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Database: PDB
Entry: 3G90
LinkDB: 3G90
Original site: 3G90 
HEADER    TRANSFERASE                             12-FEB-09   3G90              
TITLE     JNK-3 BOUND TO (Z)-5-FLUORO-1-((6-FLUORO-4H-BENZO[D][1,3]DIOXIN-8-YL) 
TITLE    2 METHYL)-3-(HYDROXYIMINO)INDOLIN-2-ONE                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 10;                       
COMPND   3 CHAIN: X;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN;                                             
COMPND   5 SYNONYM: STRESS-ACTIVATED PROTEIN KINASE JNK3, C-JUN N-TERMINAL      
COMPND   6 KINASE 3, MAP KINASE P49 3F12;                                       
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 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: JNK3, JNK3A, MAPK10, PRKM10;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-15B                                   
KEYWDS    KINASE, INHIBITOR, PHOSPHORYLATION, ATP-BINDING, EPILEPSY,            
KEYWDS   2 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, SERINE/THREONINE-PROTEIN KINASE, 
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.XIE,M.D.JACOBS                                                      
REVDAT   4   13-JUL-11 3G90    1       VERSN                                    
REVDAT   3   19-MAY-09 3G90    1       JRNL                                     
REVDAT   2   28-APR-09 3G90    1       JRNL                                     
REVDAT   1   24-FEB-09 3G90    0                                                
JRNL        AUTH   J.CAO,H.GAO,G.BEMIS,F.SALITURO,M.LEDEBOER,E.HARRINGTON,      
JRNL        AUTH 2 S.WILKE,P.TASLIMI,S.PAZHANISAMY,X.XIE,M.JACOBS,J.GREEN       
JRNL        TITL   STRUCTURE-BASED DESIGN AND PARALLEL SYNTHESIS OF N-BENZYL    
JRNL        TITL 2 ISATIN OXIMES AS JNK3 MAP KINASE INHIBITORS.                 
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  19  2891 2009              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   19361991                                                     
JRNL        DOI    10.1016/J.BMCL.2009.03.043                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.26                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 14851                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 748                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1073                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.38                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 54                           
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2800                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 62                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.78000                                              
REMARK   3    B22 (A**2) : -2.49000                                             
REMARK   3    B33 (A**2) : -1.29000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.494         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.287         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.240         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.378        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2891 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3916 ; 1.233 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   341 ; 5.778 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   133 ;39.387 ;24.361       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   520 ;17.742 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;18.551 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   430 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2170 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1257 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1937 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    98 ; 0.159 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    43 ; 0.228 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.168 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1780 ; 0.534 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2812 ; 0.866 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1277 ; 1.155 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1104 ; 1.807 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X    46        X   149                          
REMARK   3    RESIDUE RANGE :   X   217        X   225                          
REMARK   3    RESIDUE RANGE :   X   372        X   400                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6520  18.1870  40.4780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0403 T22:  -0.0758                                     
REMARK   3      T33:  -0.2514 T12:  -0.0363                                     
REMARK   3      T13:   0.0042 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0928 L22:   5.1691                                     
REMARK   3      L33:   4.0306 L12:  -0.1493                                     
REMARK   3      L13:   0.6231 L23:   0.2590                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0997 S12:   0.1138 S13:   0.3011                       
REMARK   3      S21:   0.0954 S22:  -0.0870 S23:  -0.0247                       
