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Database: PDB
Entry: 3O2M
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HEADER    TRANSFERASE/INHIBITOR                   22-JUL-10   3O2M              
TITLE     CRYSTAL STRUCTURE OF JNK1-ALPHA1 ISOFORM COMPLEX WITH A BIARYL        
TITLE    2 TETRAZOL (A-82118)                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-364;                                        
COMPND   5 SYNONYM: MAP KINASE 8, MAPK 8, STRESS-ACTIVATED PROTEIN KINASE JNK1, 
COMPND   6 C-JUN N-TERMINAL KINASE 1, JNK-46, STRESS-ACTIVATED 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: C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 1, JIP1,   
COMPND  12 10MER PEPTIDE;                                                       
COMPND  13 CHAIN: F, G;                                                         
COMPND  14 SYNONYM: JNK-INTERACTING PROTEIN 1, JIP-1, JNK MAP KINASE SCAFFOLD   
COMPND  15 PROTEIN 1;                                                           
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: JNK1, MAPK8, PRKM8, SAPK1;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090                                                
KEYWDS    SERINE THREONINE PROTEIN KINASE, ATP BINDING, PHOSPHORYLATION,        
KEYWDS   2 KINASE-INHIBITOR COMPLEX, TRANSFERASE-INHIBITOR COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.ABAD-ZAPATERO                                                       
REVDAT   3   14-SEP-11 3O2M    1       JRNL   VERSN                             
REVDAT   2   23-FEB-11 3O2M    1       JRNL                                     
REVDAT   1   12-JAN-11 3O2M    0                                                
JRNL        AUTH   K.M.COMESS,C.SUN,C.ABAD-ZAPATERO,E.R.GOEDKEN,R.J.GUM,        
JRNL        AUTH 2 D.W.BORHANI,M.ARGIRIADI,D.R.GROEBE,Y.JIA,J.E.CLAMPIT,        
JRNL        AUTH 3 D.L.HAASCH,H.T.SMITH,S.WANG,D.SONG,M.L.COEN,T.E.CLOUTIER,    
JRNL        AUTH 4 H.TANG,X.CHENG,C.QUINN,B.LIU,Z.XIN,G.LIU,E.H.FRY,V.STOLL,    
JRNL        AUTH 5 T.I.NG,D.BANACH,D.MARCOTTE,D.J.BURNS,D.J.CALDERWOOD,         
JRNL        AUTH 6 P.J.HAJDUK                                                   
JRNL        TITL   DISCOVERY AND CHARACTERIZATION OF NON-ATP SITE INHIBITORS OF 
JRNL        TITL 2 THE MITOGEN ACTIVATED PROTEIN (MAP) KINASES.                 
JRNL        REF    ACS CHEM.BIOL.                V.   6   234 2011              
JRNL        REFN                   ISSN 1554-8929                               
JRNL        PMID   21090814                                                     
JRNL        DOI    10.1021/CB1002619                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 389580.090                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 43787                          
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 SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4384                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5078                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 545                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5955                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 82                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.39                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.37                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.46                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.42                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.02                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 39.56                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : SO4.PAR                                        
REMARK   3  PARAMETER FILE  5  : LIG.PAR                                        
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : SO4.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : LIG.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3O2M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060586.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46583                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 76.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP : 2 UL OF 10 MG/ML          
REMARK 280  PROTEIN PLUS 2 UL OF WELL SOLUTION WELL SOLUTION : 3.0 M AMMONIUM   
REMARK 280  SULFATE, 10 % GLYCEROL CO-CRYSTALLIZATION : COMPOUNDS IN DMSO       
REMARK 280  ADDED TO THE PROTEIN SOLUTION (0.62 MM COMPOUND WITH PROTEIN        
REMARK 280  CONCENTRATION OF 9 MG/ML) MORE THAN 1 HOUR INCUBATION ON ICE, PH    
REMARK 280  6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.63933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       41.31967            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       41.31967            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       82.63933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 300 REMARK: TWO UNDECAPEPTIDES IN ONE ASYMMETRIC UNIT                    
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: 1640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, B, G                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     HIS A   365                                                      
REMARK 465     HIS A   366                                                      
REMARK 465     HIS A   367                                                      
