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PDBsum entry 3rzf

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Immune system, signaling protein PDB id
3rzf
Jmol
Contents
Protein chain
541 a.a.
Ligands
XNM
HEADER    IMMUNE SYSTEM, SIGNALING PROTEIN        11-MAY-11   3RZF
TITLE     CRYSTAL STRUCTURE OF INHIBITOR OF KAPPAB KINASE BETA (I4122)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MGC80376 PROTEIN;
COMPND   3 CHAIN: A;
COMPND   4 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE   3 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;
SOURCE   4 ORGANISM_TAXID: 8355
KEYWDS    KINASE ULD, KINASE UBIQUITIN-LIKE DOMAIN SCAFFOLD HELIX, KINASE, I
KEYWDS   2 KAPPA B ALPHA, PHOSPHORYLATION, IMMUNE SYSTEM, SIGNALING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.XU,Y.C.LO,Q.LI,G.NAPOLITANO,X.WU,X.JIANG,M.DREANO,M.KARIN,H.WU
REVDAT   1   25-MAY-11 3RZF    0
SPRSDE     25-MAY-11 3RZF      3QAD
JRNL        AUTH   G.XU,Y.C.LO,Q.LI,G.NAPOLITANO,X.WU,X.JIANG,M.DREANO,M.KARIN,
JRNL        AUTH 2 H.WU
JRNL        TITL   CRYSTAL STRUCTURE OF INHIBITOR OF KAPPAB KINASE BETA.
JRNL        REF    NATURE                        V. 472   325 2011
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   21423167
JRNL        DOI    10.1038/NATURE09853
REMARK   2
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 4.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.96
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 83.7
REMARK   3   NUMBER OF REFLECTIONS             : 13319
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.273
REMARK   3   R VALUE            (WORKING SET) : 0.270
REMARK   3   FREE R VALUE                     : 0.340
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.920
REMARK   3   FREE R VALUE TEST SET COUNT      : 655
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 14.9651 -  6.6742    0.99     3096   166  0.2117 0.2742
REMARK   3     2  6.6742 -  5.3780    0.94     2882   153  0.3086 0.3953
REMARK   3     3  5.3780 -  4.7226    0.84     2534   112  0.3273 0.4394
REMARK   3     4  4.7226 -  4.3021    0.75     2234   120  0.3244 0.3794
REMARK   3     5  4.3021 -  4.0000    0.65     1918   104  0.4022 0.5085
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.49
REMARK   3   K_SOL              : 0.18
REMARK   3   B_SOL              : 200.53
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.720
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.230
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 130.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 40.20130
REMARK   3    B22 (A**2) : 40.20130
REMARK   3    B33 (A**2) : -80.40260
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      :  0.048           4579
REMARK   3   ANGLE     :  1.747           6060
REMARK   3   CHIRALITY :  0.106            677
REMARK   3   PLANARITY :  0.006            778
REMARK   3   DIHEDRAL  : 20.509           1735
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 10
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 16:100)
REMARK   3    ORIGIN FOR THE GROUP (A):  96.4567 -33.2915  60.0335
REMARK   3    T TENSOR
REMARK   3      T11:   0.9916 T22:   1.8687