REMARK   3      S31:  -0.2062 S32:   0.0123 S33:   0.1867                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X   150        X   211                          
REMARK   3    RESIDUE RANGE :   X   226        X   371                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.5660  13.9580  11.8550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0227 T22:  -0.0996                                     
REMARK   3      T33:  -0.2375 T12:   0.0060                                     
REMARK   3      T13:  -0.0363 T23:  -0.0238                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6273 L22:   3.1047                                     
REMARK   3      L33:   3.0267 L12:   0.7557                                     
REMARK   3      L13:   0.5826 L23:   0.5755                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0699 S12:   0.0963 S13:   0.2249                       
REMARK   3      S21:  -0.3482 S22:   0.0424 S23:   0.0474                       
REMARK   3      S31:  -0.1959 S32:   0.0549 S33:   0.0275                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3G90 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051574.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15243                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% (V/V) POLYETHYLENE GLYCOL         
REMARK 280  MONOMETHYL ETHER (AVERAGE MR = 550), 10% (V/V) ETHYLENE GLYCOL,     
REMARK 280  20 MM BETA-MERCAPTOETHANOL, 100 MM HEPES, PH 7.5, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.82750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.59450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.14450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.59450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.82750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.14450            
REMARK 290   SMTRY3   4  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET X    38                                                      
REMARK 465     GLY X    39                                                      
REMARK 465     SER X    40                                                      
REMARK 465     LYS X    41                                                      
REMARK 465     SER X    42                                                      
REMARK 465     LYS X    43                                                      
REMARK 465     VAL X    44                                                      
REMARK 465     ASP X    45                                                      
REMARK 465     GLY X    73                                                      
REMARK 465     ALA X    74                                                      
REMARK 465     ARG X   212                                                      
REMARK 465     THR X   213                                                      
REMARK 465     ALA X   214                                                      
REMARK 465     GLY X   215                                                      
REMARK 465     THR X   216                                                      
REMARK 465     TYR X   376                                                      
REMARK 465     ASP X   377                                                      
REMARK 465     LYS X   378                                                      
REMARK 465     SER X   401                                                      
REMARK 465     GLU X   402                                                      
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 X 303    CG   CD   CE   NZ                                   
REMARK 470     GLN X 379    CG   CD   OE1  NE2                                  
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 X 140      -53.69   -140.99                                   
REMARK 500    MET X 149     -151.85   -121.84                                   
REMARK 500    ASP X 189       26.44   -144.21                                   
REMARK 500    CYS X 201        2.29     80.77                                   
REMARK 500    MET X 220       72.17   -103.85                                   
REMARK 500    PRO X 264     -166.32    -74.23                                   
REMARK 500    ALA X 320       38.56   -155.35                                   
REMARK 500    GLU X 369       52.19   -119.97                                   
REMARK 500    PRO X 371      121.54    -38.10                                   
REMARK 500    LEU X 380       77.01     52.93                                   
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 J72 X 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3G9L   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3G9N   RELATED DB: PDB                                   
DBREF  3G90 X   40   402  UNP    P53779   MK10_HUMAN      40    402             
SEQADV 3G90 MET X   38  UNP  P53779              EXPRESSION TAG                 
SEQADV 3G90 GLY X   39  UNP  P53779              EXPRESSION TAG                 
SEQRES   1 X  365  MET GLY SER LYS SER LYS VAL ASP ASN GLN PHE TYR SER          
SEQRES   2 X  365  VAL GLU VAL GLY ASP SER THR PHE THR VAL LEU LYS ARG          
SEQRES   3 X  365  TYR GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY          
SEQRES   4 X  365  ILE VAL CYS ALA ALA TYR ASP ALA VAL LEU ASP ARG ASN          
