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PDBsum entry 2xs0

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Transcription PDB id
2xs0
Jmol
Contents
Protein chains
346 a.a.
12 a.a.
Ligands
ANP
Waters ×18
HEADER    TRANSCRIPTION                           24-SEP-10   2XS0
TITLE     LINEAR BINDING MOTIFS FOR JNK AND FOR CALCINEURIN ANTAGONISTICALLY
TITLE    2 CONTROL THE NUCLEAR SHUTTLING OF NFAT4
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: MAP KINASE 8, MAPK 8, STRESS-ACTIVATED PROTEIN KINASE
COMPND   5  JNK1, JNK1, C-JUN N-TERMINAL KINASE 1, JNK-46, STRESS-ACTIVATED
COMPND   6  PROTEIN KINASE 1;
COMPND   7 EC: 2.7.11.24;
COMPND   8 ENGINEERED: YES;
COMPND   9 MUTATION: YES;
COMPND  10 MOL_ID: 2;
COMPND  11 MOLECULE: NUCLEAR FACTOR OF ACTIVATED T-CELLS, CYTOPLASMIC 3;
COMPND  12 CHAIN: B;
COMPND  13 FRAGMENT: FRAGMENT OF NFAT4, RESIDUES 141-154;
COMPND  14 SYNONYM: NF-ATC3, T-CELL TRANSCRIPTION FACTOR NFAT4, NFATX
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET DERIVATIVE;
SOURCE  11 MOL_ID: 2;
SOURCE  12 SYNTHETIC: YES;
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  14 ORGANISM_COMMON: HUMAN;
SOURCE  15 ORGANISM_TAXID: 9606
KEYWDS    TRANSCRIPTION, TRANSFERASE, MAPK SIGNALING PATHWAYS, LINEAR BINDING
KEYWDS   2 MOTIFS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.BARKAI,I.TOEOROE,A.GARAI,A.REMENYI
REVDAT   2   24-OCT-12 2XS0    1       JRNL
REVDAT   1   28-SEP-11 2XS0    0
JRNL        AUTH   A.GARAI,A.ZEKE,G.GOGL,I.TORO,F.FORDOS,H.BLANKENBURG,
JRNL        AUTH 2 T.BARKAI,J.VARGA,A.ALEXA,D.EMIG,M.ALBRECHT,A.REMENYI
JRNL        TITL   SPECIFICITY OF LINEAR MOTIFS THAT BIND TO A COMMON MITOGEN-
JRNL        TITL 2 ACTIVATED PROTEIN KINASE DOCKING GROOVE.
JRNL        REF    SCI. SIGNAL                   V.   5    74 2012
JRNL        REFN                   ESSN 1937-9145
JRNL        PMID   23047924
JRNL        DOI    10.1126/SCISIGNAL.2003004
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.883
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.36
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.83
REMARK   3   NUMBER OF REFLECTIONS             : 13785
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1938
REMARK   3   R VALUE            (WORKING SET) : 0.1879
REMARK   3   FREE R VALUE                     : 0.2457
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.00
REMARK   3   FREE R VALUE TEST SET COUNT      : 1379
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 30.8849 -  5.5916    0.99     1315   144  0.1665 0.2164
REMARK   3     2  5.5916 -  4.4424    1.00     1258   138  0.1601 0.2111
REMARK   3     3  4.4424 -  3.8821    1.00     1239   145  0.1579 0.2213
REMARK   3     4  3.8821 -  3.5277    1.00     1242   137  0.1837 0.2311
REMARK   3     5  3.5277 -  3.2752    1.00     1231   135  0.2122 0.2861
REMARK   3     6  3.2752 -  3.0823    1.00     1215   141  0.2221 0.2631
REMARK   3     7  3.0823 -  2.9280    1.00     1246   133  0.2375 0.3726
REMARK   3     8  2.9280 -  2.8006    1.00     1216   136  0.2628 0.3079
REMARK   3     9  2.8006 -  2.6929    1.00     1217   130  0.2840 0.3355
REMARK   3    10  2.6929 -  2.6000    1.00     1227   140  0.3207 0.3705
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.30
REMARK   3   SHRINKAGE RADIUS   : 1.10
REMARK   3   K_SOL              : 0.327
REMARK   3   B_SOL              : 40.000
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.39
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.67
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 67.47
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.59
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 32.5003
REMARK   3    B22 (A**2) : 17.0220
REMARK   3    B33 (A**2) : 13.6641
REMARK   3    B12 (A**2) : 0.0000
REMARK   3    B13 (A**2) : 0.0000
REMARK   3    B23 (A**2) : 0.0000
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      :  0.004           3000