REMARK   3      T33:   1.8545 T12:  -0.2546
REMARK   3      T13:   0.0213 T23:  -0.1613
REMARK   3    L TENSOR
REMARK   3      L11:   3.3121 L22:  -0.3815
REMARK   3      L33:   0.4864 L12:   0.8372
REMARK   3      L13:  -1.4954 L23:  -0.3243
REMARK   3    S TENSOR
REMARK   3      S11:   0.9884 S12:   1.1770 S13:   0.6902
REMARK   3      S21:   0.8001 S22:   0.2754 S23:  -0.5983
REMARK   3      S31:  -0.4041 S32:  -0.3716 S33:   1.4486
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 101:199)
REMARK   3    ORIGIN FOR THE GROUP (A):  79.3564 -30.8236  52.6644
REMARK   3    T TENSOR
REMARK   3      T11:   0.8707 T22:   1.8090
REMARK   3      T33:   1.1300 T12:  -0.6267
REMARK   3      T13:   0.1636 T23:  -0.3763
REMARK   3    L TENSOR
REMARK   3      L11:   3.9022 L22:   6.7662
REMARK   3      L33:   1.0747 L12:  -1.9657
REMARK   3      L13:   0.6870 L23:   1.6011
REMARK   3    S TENSOR
REMARK   3      S11:  -0.4279 S12:  -0.5895 S13:  -0.2299
REMARK   3      S21:   1.0836 S22:   1.0332 S23:  -0.8617
REMARK   3      S31:  -0.0973 S32:   0.8211 S33:   0.6465
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 200:309)
REMARK   3    ORIGIN FOR THE GROUP (A):  64.5919 -28.4447  50.4089
REMARK   3    T TENSOR
REMARK   3      T11:   0.7671 T22:   1.1675
REMARK   3      T33:   0.8366 T12:  -0.1944
REMARK   3      T13:   0.3160 T23:  -0.2196
REMARK   3    L TENSOR
REMARK   3      L11:   2.1442 L22:   2.5455
REMARK   3      L33:  -0.2095 L12:  -0.8008
REMARK   3      L13:  -0.4539 L23:   1.9499
REMARK   3    S TENSOR
REMARK   3      S11:   1.1020 S12:  -0.2096 S13:  -0.2635
REMARK   3      S21:   2.2229 S22:  -0.6869 S23:  -0.3937
REMARK   3      S31:   0.6979 S32:  -0.0189 S33:   0.0243
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 310:394)
REMARK   3    ORIGIN FOR THE GROUP (A):  64.9827 -21.3630  18.0643
REMARK   3    T TENSOR
REMARK   3      T11:   1.5755 T22:   1.6407
REMARK   3      T33:   1.2375 T12:  -0.0189
REMARK   3      T13:   0.0331 T23:  -0.0363
REMARK   3    L TENSOR
REMARK   3      L11:   1.9631 L22:   4.2094
REMARK   3      L33:   0.6432 L12:   0.0995
REMARK   3      L13:  -0.7998 L23:  -0.7452
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2625 S12:   1.6145 S13:   0.6327
REMARK   3      S21:  -2.0422 S22:   0.5204 S23:   0.3516
REMARK   3      S31:  -0.4256 S32:   1.2967 S33:  -0.0000
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 401:445)
REMARK   3    ORIGIN FOR THE GROUP (A):  63.0529  -5.2762  43.8078
REMARK   3    T TENSOR
REMARK   3      T11:   1.2782 T22:  -0.6151
REMARK   3      T33:   1.1930 T12:   0.4117
REMARK   3      T13:   0.6019 T23:  -0.5419
REMARK   3    L TENSOR
REMARK   3      L11:   1.1158 L22:   2.0885
REMARK   3      L33:   4.0232 L12:  -0.2673
REMARK   3      L13:  -2.0510 L23:  -1.2350
REMARK   3    S TENSOR
REMARK   3      S11:  -0.4518 S12:  -1.3793 S13:   0.6246
REMARK   3      S21:   0.2444 S22:  -0.2114 S23:  -0.3448
REMARK   3      S31:  -0.8344 S32:   3.8551 S33:  -0.0961
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 446:475)
REMARK   3    ORIGIN FOR THE GROUP (A):  73.5545  -6.2268   4.5283
REMARK   3    T TENSOR
