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Database: PDB
Entry: 2NO3
LinkDB: 2NO3
Original site: 2NO3 
HEADER    SIGNALING PROTEIN/INHIBITOR             24-OCT-06   2NO3              
TITLE     NOVEL 4-ANILINOPYRIMIDINES AS POTENT JNK1 INHIBITORS                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: JNK1 RESIDUES 1-364;                                       
COMPND   5 SYNONYM: STRESS-ACTIVATED PROTEIN KINASE JNK1, C-JUN N-TERMINAL      
COMPND   6 KINASE 1, JNK-46;                                                    
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;         
COMPND  12 CHAIN: F, G;                                                         
COMPND  13 FRAGMENT: PEPJIP1 PEPTIDE;                                           
COMPND  14 SYNONYM: JNK-INTERACTING PROTEIN 1, JIP-1, JNK MAP KINASE SCAFFOLD   
COMPND  15 PROTEIN 1, ISLET-BRAIN 1, IB-1, MITOGEN-ACTIVATED PROTEIN KINASE 8-  
COMPND  16 INTERACTING PROTEIN 1;                                               
COMPND  17 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: MAPK8, JNK1, PRKM8;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 OTHER_DETAILS: THE SEQUENCE IS FOUND NATURALLY IN HOMO SAPIENS       
KEYWDS    JNK1, C-JUN N-TERMINAL KINASE, JNK1 INHIBITORS, ANILINOPYRIMIDINES    
KEYWDS   2 JNK1 INHIBITORS, SIGNALING PROTEIN-INHIBITOR COMPLEX                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.ABAD-ZAPATERO                                                       
REVDAT   5   30-AUG-23 2NO3    1       REMARK                                   
REVDAT   4   20-OCT-21 2NO3    1       REMARK SEQADV                            
REVDAT   3   18-OCT-17 2NO3    1       REMARK                                   
REVDAT   2   24-FEB-09 2NO3    1       VERSN                                    
REVDAT   1   17-APR-07 2NO3    0                                                
JRNL        AUTH   M.LIU,S.WANG,J.E.CLAMPIT,R.J.GUM,D.L.HAASCH,C.M.RONDINONE,   
JRNL        AUTH 2 J.M.TREVILLYAN,C.ABAD-ZAPATERO,E.H.FRY,H.L.SHAM,G.LIU        
JRNL        TITL   DISCOVERY OF A NEW CLASS OF 4-ANILINOPYRIMIDINES AS POTENT   
JRNL        TITL 2 C-JUN N-TERMINAL KINASE INHIBITORS: SYNTHESIS AND SAR        
JRNL        TITL 3 STUDIES.                                                     
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  17   668 2007              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   17107797                                                     
JRNL        DOI    10.1016/J.BMCL.2006.10.093                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.LIU,Z.XIN,J.E.CLAMPIT,S.WANG,R.J.GUM,D.L.HAASCH,           
REMARK   1  AUTH 2 J.M.TREVILLYAN,C.ABAD-ZAPATERO,E.H.FRY,H.L.SHAM              
REMARK   1  TITL   SYNTHESIS AND SAR OF                                         
REMARK   1  TITL 2 1,9-DIHYDRO-9-HYDROXYPYRAZOLO[3,4-B]QUINOLIN-4-ONES AS       
REMARK   1  TITL 3 NOVEL, SELECTIVE C-JUN N-TERMINAL KINASE INHIBITORS.         