REMARK 465     HIS A   368                                                      
REMARK 465     HIS A   369                                                      
REMARK 465     HIS A   370                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     HIS B   365                                                      
REMARK 465     HIS B   366                                                      
REMARK 465     HIS B   367                                                      
REMARK 465     HIS B   368                                                      
REMARK 465     HIS B   369                                                      
REMARK 465     HIS B   370                                                      
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 B 168   CA  -  CB  -  CG  ANGL. DEV. =  15.1 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    ASN A   8     -116.77    -90.36                                   
REMARK 500    ASN A  28      -37.28     83.88                                   
REMARK 500    LEU A  29     -110.46     50.25                                   
REMARK 500    LYS A  30      123.70     72.11                                   
REMARK 500    ILE A  32      -18.88   -141.04                                   
REMARK 500    GLU A  49       63.44     60.16                                   
REMARK 500    ARG A  50      147.31   -173.77                                   
REMARK 500    ARG A  59       83.95     65.98                                   
REMARK 500    ASN A  63      154.35    175.36                                   
REMARK 500    PHE A 101      119.22    -39.39                                   
REMARK 500    GLN A 102      -33.77   -140.36                                   
REMARK 500    MET A 111     -159.72    -95.48                                   
REMARK 500    ARG A 150      -13.97     72.90                                   
REMARK 500    ASP A 169       93.80     80.49                                   
REMARK 500    ALA A 176      170.90    -52.97                                   
REMARK 500    GLU A 183       61.14     39.00                                   
REMARK 500    HIS A 221       -2.03     75.51                                   
REMARK 500    PRO A 226     -124.08    -56.88                                   
REMARK 500    SER A 284     -158.80   -117.07                                   
REMARK 500    LYS A 288      -72.28    -88.02                                   
REMARK 500    LEU A 289       72.67    -69.03                                   
REMARK 500    ASP A 339      -11.96    133.01                                   
REMARK 500    GLU A 344       23.21    -74.14                                   
REMARK 500    LYS A 358      -77.44    -52.69                                   
REMARK 500    GLU A 359      -62.89    -27.91                                   
REMARK 500    MET A 361      -73.62    -54.01                                   
REMARK 500    ASP A 362       27.08    -64.70                                   
REMARK 500    ASN B   8     -133.82   -107.83                                   
REMARK 500    ASN B  28      -54.62     81.91                                   
REMARK 500    LEU B  29      -80.41     60.26                                   
REMARK 500    LYS B  30      105.51     42.62                                   
REMARK 500    ILE B  47      -74.24    -66.20                                   
REMARK 500    LEU B  89      -60.34   -100.14                                   
REMARK 500    PHE B 101      132.99    -37.28                                   
REMARK 500    GLN B 102      -32.86   -156.30                                   
REMARK 500    SER B 144        1.30    -65.08                                   
REMARK 500    ARG B 150       -6.68     66.21                                   
REMARK 500    ASP B 169       93.12     61.31                                   
REMARK 500    GLU B 183       55.60     36.50                                   
REMARK 500    PRO B 184      -19.34    -49.95                                   
REMARK 500    PRO B 226     -108.20    -57.87                                   
REMARK 500    SER B 284     -111.38    -84.14                                   
REMARK 500    GLU B 285       87.62   -173.37                                   
REMARK 500    HIS B 286       67.06   -156.61                                   
REMARK 500    ASN B 287      -75.87     11.03                                   
REMARK 500    LYS B 288      -83.69    -25.13                                   
REMARK 500    ASN B 322      -37.60    -39.99                                   
REMARK 500    PRO B 327      -36.00    -33.63                                   
REMARK 500    GLU B 331       76.19   -178.43                                   
REMARK 500    PRO B 338      -72.90    -38.47                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.                        
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 46A A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 46A B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 802                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3O17   RELATED DB: PDB                                   
REMARK 900 APO JNK1-ALPHA1 ISOFORM                                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHORS SEQUENCE MATCHES WITH SEQUENCE PUBLISHED BY HEO ET AL.       