REMARK   3      T11:   2.7881 T22:   2.8280
REMARK   3      T33:   2.4133 T12:  -0.3452
REMARK   3      T13:  -0.0183 T23:   0.0788
REMARK   3    L TENSOR
REMARK   3      L11:   0.0743 L22:   0.7507
REMARK   3      L33:   0.1226 L12:   0.6211
REMARK   3      L13:   0.0806 L23:   0.2089
REMARK   3    S TENSOR
REMARK   3      S11:  -1.2580 S12:   2.7060 S13:  -0.5852
REMARK   3      S21:  -0.8401 S22:  -0.3854 S23:   0.2178
REMARK   3      S31:   0.8363 S32:   0.6251 S33:   0.0000
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 528:551)
REMARK   3    ORIGIN FOR THE GROUP (A):  70.7371   4.2629   0.1771
REMARK   3    T TENSOR
REMARK   3      T11:   1.6943 T22:   1.7969
REMARK   3      T33:   2.2912 T12:   0.0036
REMARK   3      T13:   0.3684 T23:   0.1888
REMARK   3    L TENSOR
REMARK   3      L11:  -0.1465 L22:  -0.2074
REMARK   3      L33:   0.0249 L12:  -0.1253
REMARK   3      L13:   0.1057 L23:   0.0178
REMARK   3    S TENSOR
REMARK   3      S11:   1.2849 S12:   0.1417 S13:   0.5077
REMARK   3      S21:   0.7953 S22:   1.6862 S23:   2.4158
REMARK   3      S31:  -0.3155 S32:   0.4293 S33:  -0.0000
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 559:585)
REMARK   3    ORIGIN FOR THE GROUP (A):  74.4174  -0.1119  50.0928
REMARK   3    T TENSOR
REMARK   3      T11:   2.3424 T22:   1.9376
REMARK   3      T33:   2.4687 T12:  -0.6939
REMARK   3      T13:   0.3975 T23:  -0.5684
REMARK   3    L TENSOR
REMARK   3      L11:   0.0727 L22:  -0.1512
REMARK   3      L33:   0.1943 L12:  -0.0377
REMARK   3      L13:  -0.2155 L23:  -0.0560
REMARK   3    S TENSOR
REMARK   3      S11:   0.1396 S12:  -0.2977 S13:   0.8549
REMARK   3      S21:  -0.2926 S22:   1.6363 S23:  -0.5543
REMARK   3      S31:   0.1311 S32:   3.2704 S33:  -0.0000
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 586:610)
REMARK   3    ORIGIN FOR THE GROUP (A):  63.5584   2.6885  34.8697
REMARK   3    T TENSOR
REMARK   3      T11:   1.5666 T22:   0.8975
REMARK   3      T33:   2.1445 T12:   0.1793
REMARK   3      T13:   0.7065 T23:  -0.1232
REMARK   3    L TENSOR
REMARK   3      L11:   0.4357 L22:   0.7727
REMARK   3      L33:   0.1712 L12:  -0.9480
REMARK   3      L13:   0.2231 L23:  -0.0484
REMARK   3    S TENSOR
REMARK   3      S11:   1.7541 S12:   0.9383 S13:   0.5418
REMARK   3      S21:  -1.5669 S22:  -0.7132 S23:   1.0456
REMARK   3      S31:   0.8027 S32:   2.6221 S33:  -0.0000
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 611:637)
REMARK   3    ORIGIN FOR THE GROUP (A):  65.1787  -4.6189  -3.3832
REMARK   3    T TENSOR
REMARK   3      T11:   2.0124 T22:   2.5803
REMARK   3      T33:   2.5558 T12:  -0.3319
REMARK   3      T13:   0.0011 T23:   0.2304
REMARK   3    L TENSOR
REMARK   3      L11:   0.0052 L22:   0.6635
REMARK   3      L33:   0.0581 L12:  -0.2707
REMARK   3      L13:  -0.0254 L23:   0.1129
REMARK   3    S TENSOR
REMARK   3      S11:   1.1970 S12:   0.0290 S13:  -1.2469
REMARK   3      S21:  -0.0720 S22:   0.5531 S23:  -1.1709
REMARK   3      S31:  -2.3177 S32:  -2.0468 S33:   0.0000
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 3RZF COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-11.