REMARK   1  REF    BIOORG.MED.CHEM.LETT.         V.  16  2590 2006              
REMARK   1  REFN                   ISSN 0960-894X                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   B.G.SZCZEPANKIEWICZ,C.KOSOGOF,L.T.J.NELSON,G.LIU,H.ZHAO,     
REMARK   1  AUTH 2 M.D.SERBY,Z.XIN,B.LIU,R.J.GUM,D.HAASCH                       
REMARK   1  TITL   SELECTIVE AMINOPYRIDINE-BASED C-JUN N-TERMINAL KINASE        
REMARK   1  TITL 2 INHIBITORS WITH CELLULAR ACTIVIY                             
REMARK   1  REF    J.MED.CHEM.                   V.  49  3563 2006              
REMARK   1  REFN                   ISSN 0022-2623                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   H.ZHAO,M.D.SERBY,Z.XIN,B.G.SZCZEPANKIEWICZ,M.LIU,C.KOSOGOF,  
REMARK   1  AUTH 2 B.LIU,R.J.GUM,J.E.CLAMPIT,D.L.HAASCH                         
REMARK   1  TITL   DISCOVERY OF POTENT, HIGHLY SELECTIVE AND ORALLY             
REMARK   1  TITL 2 BIOAVAILABLE PYRIDINE CARBOXAMIDE C-JUN NH2-TERMINAL KINASE  
REMARK   1  TITL 3 INHIBITORS                                                   
REMARK   1  REF    J.MED.CHEM.                   V.  49  4455 2006              
REMARK   1  REFN                   ISSN 0022-2623                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2002                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 162862.680                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 75.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 22039                          
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2180                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : NULL                 
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.31                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 45.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1163                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780                       
REMARK   3   BIN FREE R VALUE                    : 0.3350                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 11.60                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 153                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5897                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.93000                                              
REMARK   3    B22 (A**2) : 7.93000                                              
REMARK   3    B33 (A**2) : -15.87000                                            
REMARK   3    B12 (A**2) : 22.73000                                             
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) : 0.35                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.34                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 8.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.48                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.44                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.830                           
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        : 0.22                                                 
REMARK   3   BSOL        : 24.18                                                
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  : ACCELRYS_CNX_TOPPAR:PROTEIN_REP.PARAM          
REMARK   3  PARAMETER FILE  2  : GCR.PAR                                        
REMARK   3  PARAMETER FILE  3  : ACCELRYS_CNX_TOPPAR:ION.PARAM                  
REMARK   3  PARAMETER FILE  4  : 859.PAR                                        
REMARK   3  PARAMETER FILE  5  : SO4.PAR                                        
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : GCR.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : ACCELRYS_CNX_TOPPAR:ION.PARAM                  
REMARK   3  TOPOLOGY FILE  4   : 859.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : SO4.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2NO3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000040098.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JAN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 6.20                               
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 RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27814                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.81200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNX                                                   
REMARK 200 STARTING MODEL: ENTRY 2H96                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS PREINCUBATED WITH THE JIP1   
REMARK 280  PEPTIDE AT A 5X MOLAR EXCESS. PROTEIN CONCENTRATION 9- 12.6 MG/     
REMARK 280  ML. HANGING DROPS CONSISTED OF 2UL PROTEIN PLUS 2 UL WELL           
REMARK 280  SOLUTION. WELL SOLUTION:2.8-3.1 M AMMONIUM SULFATE, 10- 14%         
REMARK 280  GLYCEROL. FOR CO-CRYSTALLIZATION EXPERIMENT WITH THE COMPOUND,      
REMARK 280  THE COMPOUND WAS DISSOLVED IN DMSO AT 100 MM CONCENTRATION.         
REMARK 280  ALLOW TO INCUBATE FOR AT LEAST AN HOUR ON ICE. SOLUTION WAS SPUN    
REMARK 280  FOR 5 MINUTES AT 2000G PRIOR TO SETTING UP FOR CRYSTALLIZATION.,    
REMARK 280  PH 6.20, VAPOR DIFFUSION, TEMPERATURE 277.0K                        
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       82.24133            
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       41.12067            
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       41.12067            
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       82.24133            
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 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: 2280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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: 2410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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: 6040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 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     ASP A     7                                                      
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     ARG F   553                                                      
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     GLU B   364                                                      
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 465     ARG G   553                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  24    CG   CD   CE   NZ                                   
REMARK 470     LYS A  68    CG   CD   CE   NZ                                   
REMARK 470     GLU A 185    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 346    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 358    CG   CD   CE   NZ                                   
REMARK 470     LYS B  24    CG   CD   CE   NZ                                   