REMARK   3   ANGLE     :  0.811           4063
REMARK   3   CHIRALITY :  0.057            444
REMARK   3   PLANARITY :  0.003            517
REMARK   3   DIHEDRAL  : 18.692           1175
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 13
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: (CHAIN A AND RESID 5:9)
REMARK   3    ORIGIN FOR THE GROUP (A): -52.2801  19.1703  -2.7399
REMARK   3    T TENSOR
REMARK   3      T11:   0.3716 T22:   0.5139
REMARK   3      T33:   0.5467 T12:   0.2171
REMARK   3      T13:  -0.0461 T23:  -0.2280
REMARK   3    L TENSOR
REMARK   3      L11:   3.1651 L22:   6.9771
REMARK   3      L33:   1.0764 L12:  -4.3751
REMARK   3      L13:   1.8423 L23:  -2.6075
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0292 S12:   0.3803 S13:  -0.1910
REMARK   3      S21:   0.0236 S22:  -0.2647 S23:   0.2835
REMARK   3      S31:  -0.3012 S32:  -0.5934 S33:   0.2867
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: (CHAIN A AND RESID 10:39)
REMARK   3    ORIGIN FOR THE GROUP (A): -37.1442  14.4014  -3.9582
REMARK   3    T TENSOR
REMARK   3      T11:   0.2543 T22:  -0.0029
REMARK   3      T33:   0.2566 T12:   0.0774
REMARK   3      T13:  -0.0627 T23:  -0.0396
REMARK   3    L TENSOR
REMARK   3      L11:   0.1955 L22:   0.1587
REMARK   3      L33:   0.0797 L12:   0.1007
REMARK   3      L13:  -0.0468 L23:  -0.1036
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0712 S12:   0.0727 S13:  -0.0515
REMARK   3      S21:  -0.0426 S22:   0.0694 S23:   0.0159
REMARK   3      S31:   0.0755 S32:   0.0594 S33:   0.0175
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: (CHAIN A AND RESID 40:71)
REMARK   3    ORIGIN FOR THE GROUP (A): -38.0118  11.8282   5.8017
REMARK   3    T TENSOR
REMARK   3      T11:   0.1961 T22:   0.0084
REMARK   3      T33:   0.3439 T12:  -0.0733
REMARK   3      T13:   0.1510 T23:   0.0552
REMARK   3    L TENSOR
REMARK   3      L11:   0.0796 L22:   0.0014
REMARK   3      L33:   0.0955 L12:   0.0017
REMARK   3      L13:  -0.0175 L23:  -0.0023
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1166 S12:  -0.0582 S13:   0.0463
REMARK   3      S21:   0.0455 S22:  -0.0862 S23:  -0.0171
REMARK   3      S31:   0.1035 S32:   0.0378 S33:  -0.0424
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: (CHAIN A AND RESID 72:93)
REMARK   3    ORIGIN FOR THE GROUP (A): -35.8611  16.4008  14.7493
REMARK   3    T TENSOR
REMARK   3      T11:   0.1181 T22:   0.0158
REMARK   3      T33:   0.0849 T12:   0.0843
REMARK   3      T13:   0.2441 T23:  -0.0999
REMARK   3    L TENSOR
REMARK   3      L11:   0.0377 L22:   0.0247
REMARK   3      L33:   0.0653 L12:  -0.0228
REMARK   3      L13:  -0.0494 L23:   0.0311
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0247 S12:   0.0549 S13:  -0.0272
REMARK   3      S21:   0.0133 S22:  -0.0175 S23:   0.0060
REMARK   3      S31:   0.0093 S32:  -0.0491 S33:  -0.0187
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: (CHAIN A AND RESID 94:123)
REMARK   3    ORIGIN FOR THE GROUP (A): -32.2709  12.6813   4.6885
REMARK   3    T TENSOR
REMARK   3      T11:   0.1473 T22:   0.1108
REMARK   3      T33:   0.1663 T12:  -0.0250
REMARK   3      T13:   0.0785 T23:  -0.0448
REMARK   3    L TENSOR
REMARK   3      L11:   0.0068 L22:   0.1746
REMARK   3      L33:   0.3374 L12:   0.0042
REMARK   3      L13:  -0.0455 L23:  -0.0383
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0409 S12:  -0.0112 S13:  -0.0632
REMARK   3      S21:  -0.0766 S22:  -0.1161 S23:   0.0691
REMARK   3      S31:   0.0631 S32:   0.0690 S33:  -0.1095
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: (CHAIN A AND RESID 124:173)
REMARK   3    ORIGIN FOR THE GROUP (A): -21.2544  14.4245  17.2037
REMARK   3    T TENSOR
REMARK   3      T11:   0.0446 T22:   0.0818
REMARK   3      T33:  -0.1224 T12:   0.1114
REMARK   3      T13:   0.3102 T23:  -0.0525
REMARK   3    L TENSOR
REMARK   3      L11:   0.0058 L22:   0.1201