REMARK 100 THE RCSB ID CODE IS RCSB065567.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-10
REMARK 200  TEMPERATURE           (KELVIN) : 83
REMARK 200  PH                             : 5.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 24-ID-C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.963937, 0.979163, 0.979328
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13319
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : 6.900
REMARK 200  R MERGE                    (I) : 0.05600
REMARK 200  R SYM                      (I) : 0.07800
REMARK 200   FOR THE DATA SET  : 25.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.30
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.05600
REMARK 200  R SYM FOR SHELL            (I) : 0.07800
REMARK 200   FOR SHELL         : 25.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 79.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M K/NA PHOSPHATE, PH 5.6, VAPOR
REMARK 280  DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       3555   -Y,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X,Z+3/4
REMARK 290       5555   -X+1/2,Y,-Z+3/4
REMARK 290       6555   X,-Y+1/2,-Z+1/4
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2
REMARK 290       8555   -Y,-X,-Z
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2
REMARK 290      10555   -X,-Y,Z
REMARK 290      11555   -Y+1/2,X,Z+3/4
REMARK 290      12555   Y,-X+1/2,Z+1/4
REMARK 290      13555   -X,Y+1/2,-Z+1/4
REMARK 290      14555   X+1/2,-Y,-Z+3/4
REMARK 290      15555   Y,X,-Z
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       82.32800
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       82.32800
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      136.72900
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       82.32800
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       68.36450
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       82.32800
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      205.09350
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       82.32800
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      205.09350
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       82.32800
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       68.36450
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       82.32800
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       82.32800
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      136.72900
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       82.32800
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       82.32800
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      136.72900
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       82.32800
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      205.09350
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       82.32800
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       68.36450
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       82.32800
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       68.36450
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       82.32800
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      205.09350
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       82.32800
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       82.32800
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      136.72900
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLN A    -1
REMARK 465     GLY A     0
REMARK 465     GLY A     1
REMARK 465     GLY A     2
REMARK 465     ARG A     3
REMARK 465     SER A     4
REMARK 465     PRO A     5
REMARK 465     SER A     6
REMARK 465     LEU A     7
REMARK 465     PRO A     8
REMARK 465     THR A     9
REMARK 465     GLN A    10
REMARK 465     THR A    11