REMARK 999 (2004) EMBO JOURNAL VOL. 23, 2185-2195 AND SUPPLEMENTAL INFORMATION  
DBREF  3O2M A    1   364  UNP    P45983   MK08_HUMAN       1    364             
DBREF  3O2M F  554   563  UNP    Q9WVI9   JIP1_MOUSE     154    163             
DBREF  3O2M B    1   364  UNP    P45983   MK08_HUMAN       1    364             
DBREF  3O2M G  554   563  UNP    Q9WVI9   JIP1_MOUSE     154    163             
SEQADV 3O2M GLU A  183  UNP  P45983    THR   183 ENGINEERED MUTATION            
SEQADV 3O2M GLU A  185  UNP  P45983    TYR   185 ENGINEERED MUTATION            
SEQADV 3O2M ILE A  208  UNP  P45983    LEU   208 VARIANT                        
SEQADV 3O2M ALA A  247  UNP  P45983    GLU   247 SEE REMARK 999                 
SEQADV 3O2M ASN A  258  UNP  P45983    THR   258 SEE REMARK 999                 
SEQADV 3O2M HIS A  365  UNP  P45983              EXPRESSION TAG                 
SEQADV 3O2M HIS A  366  UNP  P45983              EXPRESSION TAG                 
SEQADV 3O2M HIS A  367  UNP  P45983              EXPRESSION TAG                 
SEQADV 3O2M HIS A  368  UNP  P45983              EXPRESSION TAG                 
SEQADV 3O2M HIS A  369  UNP  P45983              EXPRESSION TAG                 
SEQADV 3O2M HIS A  370  UNP  P45983              EXPRESSION TAG                 
SEQADV 3O2M GLU B  183  UNP  P45983    THR   183 ENGINEERED MUTATION            
SEQADV 3O2M GLU B  185  UNP  P45983    TYR   185 ENGINEERED MUTATION            
SEQADV 3O2M ILE B  208  UNP  P45983    LEU   208 VARIANT                        
SEQADV 3O2M ALA B  247  UNP  P45983    GLU   247 SEE REMARK 999                 
SEQADV 3O2M ASN B  258  UNP  P45983    THR   258 SEE REMARK 999                 
SEQADV 3O2M HIS B  365  UNP  P45983              EXPRESSION TAG                 
SEQADV 3O2M HIS B  366  UNP  P45983              EXPRESSION TAG                 
SEQADV 3O2M HIS B  367  UNP  P45983              EXPRESSION TAG                 
SEQADV 3O2M HIS B  368  UNP  P45983              EXPRESSION TAG                 
SEQADV 3O2M HIS B  369  UNP  P45983              EXPRESSION TAG                 
SEQADV 3O2M HIS B  370  UNP  P45983              EXPRESSION TAG                 
SEQRES   1 A  370  MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL          
SEQRES   2 A  370  GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR          
SEQRES   3 A  370  GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE          
SEQRES   4 A  370  VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL          
SEQRES   5 A  370  ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR          
SEQRES   6 A  370  HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS          
SEQRES   7 A  370  CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL          
SEQRES   8 A  370  PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL          
SEQRES   9 A  370  TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN          
SEQRES  10 A  370  VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR          
SEQRES  11 A  370  LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS          
SEQRES  12 A  370  SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN          
SEQRES  13 A  370  ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP          
SEQRES  14 A  370  PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET          
SEQRES  15 A  370  GLU PRO GLU VAL VAL THR ARG TYR TYR ARG ALA PRO GLU          
SEQRES  16 A  370  VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP ILE          
SEQRES  17 A  370  TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL CYS HIS          
SEQRES  18 A  370  LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP          
SEQRES  19 A  370  ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO ALA          
SEQRES  20 A  370  PHE MET LYS LYS LEU GLN PRO THR VAL ARG ASN TYR VAL          
SEQRES  21 A  370  GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS          
SEQRES  22 A  370  LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS          
SEQRES  23 A  370  ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER          
SEQRES  24 A  370  LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL          
SEQRES  25 A  370  ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR          
SEQRES  26 A  370  ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO          
SEQRES  27 A  370  ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU          
SEQRES  28 A  370  TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU GLU          
SEQRES  29 A  370  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 F   10  PRO LYS ARG PRO THR THR LEU ASN LEU PHE                      
SEQRES   1 B  370  MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL          