REMARK   3      L33:   0.0712 L12:  -0.0010
REMARK   3      L13:   0.0175 L23:   0.0109
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0682 S12:   0.0076 S13:  -0.0517
REMARK   3      S21:   0.1261 S22:  -0.0415 S23:   0.0384
REMARK   3      S31:   0.1111 S32:   0.1060 S33:  -0.0799
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: (CHAIN A AND RESID 188:191)
REMARK   3    ORIGIN FOR THE GROUP (A): -18.7042  -1.0972  12.6987
REMARK   3    T TENSOR
REMARK   3      T11:   0.6143 T22:   0.3130
REMARK   3      T33:   0.3935 T12:   0.2169
REMARK   3      T13:   0.0583 T23:   0.1131
REMARK   3    L TENSOR
REMARK   3      L11:   0.9723 L22:   2.4041
REMARK   3      L33:   0.2076 L12:   0.3917
REMARK   3      L13:  -0.2606 L23:   0.4505
REMARK   3    S TENSOR
REMARK   3      S11:   0.1550 S12:   0.0746 S13:  -0.4553
REMARK   3      S21:  -0.4046 S22:  -0.0501 S23:   0.5294
REMARK   3      S31:   0.4963 S32:   0.2053 S33:  -0.1336
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: (CHAIN A AND RESID 192:217)
REMARK   3    ORIGIN FOR THE GROUP (A): -18.3522   1.7786  22.9926
REMARK   3    T TENSOR
REMARK   3      T11:   0.2826 T22:   0.2572
REMARK   3      T33:   0.1993 T12:   0.2408
REMARK   3      T13:   0.0964 T23:   0.2391
REMARK   3    L TENSOR
REMARK   3      L11:   0.0087 L22:   0.3234
REMARK   3      L33:   0.0453 L12:  -0.0271
REMARK   3      L13:  -0.0145 L23:  -0.0529
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0022 S12:  -0.0337 S13:  -0.0183
REMARK   3      S21:  -0.0050 S22:  -0.0017 S23:   0.0046
REMARK   3      S31:   0.0465 S32:   0.0029 S33:   0.0136
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: (CHAIN A AND RESID 218:247)
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3308  -4.9661  18.5341
REMARK   3    T TENSOR
REMARK   3      T11:   0.7933 T22:   0.3982
REMARK   3      T33:   0.5296 T12:   0.2120
REMARK   3      T13:   0.3159 T23:   0.1494
REMARK   3    L TENSOR
REMARK   3      L11:   0.3369 L22:   1.1339
REMARK   3      L33:   0.7741 L12:   0.5862
REMARK   3      L13:  -0.1293 L23:  -0.5199
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2762 S12:  -0.1277 S13:  -0.3301
REMARK   3      S21:  -0.3895 S22:  -0.2790 S23:  -0.0826
REMARK   3      S31:   0.5306 S32:   0.0602 S33:   0.4087
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: (CHAIN A AND RESID 248:263)
REMARK   3    ORIGIN FOR THE GROUP (A): -16.1294 -14.9392  29.2648
REMARK   3    T TENSOR
REMARK   3      T11:   1.1579 T22:   0.5651
REMARK   3      T33:   1.0983 T12:   0.1176
REMARK   3      T13:  -0.0666 T23:   0.3198
REMARK   3    L TENSOR
REMARK   3      L11:   2.9853 L22:   0.5161
REMARK   3      L33:   5.1822 L12:   0.1033
REMARK   3      L13:   0.0787 L23:  -1.6260
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3300 S12:   0.0001 S13:  -0.6262
REMARK   3      S21:  -0.3620 S22:   0.0239 S23:   1.0236
REMARK   3      S31:   0.9987 S32:   0.1258 S33:   0.2517
REMARK   3   TLS GROUP : 11
REMARK   3    SELECTION: (CHAIN A AND RESID 264:337)
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7845  12.1757  24.3219
REMARK   3    T TENSOR
REMARK   3      T11:   0.2603 T22:   0.5482
REMARK   3      T33:   0.1545 T12:   0.3267
REMARK   3      T13:   0.0755 T23:   0.0095
REMARK   3    L TENSOR
REMARK   3      L11:   0.1440 L22:   0.1266
REMARK   3      L33:   0.0436 L12:  -0.0257
REMARK   3      L13:   0.0075 L23:   0.0673
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1066 S12:  -0.3116 S13:  -0.1117
REMARK   3      S21:   0.1386 S22:   0.0354 S23:  -0.0364
REMARK   3      S31:   0.1106 S32:   0.1154 S33:  -0.0123
REMARK   3   TLS GROUP : 12
REMARK   3    SELECTION: (CHAIN A AND RESID 338:365)
REMARK   3    ORIGIN FOR THE GROUP (A): -47.0997   7.0417  16.5400
REMARK   3    T TENSOR
REMARK   3      T11:   0.2284 T22:   0.2187
REMARK   3      T33:   0.4008 T12:  -0.1020
REMARK   3      T13:   0.1499 T23:  -0.0815