REMARK 465     CYS A    12
REMARK 465     GLY A    13
REMARK 465     PRO A    14
REMARK 465     TRP A    15
REMARK 465     GLU A   237
REMARK 465     LYS A   238
REMARK 465     SER A   239
REMARK 465     ASN A   240
REMARK 465     GLU A   241
REMARK 465     HIS A   242
REMARK 465     GLN A   287
REMARK 465     ARG A   288
REMARK 465     GLY A   289
REMARK 465     ILE A   377
REMARK 465     ASP A   378
REMARK 465     GLY A   379
REMARK 465     ARG A   380
REMARK 465     GLN A   381
REMARK 465     GLY A   382
REMARK 465     GLU A   383
REMARK 465     THR A   395
REMARK 465     VAL A   396
REMARK 465     TYR A   397
REMARK 465     GLU A   398
REMARK 465     PRO A   399
REMARK 465     GLN A   400
REMARK 465     CYS A   476
REMARK 465     GLU A   477
REMARK 465     GLN A   478
REMARK 465     LEU A   479
REMARK 465     LYS A   480
REMARK 465     ALA A   481
REMARK 465     LYS A   482
REMARK 465     LEU A   483
REMARK 465     ASP A   484
REMARK 465     PHE A   485
REMARK 465     PHE A   486
REMARK 465     ARG A   487
REMARK 465     SER A   488
REMARK 465     SER A   489
REMARK 465     ILE A   490
REMARK 465     GLN A   491
REMARK 465     ILE A   492
REMARK 465     ASP A   493
REMARK 465     LEU A   494
REMARK 465     GLU A   495
REMARK 465     LYS A   496
REMARK 465     TYR A   497
REMARK 465     SER A   498
REMARK 465     GLU A   499
REMARK 465     GLN A   500
REMARK 465     MET A   501
REMARK 465     GLU A   502
REMARK 465     PHE A   503
REMARK 465     GLY A   504
REMARK 465     ILE A   505
REMARK 465     THR A   506
REMARK 465     SER A   507
REMARK 465     GLU A   508
REMARK 465     LYS A   509
REMARK 465     LEU A   510
REMARK 465     LEU A   511
REMARK 465     SER A   512
REMARK 465     ALA A   513
REMARK 465     TRP A   514
REMARK 465     ARG A   515
REMARK 465     GLU A   516
REMARK 465     MET A   517
REMARK 465     GLU A   518
REMARK 465     GLN A   519
REMARK 465     ALA A   520
REMARK 465     VAL A   521
REMARK 465     GLU A   522
REMARK 465     LEU A   523
REMARK 465     CYS A   524
REMARK 465     GLY A   525
REMARK 465     ARG A   526
REMARK 465     GLU A   527
REMARK 465     LEU A   552
REMARK 465     GLY A   553
REMARK 465     ARG A   554
REMARK 465     LYS A   555
REMARK 465     HIS A   556
REMARK 465     ARG A   557
REMARK 465     GLY A   558
REMARK 465     GLU A   638
REMARK 465     ASP A   639
REMARK 465     GLU A   640
REMARK 465     LYS A   641
REMARK 465     ILE A   642
REMARK 465     VAL A   643
REMARK 465     VAL A   644
REMARK 465     ARG A   645
REMARK 465     ARG A   646
REMARK 465     GLN A   647
REMARK 465     GLU A   648
REMARK 465     LYS A   649
REMARK 465     ARG A   650
REMARK 465     GLN A   651
REMARK 465     GLN A   652
REMARK 465     GLU A   653
REMARK 465     LEU A   654
REMARK 465     TRP A   655
REMARK 465     ASN A   656
REMARK 465     LEU A   657
REMARK 465     LEU A   658
REMARK 465     LYS A   659
REMARK 465     ILE A   660
REMARK 465     ALA A   661
REMARK 465     CYS A   662
REMARK 465     SER A   663
REMARK 465     LYS A   664
REMARK 465     VAL A   665
REMARK 465     ARG A   666
REMARK 465     GLY A   667
REMARK 465     PRO A   668
REMARK 465     VAL A   669
REMARK 465     SER A   670
REMARK 465     GLY A   671
REMARK 465     SER A   672
REMARK 465     PRO A   673
REMARK 465     ASP A   674
REMARK 465     SER A   675
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     SER A  51    OG
REMARK 470     VAL A  79    CG1  CG2
REMARK 470     ASP A  90    CG   OD1  OD2
REMARK 470     ASP A 291    CG   OD1  OD2
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   CE   MET A    65     CD1  LEU A   167              1.32
REMARK 500   O    CYS A    99     CG   GLU A   100              1.67
REMARK 500   CD   ARG A   144     O    TYR A   169              1.89
REMARK 500   SD   MET A    65     CD1  LEU A   167              1.95