SEQRES   2 B  370  GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR          
SEQRES   3 B  370  GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE          
SEQRES   4 B  370  VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL          
SEQRES   5 B  370  ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR          
SEQRES   6 B  370  HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS          
SEQRES   7 B  370  CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL          
SEQRES   8 B  370  PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL          
SEQRES   9 B  370  TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN          
SEQRES  10 B  370  VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR          
SEQRES  11 B  370  LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS          
SEQRES  12 B  370  SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN          
SEQRES  13 B  370  ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP          
SEQRES  14 B  370  PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET          
SEQRES  15 B  370  GLU PRO GLU VAL VAL THR ARG TYR TYR ARG ALA PRO GLU          
SEQRES  16 B  370  VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP ILE          
SEQRES  17 B  370  TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL CYS HIS          
SEQRES  18 B  370  LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP          
SEQRES  19 B  370  ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO ALA          
SEQRES  20 B  370  PHE MET LYS LYS LEU GLN PRO THR VAL ARG ASN TYR VAL          
SEQRES  21 B  370  GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS          
SEQRES  22 B  370  LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS          
SEQRES  23 B  370  ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER          
SEQRES  24 B  370  LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL          
SEQRES  25 B  370  ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR          
SEQRES  26 B  370  ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO          
SEQRES  27 B  370  ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU          
SEQRES  28 B  370  TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU GLU          
SEQRES  29 B  370  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 G   10  PRO LYS ARG PRO THR THR LEU ASN LEU PHE                      
HET    46A  A 701      31                                                       
HET    46A  B 701      31                                                       
HET    SO4  A 801       5                                                       
HET    SO4  A 802       5                                                       
HET    SO4  B 801       5                                                       
HET    SO4  B 802       5                                                       
HETNAM     46A N-BUTYL-4,6-DIMETHYL-N-{[2'-(2H-TETRAZOL-5-YL)BIPHENYL-          
HETNAM   2 46A  4-YL]METHYL}PYRIMIDIN-2-AMINE                                   
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  46A    2(C24 H27 N7)                                                
FORMUL   7  SO4    4(O4 S 2-)                                                   
HELIX    1   1 ASN A   63  VAL A   80  1                                  18    
HELIX    2   2 LEU A  115  ILE A  119  1                                   5    
HELIX    3   3 ASP A  124  SER A  144  1                                  21    
HELIX    4   4 GLU A  183  VAL A  187  5                                   5    
HELIX    5   5 THR A  188  ARG A  192  5                                   5    
HELIX    6   6 ALA A  193  LEU A  198  1                                   6    
HELIX    7   7 ASN A  205  HIS A  221  1                                  17    
HELIX    8   8 ILE A  231  GLY A  242  1                                  12    
HELIX    9   9 CYS A  245  LYS A  250  1                                   6    
HELIX   10  10 GLN A  253  ASN A  262  1                                  10    
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 LYS A  290  LEU A  302  1                                  13    
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  ASP A  362  1                                  15    
HELIX   18  18 ASN B   63  VAL B   80  1                                  18    
HELIX   19  19 LEU B  115  GLN B  120  1                                   6    
HELIX   20  20 ASP B  124  SER B  144  1                                  21    
HELIX   21  21 LYS B  153  SER B  155  5                                   3    
HELIX   22  22 GLU B  183  VAL B  187  5                                   5    
HELIX   23  23 THR B  188  ARG B  192  5                                   5    