SEQRES   5 X  365  VAL ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN          
SEQRES   6 X  365  THR HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET          
SEQRES   7 X  365  LYS CYS VAL ASN HIS LYS ASN ILE ILE SER LEU LEU ASN          
SEQRES   8 X  365  VAL PHE THR PRO GLN LYS THR LEU GLU GLU PHE GLN ASP          
SEQRES   9 X  365  VAL TYR LEU VAL MET GLU LEU MET ASP ALA ASN LEU CYS          
SEQRES  10 X  365  GLN VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER          
SEQRES  11 X  365  TYR LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU          
SEQRES  12 X  365  HIS SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER          
SEQRES  13 X  365  ASN ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU          
SEQRES  14 X  365  ASP PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET          
SEQRES  15 X  365  MET THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO          
SEQRES  16 X  365  GLU VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP          
SEQRES  17 X  365  ILE TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL ARG          
SEQRES  18 X  365  HIS LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN          
SEQRES  19 X  365  TRP ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO          
SEQRES  20 X  365  GLU PHE MET LYS LYS LEU GLN PRO THR VAL ARG ASN TYR          
SEQRES  21 X  365  VAL GLU ASN ARG PRO LYS TYR ALA GLY LEU THR PHE PRO          
SEQRES  22 X  365  LYS LEU PHE PRO ASP SER LEU PHE PRO ALA ASP SER GLU          
SEQRES  23 X  365  HIS ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU          
SEQRES  24 X  365  SER LYS MET LEU VAL ILE ASP PRO ALA LYS ARG ILE SER          
SEQRES  25 X  365  VAL ASP ASP ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP          
SEQRES  26 X  365  TYR ASP PRO ALA GLU VAL GLU ALA PRO PRO PRO GLN ILE          
SEQRES  27 X  365  TYR ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU          
SEQRES  28 X  365  GLU TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASN SER          
SEQRES  29 X  365  GLU                                                          
HET    J72  X   1      25                                                       
HETNAM     J72 (3E)-5-FLUORO-1-[(6-FLUORO-4H-1,3-BENZODIOXIN-8-YL)              
HETNAM   2 J72  METHYL]-1H-INDOLE-2,3-DIONE 3-OXIME                             
FORMUL   2  J72    C17 H12 F2 N2 O4                                             
FORMUL   3  HOH   *62(H2 O)                                                     
HELIX    1   1 PRO X   98  GLN X  100  5                                   3    
HELIX    2   2 ASN X  101  VAL X  118  1                                  18    
HELIX    3   3 LEU X  153  GLN X  158  1                                   6    
HELIX    4   4 ASP X  162  SER X  182  1                                  21    
HELIX    5   5 LYS X  191  SER X  193  5                                   3    
HELIX    6   6 ALA X  231  LEU X  236  1                                   6    
HELIX    7   7 ASN X  243  HIS X  259  1                                  17    
HELIX    8   8 ASP X  267  GLY X  280  1                                  14    
HELIX    9   9 CYS X  283  LYS X  288  1                                   6    
HELIX   10  10 GLN X  291  ASN X  300  1                                  10    
HELIX   11  11 THR X  308  PHE X  313  1                                   6    
HELIX   12  12 PRO X  314  PHE X  318  5                                   5    
HELIX   13  13 SER X  322  LEU X  340  1                                  19    
HELIX   14  14 SER X  349  GLN X  355  1                                   7    
HELIX   15  15 ILE X  359  TYR X  363  5                                   5    
HELIX   16  16 ASP X  364  GLU X  369  1                                   6    
HELIX   17  17 THR X  386  ASN X  400  1                                  15    
SHEET    1   A 2 PHE X  48  VAL X  53  0                                        
SHEET    2   A 2 SER X  56  LEU X  61 -1  O  SER X  56   N  VAL X  53           
SHEET    1   B 5 TYR X  64  GLY X  71  0                                        
SHEET    2   B 5 ILE X  77  ASP X  83 -1  O  TYR X  82   N  GLN X  65           
SHEET    3   B 5 ARG X  88  SER X  96 -1  O  ILE X  92   N  CYS X  79           
SHEET    4   B 5 ASP X 141  GLU X 147 -1  O  VAL X 142   N  LEU X  95           
SHEET    5   B 5 LEU X 126  PHE X 130 -1  N  LEU X 127   O  VAL X 145           
SHEET    1   C 3 ALA X 151  ASN X 152  0                                        
SHEET    2   C 3 ILE X 195  VAL X 197 -1  O  VAL X 197   N  ALA X 151           
SHEET    3   C 3 LEU X 203  ILE X 205 -1  O  LYS X 204   N  VAL X 196           
SITE     1 AC1 12 ILE X  70  GLN X  75  VAL X  78  ALA X  91                    
SITE     2 AC1 12 ILE X 124  GLU X 147  MET X 149  ASP X 150                    
SITE     3 AC1 12 ALA X 151  ASN X 152  GLN X 155  VAL X 196                    
CRYST1   49.655   72.289  107.189  90.00  90.00  90.00 P 21 21 21    4          
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      0.020139  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013833  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009329        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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