REMARK 500   CA   GLY A   102     CAT  XNM A   676              2.12
REMARK 500   CA   GLY A   102     CAS  XNM A   676              2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    LEU A 249   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES
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    LYS A  18     -153.57    -65.58
REMARK 500    LEU A  21      -47.42   -135.20
REMARK 500    ASP A  36      -60.52   -124.95
REMARK 500    GLN A  48     -147.68   -105.21
REMARK 500    LEU A  50       71.51     14.57
REMARK 500    PRO A  71       47.17    -58.07
REMARK 500    ASN A  72       -1.86   -142.62
REMARK 500    ARG A  77      -23.71   -141.02
REMARK 500    GLU A  78     -117.83     86.82
REMARK 500    ASP A  81       42.98    -81.18
REMARK 500    GLN A  84     -107.21     61.70
REMARK 500    ALA A  87      139.19     61.48
REMARK 500    ASP A  90       37.02    -96.68
REMARK 500    PRO A  92     -169.60    -64.15
REMARK 500    GLU A 100      -22.33    151.15
REMARK 500    CYS A 114      170.20    -54.05
REMARK 500    CYS A 115       16.48     53.75
REMARK 500    GLU A 119     -139.88   -108.27
REMARK 500    ARG A 134      -70.86    -47.07
REMARK 500    TYR A 135      -62.15    -19.45
REMARK 500    ILE A 141       71.29   -106.56
REMARK 500    ASP A 145     -157.32   -126.73
REMARK 500    LEU A 146      120.88    175.51
REMARK 500    ARG A 159      117.21   -168.40
REMARK 500    ASP A 166       79.38     64.19
REMARK 500    LEU A 173      -41.64     77.28
REMARK 500    CYS A 179     -148.81   -111.98
REMARK 500    THR A 180       11.02   -162.85
REMARK 500    GLN A 187      -64.09     51.05
REMARK 500    LEU A 189      156.56    107.88
REMARK 500    GLU A 192      -53.58    -28.34
REMARK 500    GLN A 196       14.46     59.31
REMARK 500    THR A 202      -24.82    -35.56
REMARK 500    TRP A 206      -70.18    -55.30
REMARK 500    PHE A 219     -106.34   -139.03
REMARK 500    ARG A 220      171.13    144.45
REMARK 500    PRO A 221       73.99   -101.52
REMARK 500    TRP A 226     -132.65     46.36
REMARK 500    GLN A 227      -64.31   -138.07
REMARK 500    VAL A 229      -17.33    103.39
REMARK 500    GLN A 230      -12.55   -156.93
REMARK 500    VAL A 235       48.08      7.60
REMARK 500    LEU A 249     -157.06   -146.14
REMARK 500    THR A 250      -68.02   -134.99
REMARK 500    ALA A 252       76.35   -155.74
REMARK 500    VAL A 258      -46.95   -143.03
REMARK 500    THR A 261      -83.23   -111.84
REMARK 500    LEU A 265      -45.67   -174.04
REMARK 500    SER A 266     -152.64   -166.57
REMARK 500    LYS A 272      -70.32     -3.56
REMARK 500
REMARK 500 THIS ENTRY HAS     123 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 HIS A  232     GLY A  233                  148.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PHE A 219        23.9      L          L   OUTSIDE RANGE
REMARK 500    VAL A 229        22.4      L          L   OUTSIDE RANGE
REMARK 500    THR A 261        23.4      L          L   OUTSIDE RANGE
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 XNM A 676
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QA8   RELATED DB: PDB
DBREF  3RZF A   17   675  UNP    Q6INT1   Q6INT1_XENLA     1    659
SEQADV 3RZF GLN A   -1  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF GLY A    0  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF GLY A    1  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF GLY A    2  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF ARG A    3  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF SER A    4  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF PRO A    5  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF SER A    6  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF LEU A    7  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF PRO A    8  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF THR A    9  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF GLN A   10  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF THR A   11  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF CYS A   12  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF GLY A   13  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF PRO A   14  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF TRP A   15  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF GLU A   16  UNP  Q6INT1              EXPRESSION TAG
