER VAL GLY CYS ILE
SEQRES  17 C  356  MET GLY GLU MET VAL ARG HIS LYS ILE LEU PHE PRO GLY
SEQRES  18 C  356  ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL ILE GLU GLN
SEQRES  19 C  356  LEU GLY THR PRO CYS PRO GLU PHE MET LYS LYS LEU GLN
SEQRES  20 C  356  PRO THR VAL ARG ASN TYR VAL GLU ASN ARG PRO LYS TYR
SEQRES  21 C  356  ALA GLY LEU THR PHE PRO LYS LEU PHE PRO ASP SER LEU
SEQRES  22 C  356  PHE PRO ALA ASP SER GLU HIS ASN LYS LEU LYS ALA SER
SEQRES  23 C  356  GLN ALA ARG ASP LEU LEU SER LYS MET LEU VAL ILE ASP
SEQRES  24 C  356  PRO ALA LYS ARG ILE SER VAL ASP ASP ALA LEU GLN HIS
SEQRES  25 C  356  PRO TYR ILE ASN VAL TRP TYR ASP PRO ALA GLU VAL GLU
SEQRES  26 C  356  ALA PRO PRO PRO GLN ILE TYR ASP LYS GLN LEU ASP GLU
SEQRES  27 C  356  ARG GLU HIS THR ILE GLU GLU TRP LYS GLU LEU ILE TYR
SEQRES  28 C  356  LYS GLU VAL MET ASN
SEQRES   1 D   10  VAL VAL ARG PRO GLY SER LEU ASP LEU PRO
FORMUL   5  HOH   *445(H2 O)
HELIX    1   1 ASN A  101  CYS A  117  1                                  17
HELIX    2   2 LEU A  153  MET A  159  1                                   7
HELIX    3   3 ASP A  162  ALA A  183  1                                  22
HELIX    4   4 LYS A  191  SER A  193  5                                   3
HELIX    5   5 GLY A  215  MET A  220  1                                   6
HELIX    6   6 THR A  226  ARG A  230  5                                   5
HELIX    7   7 ALA A  231  LEU A  236  1                                   6
HELIX    8   8 ASN A  243  HIS A  259  1                                  17
HELIX    9   9 ASP A  267  GLY A  280  1                                  14
HELIX   10  10 CYS A  283  LYS A  288  1                                   6
HELIX   11  11 GLN A  291  ASN A  300  1                                  10
HELIX   12  12 THR A  308  PHE A  313  1                                   6
HELIX   13  13 PRO A  314  PHE A  318  5                                   5
HELIX   14  14 LYS A  326  LEU A  340  1                                  15
HELIX   15  15 ASP A  343  ARG A  347  5                                   5
HELIX   16  16 SER A  349  HIS A  356  1                                   8
HELIX   17  17 HIS A  356  VAL A  361  1                                   6
HELIX   18  18 ASP A  364  GLU A  369  1                                   6
HELIX   19  19 ASP A  377  ASP A  381  5                                   5
HELIX   20  20 THR A  386  ASN A  400  1                                  15
HELIX   21  21 ASN C  101  CYS C  117  1                                  17
HELIX   22  22 LEU C  153  MET C  159  1                                   7
HELIX   23  23 ASP C  162  ALA C  183  1                                  22
HELIX   24  24 LYS C  191  SER C  193  5                                   3
HELIX   25  25 GLY C  215  MET C  220  1                                   6
HELIX   26  26 THR C  226  ARG C  230  5                                   5
HELIX   27  27 ALA C  231  LEU C  236  1                                   6
HELIX   28  28 ASN C  243  HIS C  259  1                                  17
HELIX   29  29 ASP C  267  GLY C  280  1                                  14
HELIX   30  30 CYS C  283  LYS C  288  1                                   6
HELIX   31  31 GLN C  291  ASN C  300  1                                  10
HELIX   32  32 THR C  308  PHE C  313  1                                   6
HELIX   33  33 PRO C  314  PHE C  318  5                                   5
HELIX   34  34 LYS C  328  LEU C  340  1                                  13
HELIX   35  35 ASP C  343  ARG C  347  5                                   5
HELIX   36  36 SER C  349  HIS C  356  1                                   8
HELIX   37  37 HIS C  356  VAL C  361  1                                   6
HELIX   38  38 ASP C  364  GLU C  369  1                                   6
HELIX   39  39 ASP C  377  ASP C  381  5                                   5
HELIX   40  40 THR C  386  ASN C  400  1                                  15
SHEET    1   A 2 PHE A  48  VAL A  53  0
SHEET    2   A 2 SER A  56  LEU A  61 -1  O  PHE A  58   N  VAL A  51
SHEET    1   B 5 TYR A  64  GLY A  73  0
SHEET    2   B 5 GLY A  76  ASP A  83 -1  O  TYR A  82   N  GLN A  65
SHEET    3   B 5 ARG A  88  LEU A  95 -1  O  ILE A  92   N  CYS A  79
SHEET    4   B 5 TYR A 143  GLU A 147 -1  O  LEU A 144   N  LYS A  93
SHEET    5   B 5 LEU A 126  PHE A 130 -1  N  ASN A 128   O  VAL A 145
SHEET    1   C 3 ALA A 151  ASN A 152  0
SHEET    2   C 3 ILE A 195  VAL A 197 -1  O  VAL A 197   N  ALA A 151
SHEET    3   C 3 LEU A 203  ILE A 205 -1  O  LYS A 204   N  VAL A 196
SHEET    1   D 2 PHE C  48  VAL C  53  0
SHEET    2   D 2 SER C  56  LEU C  61 -1  O  PHE C  58   N  VAL C  51
SHEET    1   E 5 TYR C  64  GLY C  73  0
SHEET    2   E 5 GLY C  76  ASP C  83 -1  O  TYR C  82   N  GLN C  65
SHEET    3   E 5 ARG C  88  LEU C  95 -1  O  ILE C  92   N  CYS C  79
SHEET    4   E 5 TYR C 143  GLU C 147 -1  O  LEU C 144   N  LYS C  93
SHEET    5   E 5 LEU C 126  PHE C 130 -1  N  ASN C 128   O  VAL C 145
SHEET    1   F 3 ALA C 151  ASN C 152  0
SHEET    2   F 3 ILE C 195  VAL C 197 -1  O  VAL C 197   N  ALA C 151
SHEET    3   F 3 LEU C 203  ILE C 205 -1  O  LYS C 204   N  VAL C 196
CISPEP   1 THR A  221    PRO A  222          0        -0.42
CISPEP   2 THR C  221    PRO C  222          0        -3.70
CISPEP   3 LYS C  326    LEU C  327          0         1.22
CRYST1   84.520   84.520  127.250  90.00  90.00 120.00 P 31          6
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      0.011832  0.006831  0.000000        0.00000
SCALE2      0.000000  0.013662  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007859        0.00000
      
PROCHECK
Go to PROCHECK summary
 References