REMARK   3    L TENSOR
REMARK   3      L11:   0.2467 L22:   0.0541
REMARK   3      L33:   0.1318 L12:   0.0831
REMARK   3      L13:   0.1013 L23:  -0.0031
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0685 S12:  -0.0016 S13:   0.0659
REMARK   3      S21:   0.0250 S22:  -0.0766 S23:  -0.0107
REMARK   3      S31:   0.0881 S32:  -0.0080 S33:   0.0551
REMARK   3   TLS GROUP : 13
REMARK   3    SELECTION: (CHAIN B)
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8543  27.1964  10.7789
REMARK   3    T TENSOR
REMARK   3      T11:   0.2044 T22:   0.2146
REMARK   3      T33:   0.1661 T12:  -0.0574
REMARK   3      T13:   0.0092 T23:   0.0112
REMARK   3    L TENSOR
REMARK   3      L11:   0.4174 L22:   0.7377
REMARK   3      L33:   2.1333 L12:   0.2470
REMARK   3      L13:  -0.4507 L23:  -1.1239
REMARK   3    S TENSOR
REMARK   3      S11:   0.0080 S12:   0.0623 S13:   0.1421
REMARK   3      S21:  -0.1146 S22:   0.1769 S23:   0.0552
REMARK   3      S31:   0.1100 S32:  -0.1228 S33:  -0.1205
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES -1,0,1-5, 174-187, 366-384 IN
REMARK   3   CHAIN A AND 141-142 IN CHAIN B ARE DISORDERED.
REMARK   4
REMARK   4 2XS0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-SEP-10.
REMARK 100 THE PDBE ID CODE IS EBI-45492.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-FEB-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X06SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : BENT MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13792
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.90
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 6.5
REMARK 200  R MERGE                    (I) : 0.07
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 16.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.5
REMARK 200  R MERGE FOR SHELL          (I) : 0.87
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.06
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2XRW
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24-26% PEG1000, 100MM TRIS
REMARK 280  PH 8.5
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       65.45500
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       65.45500
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       31.26500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.27500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       31.26500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.27500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       65.45500
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       31.26500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       53.27500
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       65.45500
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       31.26500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       53.27500
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 2260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.9 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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, THR 183 TO VAL
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, TYR 185 TO PHE
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     GLY A    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     SER A     2
REMARK 465     ARG A     3
REMARK 465     SER A     4
REMARK 465     LYS A     5
REMARK 465     ARG A   174
REMARK 465     THR A   175
REMARK 465     ALA A   176
REMARK 465     GLY A   177
REMARK 465     THR A   178
REMARK 465     SER A   179
REMARK 465     PHE A   180
REMARK 465     MET A   181
REMARK 465     MET A   182
REMARK 465     VAL A   183
REMARK 465     PRO A   184
REMARK 465     PHE A   185
REMARK 465     VAL A   186
REMARK 465     VAL A   187
REMARK 465     ARG A   366
REMARK 465     THR A   367
REMARK 465     LYS A   368
REMARK 465     ASN A   369
REMARK 465     GLY A   370