HELIX   24  24 ALA B  193  LEU B  198  1                                   6    
HELIX   25  25 ASN B  205  HIS B  221  1                                  17    
HELIX   26  26 ILE B  231  GLY B  242  1                                  12    
HELIX   27  27 CYS B  245  LYS B  250  1                                   6    
HELIX   28  28 GLN B  253  ASN B  262  1                                  10    
HELIX   29  29 SER B  270  PHE B  275  1                                   6    
HELIX   30  30 PRO B  276  PHE B  280  5                                   5    
HELIX   31  31 LYS B  290  LEU B  302  1                                  13    
HELIX   32  32 ASP B  305  ARG B  309  5                                   5    
HELIX   33  33 SER B  311  GLN B  317  1                                   7    
HELIX   34  34 HIS B  318  VAL B  323  1                                   6    
HELIX   35  35 ASP B  326  GLU B  331  1                                   6    
HELIX   36  36 ASP B  339  GLU B  344  5                                   6    
HELIX   37  37 THR B  348  ASP B  362  1                                  15    
SHEET    1   A 2 PHE A  10  ILE A  15  0                                        
SHEET    2   A 2 SER A  18  LEU A  23 -1  O  SER A  18   N  ILE A  15           
SHEET    1   B 3 TYR A  26  GLN A  27  0                                        
SHEET    2   B 3 GLY A  38  ASP A  45 -1  O  TYR A  44   N  GLN A  27           
SHEET    3   B 3 PRO A  31  GLY A  35 -1  N  GLY A  33   O  VAL A  40           
SHEET    1   C 5 TYR A  26  GLN A  27  0                                        
SHEET    2   C 5 GLY A  38  ASP A  45 -1  O  TYR A  44   N  GLN A  27           
SHEET    3   C 5 ARG A  50  LYS A  56 -1  O  ILE A  54   N  CYS A  41           
SHEET    4   C 5 TYR A 105  GLU A 109 -1  O  ILE A 106   N  LYS A  55           
SHEET    5   C 5 LEU A  88  PHE A  92 -1  N  ASN A  90   O  VAL A 107           
SHEET    1   D 3 ALA A 113  ASN A 114  0                                        
SHEET    2   D 3 ILE A 157  VAL A 159 -1  O  VAL A 159   N  ALA A 113           
SHEET    3   D 3 LEU A 165  ILE A 167 -1  O  LYS A 166   N  VAL A 158           
SHEET    1   E 2 ILE A 147  ILE A 148  0                                        
SHEET    2   E 2 ARG A 174  THR A 175 -1  O  ARG A 174   N  ILE A 148           
SHEET    1   F 2 PHE B  10  ILE B  15  0                                        
SHEET    2   F 2 SER B  18  LEU B  23 -1  O  VAL B  22   N  TYR B  11           
SHEET    1   G 3 TYR B  26  GLN B  27  0                                        
SHEET    2   G 3 GLY B  38  ASP B  45 -1  O  TYR B  44   N  GLN B  27           
SHEET    3   G 3 PRO B  31  GLY B  35 -1  N  GLY B  33   O  VAL B  40           
SHEET    1   H 5 TYR B  26  GLN B  27  0                                        
SHEET    2   H 5 GLY B  38  ASP B  45 -1  O  TYR B  44   N  GLN B  27           
SHEET    3   H 5 ARG B  50  LYS B  56 -1  O  VAL B  52   N  ALA B  43           
SHEET    4   H 5 TYR B 105  GLU B 109 -1  O  MET B 108   N  ALA B  53           
SHEET    5   H 5 LEU B  88  PHE B  92 -1  N  ASN B  90   O  VAL B 107           
SHEET    1   I 3 ALA B 113  ASN B 114  0                                        
SHEET    2   I 3 ILE B 157  VAL B 159 -1  O  VAL B 159   N  ALA B 113           
SHEET    3   I 3 LEU B 165  ILE B 167 -1  O  LYS B 166   N  VAL B 158           
SITE     1 AC1 12 PHE A 180  ILE A 197  LEU A 198  GLY A 199                    
SITE     2 AC1 12 TYR A 230  ILE A 231  GLN A 253  THR A 255                    
SITE     3 AC1 12 VAL A 256  PRO B 184  THR B 255  46A B 701                    
SITE     1 AC2 11 PRO A 184  VAL A 256  46A A 701  PHE B 180                    
SITE     2 AC2 11 ILE B 197  GLY B 199  TYR B 230  ILE B 231                    
SITE     3 AC2 11 GLN B 253  THR B 255  VAL B 256                               
SITE     1 AC3  5 ARG A 189  ARG A 192  TYR A 230  THR B 255                    
SITE     2 AC3  5 ASN B 258                                                     
SITE     1 AC4  5 LYS A  68  ARG A  69  ARG A  72  ARG A 150                    
SITE     2 AC4  5 MET A 181                                                     
SITE     1 AC5  4 THR A 255  ARG B 189  ARG B 192  TYR B 230                    
SITE     1 AC6  6 LYS B  68  ARG B  69  ARG B  72  ARG B 150                    
SITE     2 AC6  6 ARG B 174  MET B 181                                          
CRYST1  158.379  158.379  123.959  90.00  90.00 120.00 P 32 2 1     12          
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      0.006314  0.003645  0.000000        0.00000                         
SCALE2      0.000000  0.007291  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008067        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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