SEQADV 3RZF GLU A  177  UNP  Q6INT1    SER   161 ENGINEERED MUTATION
SEQADV 3RZF GLU A  181  UNP  Q6INT1    SER   165 ENGINEERED MUTATION
SEQRES   1 A  677  GLN GLY GLY GLY ARG SER PRO SER LEU PRO THR GLN THR
SEQRES   2 A  677  CYS GLY PRO TRP GLU MET LYS GLU ARG LEU GLY THR GLY
SEQRES   3 A  677  GLY PHE GLY TYR VAL LEU ARG TRP ILE HIS GLN ASP THR
SEQRES   4 A  677  GLY GLU GLN VAL ALA ILE LYS GLN CYS ARG GLN GLU LEU
SEQRES   5 A  677  SER PRO LYS ASN ARG GLU ARG TRP CYS LEU GLU ILE GLN
SEQRES   6 A  677  ILE MET LYS LYS LEU ASN HIS PRO ASN VAL VAL SER ALA
SEQRES   7 A  677  ARG GLU VAL PRO ASP GLY LEU GLN LYS LEU ALA PRO ASN
SEQRES   8 A  677  ASP LEU PRO LEU LEU ALA MET GLU TYR CYS GLU GLY GLY
SEQRES   9 A  677  ASP LEU ARG LYS TYR LEU ASN GLN PHE GLU ASN CYS CYS
SEQRES  10 A  677  GLY LEU LYS GLU GLY PRO ILE ARG THR LEU LEU SER ASP
SEQRES  11 A  677  ILE SER SER ALA LEU ARG TYR LEU HIS GLU ASN ARG ILE
SEQRES  12 A  677  ILE HIS ARG ASP LEU LYS PRO GLU ASN ILE VAL LEU GLN
SEQRES  13 A  677  PRO GLY PRO GLN ARG LEU ILE HIS LYS ILE ILE ASP LEU
SEQRES  14 A  677  GLY TYR ALA LYS GLU LEU ASP GLN GLY GLU LEU CYS THR
SEQRES  15 A  677  GLU PHE VAL GLY THR LEU GLN TYR LEU ALA PRO GLU LEU
SEQRES  16 A  677  LEU GLU GLN LYS LYS TYR THR VAL THR VAL ASP TYR TRP
SEQRES  17 A  677  SER PHE GLY THR LEU ALA PHE GLU CYS ILE THR GLY PHE
SEQRES  18 A  677  ARG PRO PHE LEU PRO ASN TRP GLN PRO VAL GLN TRP HIS
SEQRES  19 A  677  GLY LYS VAL ARG GLU LYS SER ASN GLU HIS ILE VAL VAL
SEQRES  20 A  677  TYR ASP ASP LEU THR GLY ALA VAL LYS PHE SER SER VAL
SEQRES  21 A  677  LEU PRO THR PRO ASN HIS LEU SER GLY ILE LEU ALA GLY
SEQRES  22 A  677  LYS LEU GLU ARG TRP LEU GLN CYS MET LEU MET TRP HIS
SEQRES  23 A  677  GLN ARG GLN ARG GLY THR ASP PRO GLN ASN PRO ASN VAL
SEQRES  24 A  677  GLY CYS PHE GLN ALA LEU ASP SER ILE LEU SER LEU LYS
SEQRES  25 A  677  LEU LEU SER VAL MET ASN MET VAL SER GLY ARG VAL HIS
SEQRES  26 A  677  THR TYR PRO VAL THR GLU ASN GLU ASN LEU GLN ASN LEU
SEQRES  27 A  677  LYS SER TRP LEU GLN GLN ASP THR GLY ILE PRO GLU GLU
SEQRES  28 A  677  GLU GLN GLU LEU LEU GLN ALA SER GLY LEU ALA LEU ASN
SEQRES  29 A  677  SER ALA GLN PRO LEU THR GLN TYR VAL ILE ASP CYS THR
SEQRES  30 A  677  VAL ILE ASP GLY ARG GLN GLY GLU GLY ASP LEU ILE PHE
SEQRES  31 A  677  LEU PHE ASP ASN ARG LYS THR VAL TYR GLU PRO GLN ILE
SEQRES  32 A  677  SER LEU PRO ALA HIS PRO GLU SER VAL SER ILE VAL LEU
SEQRES  33 A  677  GLN ASP PRO LYS ARG PRO LEU THR TYR THR HIS LEU ARG
SEQRES  34 A  677  ARG VAL TRP GLY GLN ILE TRP GLN THR ILE ARG ALA LEU
SEQRES  35 A  677  LYS GLU ASP CYS ALA ARG LEU LEU GLN GLY GLN ARG THR
SEQRES  36 A  677  SER MET VAL ASN LEU LEU ARG TYR ASN THR GLU LEU SER
SEQRES  37 A  677  LYS LYS LYS ASN SER MET THR SER GLU CYS GLU GLN LEU
SEQRES  38 A  677  LYS ALA LYS LEU ASP PHE PHE ARG SER SER ILE GLN ILE
SEQRES  39 A  677  ASP LEU GLU LYS TYR SER GLU GLN MET GLU PHE GLY ILE
SEQRES  40 A  677  THR SER GLU LYS LEU LEU SER ALA TRP ARG GLU MET GLU
SEQRES  41 A  677  GLN ALA VAL GLU LEU CYS GLY ARG GLU ARG GLU VAL GLN
SEQRES  42 A  677  ALA LEU VAL ASP LYS MET MET ALA LEU GLN THR ASP SER
SEQRES  43 A  677  VAL ASP LEU GLN ARG ASN PRO LEU GLY ARG LYS HIS ARG
SEQRES  44 A  677  GLY THR LEU ASP ASP LEU GLU GLU GLN ALA ARG ASP LEU
SEQRES  45 A  677  TYR ARG ARG LEU ARG GLU ARG PRO ARG ASP GLN ARG THR