REMARK 465     VAL A   371
REMARK 465     ILE A   372
REMARK 465     ARG A   373
REMARK 465     GLY A   374
REMARK 465     GLN A   375
REMARK 465     PRO A   376
REMARK 465     SER A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     ALA A   380
REMARK 465     GLN A   381
REMARK 465     VAL A   382
REMARK 465     GLN A   383
REMARK 465     GLN A   384
REMARK 465     LEU B   141
REMARK 465     GLU B   142
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    GLN A  37       33.83    -74.89
REMARK 500    ASN A  63      155.76     94.10
REMARK 500    GLN A 102      -52.82   -128.81
REMARK 500    GLN A 120       31.04    -78.14
REMARK 500    ARG A 150      -20.02     78.49
REMARK 500    LYS A 203     -165.59   -118.34
REMARK 500    PRO A 254      -49.86    -29.60
REMARK 500    GLU A 261       34.39    -99.82
REMARK 500    ASN A 262       -0.64   -140.54
REMARK 500    ASP A 283      -88.84    -88.64
REMARK 500    ALA A 306        5.48    -64.46
REMARK 500    LYS A 340      -81.49     52.61
REMARK 500    LEU A 342      144.41    -29.98
REMARK 500    ASP A 343       53.90     39.78
REMARK 500    GLU A 344       15.45    179.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A1367
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XRW   RELATED DB: PDB
REMARK 900  LINEAR BINDING MOTIFS FOR JNK AND FOR CALCINEURIN
REMARK 900  ANTAGONISTICALLY CONTROL THE NUCLEAR SHUTTLING OF NFAT4
REMARK 900 RELATED ID: 1UKH   RELATED DB: PDB
REMARK 900  STRUCTURAL BASIS FOR THE SELECTIVE INHIBITION OF JNK1
REMARK 900  BYTHE SCAFFOLDING PROTEIN JIP1 AND SP600125
REMARK 900 RELATED ID: 2GMX   RELATED DB: PDB
REMARK 900  SELECTIVE AMINOPYRIDINE-BASED C-JUN N-TERMINAL
REMARK 900  KINASEINHIBITORS WITH CELLULAR ACTIVITY
REMARK 900 RELATED ID: 1UKI   RELATED DB: PDB
REMARK 900  STRUCTURAL BASIS FOR THE SELECTIVE INHIBITION OF JNK1
REMARK 900  BYTHE SCAFFOLDING PROTEIN JIP1 AND SP600125
REMARK 900 RELATED ID: 2H96   RELATED DB: PDB
REMARK 900  DISCOVERY OF POTENT, HIGHLY SELECTIVE, AND
REMARK 900  ORALLYBIOAVAILABLE PYRIDINE CARBOXAMIDE C-JUN NH2-
REMARK 900  TERMINALKINASE INHIBITORS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF CHAIN A CORRESPONDS TO ISOFORM 3 OF THE
REMARK 999 UNIPROT ACCESSION ID P45983
DBREF  2XS0 A    1   384  UNP    P45983   MK08_HUMAN       1    384
DBREF  2XS0 B  141   154  UNP    Q12968   NFAC3_HUMAN    141    154
SEQADV 2XS0 GLY A   -1  UNP  P45983              EXPRESSION TAG
SEQADV 2XS0 SER A    0  UNP  P45983              EXPRESSION TAG
SEQADV 2XS0 VAL A  183  UNP  P45983    THR   183 ENGINEERED MUTATION
SEQADV 2XS0 PHE A  185  UNP  P45983    TYR   185 ENGINEERED MUTATION
SEQRES   1 A  386  GLY SER MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR
SEQRES   2 A  386  SER VAL GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS
SEQRES   3 A  386  ARG TYR GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN
SEQRES   4 A  386  GLY ILE VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG
SEQRES   5 A  386  ASN VAL ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN
SEQRES   6 A  386  GLN THR HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU
SEQRES   7 A  386  MET LYS CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU
SEQRES   8 A  386  ASN VAL PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN
SEQRES   9 A  386  ASP VAL TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU
SEQRES  10 A  386  CYS GLN VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET
SEQRES  11 A  386  SER TYR LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS
SEQRES  12 A  386  LEU HIS SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO
SEQRES  13 A  386  SER ASN ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE
SEQRES  14 A  386  LEU ASP PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE
SEQRES  15 A  386  MET MET VAL PRO PHE VAL VAL THR ARG TYR TYR ARG ALA