SEQRES  46 A  677  PRO GLY ASP SER ASN ASP MET VAL ARG LEU LEU ILE LEU
SEQRES  47 A  677  ALA ILE GLN SER PHE GLU LYS ARG VAL ILE LEU ILE TYR
SEQRES  48 A  677  ASP GLN LEU SER LYS THR VAL VAL CYS LYS ARG LYS ALA
SEQRES  49 A  677  LEU GLU LEU SER PRO LYS VAL LYS GLU VAL MET ASN LEU
SEQRES  50 A  677  MET ARG GLU ASP GLU LYS ILE VAL VAL ARG ARG GLN GLU
SEQRES  51 A  677  LYS ARG GLN GLN GLU LEU TRP ASN LEU LEU LYS ILE ALA
SEQRES  52 A  677  CYS SER LYS VAL ARG GLY PRO VAL SER GLY SER PRO ASP
SEQRES  53 A  677  SER
HET    XNM  A 676      31
HETNAM     XNM (4-{[4-(4-CHLOROPHENYL)PYRIMIDIN-2-YL]AMINO}PHENYL)[4-
HETNAM   2 XNM  (2-HYDROXYETHYL)PIPERAZIN-1-YL]METHANONE
FORMUL   2  XNM    C23 H24 CL N5 O2
HELIX    1   1 PRO A   52  LEU A   68  1                                  17
HELIX    2   2 ASP A  103  ASN A  109  1                                   7
HELIX    3   3 GLN A  110  CYS A  114  5                                   5
HELIX    4   4 GLY A  120  ASN A  139  1                                  20
HELIX    5   5 ALA A  190  GLU A  195  1                                   6
HELIX    6   6 VAL A  201  GLY A  218  1                                  18
HELIX    7   7 ILE A  268  MET A  280  1                                  13
HELIX    8   8 PHE A  300  LEU A  309  1                                  10
HELIX    9   9 ASN A  332  GLN A  342  1                                  11
HELIX   10  10 PRO A  347  GLN A  351  5                                   5
HELIX   11  11 PRO A  366  TYR A  370  5                                   5
HELIX   12  12 SER A  409  ASP A  416  5                                   8
HELIX   13  13 ARG A  428  ARG A  452  1                                  25
HELIX   14  14 MET A  455  LEU A  465  1                                  11
HELIX   15  15 SER A  466  ASN A  470  5                                   5
HELIX   16  16 GLN A  541  ASP A  546  1                                   6
HELIX   17  17 LEU A  560  TYR A  571  1                                  12
HELIX   18  18 ASP A  589  GLN A  599  1                                  11
HELIX   19  19 VAL A  605  SER A  613  1                                   9
HELIX   20  20 LYS A  614  VAL A  616  5                                   3
HELIX   21  21 SER A  626  GLU A  631  1                                   6
SHEET    1   A 4 ARG A  20  GLY A  24  0
SHEET    2   A 4 GLY A  27  ILE A  33 -1  O  VAL A  29   N  LEU A  21
SHEET    3   A 4 GLN A  40  CYS A  46 -1  O  VAL A  41   N  TRP A  32
SHEET    4   A 4 LEU A  94  GLU A  97 -1  O  LEU A  94   N  LYS A  44
SHEET    1   B 2 ILE A 151  GLN A 154  0
SHEET    2   B 2 ILE A 161  ILE A 164 -1  O  ILE A 161   N  GLN A 154
SHEET    1   C 2 LEU A 311  LEU A 312  0
SHEET    2   C 2 TYR A 325  PRO A 326 -1  O  TYR A 325   N  LEU A 312
SHEET    1   D 4 ARG A 321  VAL A 322  0
SHEET    2   D 4 VAL A 314  ASN A 316 -1  N  ASN A 316   O  ARG A 321
SHEET    3   D 4 LEU A 386  LEU A 389  1  O  PHE A 388   N  MET A 315
SHEET    4   D 4 GLU A 352  GLN A 355 -1  N  GLU A 352   O  LEU A 389
CISPEP   1 SER A   51    PRO A   52          0       -15.10
CISPEP   2 PRO A  221    PHE A  222          0         0.14
CISPEP   3 PRO A  228    VAL A  229          0        -5.94
CISPEP   4 THR A  344    GLY A  345          0         1.53
CISPEP   5 ASN A  362    SER A  363          0        -0.12
SITE     1 AC1 11 LEU A  21  VAL A  29  ALA A  42  MET A  96
SITE     2 AC1 11 GLU A  97  TYR A  98  CYS A  99  GLY A 102
SITE     3 AC1 11 ASP A 103  LYS A 106  VAL A 152
CRYST1  164.656  164.656  273.458  90.00  90.00  90.00 I 41 2 2     16
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      0.006073  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006073  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003657        0.00000
      
PROCHECK
Go to PROCHECK summary
 References