SEQRES  16 A  386  PRO GLU VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL
SEQRES  17 A  386  ASP ILE TRP SER VAL GLY CYS ILE MET GLY GLU MET ILE
SEQRES  18 A  386  LYS GLY GLY VAL LEU PHE PRO GLY THR ASP HIS ILE ASP
SEQRES  19 A  386  GLN TRP ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS
SEQRES  20 A  386  PRO GLU PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR
SEQRES  21 A  386  TYR VAL GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE
SEQRES  22 A  386  GLU LYS LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER
SEQRES  23 A  386  GLU HIS ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU
SEQRES  24 A  386  LEU SER LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE
SEQRES  25 A  386  SER VAL ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL
SEQRES  26 A  386  TRP TYR ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS
SEQRES  27 A  386  ILE PRO ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE
SEQRES  28 A  386  GLU GLU TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP
SEQRES  29 A  386  LEU GLU GLU ARG THR LYS ASN GLY VAL ILE ARG GLY GLN
SEQRES  30 A  386  PRO SER PRO LEU ALA GLN VAL GLN GLN
SEQRES   1 B   14  LEU GLU ARG PRO SER ARG ASP HIS LEU TYR LEU PRO LEU
SEQRES   2 B   14  GLU
HET    ANP  A1367      31
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL   3  ANP    C10 H17 N6 O12 P3
FORMUL   4  HOH   *18(H2 O)
HELIX    1   1 ARG A    6  ASN A    8  5                                   3
HELIX    2   2 ASN A   63  VAL A   80  1                                  18
HELIX    3   3 LEU A  115  GLN A  120  1                                   6
HELIX    4   4 ASP A  124  SER A  144  1                                  21
HELIX    5   5 LYS A  153  SER A  155  5                                   3
HELIX    6   6 ALA A  193  LEU A  198  1                                   6
HELIX    7   7 ASN A  205  GLY A  221  1                                  17
HELIX    8   8 ASP A  229  GLY A  242  1                                  14
HELIX    9   9 CYS A  245  LYS A  250  1                                   6
HELIX   10  10 VAL A  256  GLU A  261  1                                   6
HELIX   11  11 SER A  270  PHE A  275  1                                   6
HELIX   12  12 PRO A  276  PHE A  280  5                                   5
HELIX   13  13 SER A  284  LEU A  302  1                                  19
HELIX   14  14 SER A  311  HIS A  318  1                                   8
HELIX   15  15 HIS A  318  VAL A  323  1                                   6
HELIX   16  16 ASP A  326  GLU A  331  1                                   6
HELIX   17  17 THR A  348  GLU A  364  1                                  17
SHEET    1  AA 2 PHE A  10  ILE A  15  0
SHEET    2  AA 2 SER A  18  LEU A  23 -1  O  SER A  18   N  ILE A  15
SHEET    1  AB 5 TYR A  26  GLY A  35  0
SHEET    2  AB 5 GLY A  38  ASP A  45 -1  O  GLY A  38   N  GLY A  35
SHEET    3  AB 5 ARG A  50  SER A  58 -1  O  ARG A  50   N  ASP A  45
SHEET    4  AB 5 ASP A 103  GLU A 109 -1  O  VAL A 104   N  LEU A  57
SHEET    5  AB 5 LEU A  88  PHE A  92 -1  N  LEU A  89   O  VAL A 107
SHEET    1  AC 3 ALA A 113  ASN A 114  0
SHEET    2  AC 3 ILE A 157  VAL A 159 -1  O  VAL A 159   N  ALA A 113
SHEET    3  AC 3 LEU A 165  ILE A 167 -1  O  LYS A 166   N  VAL A 158
SITE     1 AC1 18 ILE A  32  SER A  34  GLY A  35  GLN A  37
SITE     2 AC1 18 VAL A  40  ALA A  53  LYS A  55  ILE A  86
SITE     3 AC1 18 MET A 108  GLU A 109  MET A 111  ASN A 114
SITE     4 AC1 18 SER A 155  ASN A 156  LEU A 168  ASP A 169
SITE     5 AC1 18 HOH A2017  HOH A2018
CRYST1   62.530  106.550  130.910  90.00  90.00  90.00 C 2 2 21      8
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      0.015992  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009385  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007639        0.00000
      
PROCHECK
Go to PROCHECK summary
 References