REMARK 470     ARG B  69    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 174    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 183    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 185    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 358    CG   CD   CE   NZ                                   
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    PRO A 319   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    PRO B 333   C   -  N   -  CA  ANGL. DEV. =   9.8 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    PHE A  10     -172.58    -65.30                                   
REMARK 500    TYR A  11     -155.19   -165.43                                   
REMARK 500    ILE A  15       74.13   -109.26                                   
REMARK 500    ASP A  17       25.04    -70.16                                   
REMARK 500    LYS A  24      -18.53    -49.20                                   
REMARK 500    ASN A  28       81.73     48.07                                   
REMARK 500    LYS A  30      136.07   -170.73                                   
REMARK 500    ILE A  32       -6.50   -149.69                                   
REMARK 500    SER A  34       77.05   -105.73                                   
REMARK 500    GLU A  49       46.12     70.08                                   
REMARK 500    ARG A  59       78.16     36.57                                   
REMARK 500    PRO A  60      -19.52    -45.54                                   
REMARK 500    PHE A  61       27.41   -156.38                                   
REMARK 500    GLN A  62      -84.82    -44.04                                   
REMARK 500    GLN A  64       -6.98    -57.08                                   
REMARK 500    ALA A  67      -72.90    -68.00                                   
REMARK 500    LYS A  68      -35.90    -31.85                                   
REMARK 500    LEU A  74      -74.91    -47.01                                   
REMARK 500    CYS A  79       -0.96    -59.34                                   
REMARK 500    ILE A  86      112.64    -21.77                                   
REMARK 500    PHE A  92     -153.30   -166.66                                   
REMARK 500    THR A  93      125.51   -175.85                                   
REMARK 500    LEU A  98      -74.88    -29.65                                   
REMARK 500    GLN A 102        7.65    179.59                                   
REMARK 500    GLU A 109     -173.89    -55.57                                   
REMARK 500    ARG A 127      -71.89    -56.18                                   
REMARK 500    SER A 144       -6.96    -59.03                                   
REMARK 500    ARG A 150      -24.17     61.32                                   
REMARK 500    LYS A 153      161.25    175.67                                   
REMARK 500    SER A 155      -28.67    -38.09                                   
REMARK 500    ASP A 169      137.69     75.82                                   
REMARK 500    ALA A 176      -87.11     19.82                                   
REMARK 500    THR A 178      -40.44    -23.92                                   
REMARK 500    SER A 179     -132.92   -167.15                                   
REMARK 500    PHE A 180       42.37   -103.23                                   
REMARK 500    MET A 181     -156.62     45.79                                   
REMARK 500    ARG A 189      -87.31    -32.85                                   
REMARK 500    TYR A 190      -22.20    -29.44                                   
REMARK 500    ASN A 205       -2.88    -55.22                                   
REMARK 500    HIS A 221       11.35     80.99                                   
REMARK 500    LEU A 224      -71.34    -65.70                                   
REMARK 500    PHE A 225       75.86   -106.24                                   
REMARK 500    PRO A 226     -129.94    -43.55                                   
REMARK 500    ASP A 277      -41.35    -27.63                                   
REMARK 500    SER A 284     -112.87   -106.26                                   
REMARK 500    GLU A 285      -16.71   -141.93                                   
REMARK 500    ILE A 310      119.23    -28.32                                   
REMARK 500    PRO A 319      -20.77    -36.87                                   
REMARK 500    VAL A 323       -1.30    -56.45                                   
REMARK 500    ASP A 326      111.56   -160.43                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     122 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 SO4 A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 859 A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 859 B 902                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2G01   RELATED DB: PDB                                   
REMARK 900 PYRAZOLOQUINOLONES AS NOVEL, SELECTIVE JNK1 INHIBITORS               
REMARK 900 RELATED ID: 2GMX   RELATED DB: PDB                                   
REMARK 900 SELECTIVE AMINOPYRIDINE-BASED C-JUN N-TERMINAL KINASE INHIBITORS     
REMARK 900 WITH CELLULAR ACTIVITY                                               
REMARK 900 RELATED ID: 2H96   RELATED DB: PDB                                   
REMARK 900 HIGHLY SELECTIVE AND ORALLY BIOAVAILABLE PYRIDINE CARBOXAMIDE JNK1   
REMARK 900 INHIHIBITORS                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE NATIVE, UNMUTATED SEQUENCE IS THE SAME AS                        
REMARK 999 THE P45983-2 ISOFORM.   THE INTRODUCED MUTATIONS                     
REMARK 999 (THR183>GLU, TYR185>GLU) ARE INTENDED TO MIMIC                       
REMARK 999 THE ACTIVATED FORM OF THE KINASE UPON                                
REMARK 999 PHOSPHORYLATION OF THOSE TWO RESIDUES.                               
DBREF  2NO3 A    1   364  UNP    P45983   MK08_HUMAN       1    364             
DBREF  2NO3 B    1   364  UNP    P45983   MK08_HUMAN       1    364             
DBREF  2NO3 F  553   563  PDB    2NO3     2NO3           553    563             
DBREF  2NO3 G  553   563  PDB    2NO3     2NO3           553    563             
SEQADV 2NO3 GLU A  183  UNP  P45983    THR   183 ENGINEERED MUTATION            
SEQADV 2NO3 GLU A  185  UNP  P45983    TYR   185 ENGINEERED MUTATION            
SEQADV 2NO3 HIS A  365  UNP  P45983              EXPRESSION TAG                 
SEQADV 2NO3 HIS A  366  UNP  P45983              EXPRESSION TAG                 
SEQADV 2NO3 HIS A  367  UNP  P45983              EXPRESSION TAG                 
SEQADV 2NO3 HIS A  368  UNP  P45983              EXPRESSION TAG                 
SEQADV 2NO3 HIS A  369  UNP  P45983              EXPRESSION TAG                 
SEQADV 2NO3 HIS A  370  UNP  P45983              EXPRESSION TAG                 
SEQADV 2NO3 GLU B  183  UNP  P45983    THR   183 ENGINEERED MUTATION            
SEQADV 2NO3 GLU B  185  UNP  P45983    TYR   185 ENGINEERED MUTATION            
SEQADV 2NO3 HIS B  365  UNP  P45983              EXPRESSION TAG                 
SEQADV 2NO3 HIS B  366  UNP  P45983              EXPRESSION TAG                 
SEQADV 2NO3 HIS B  367  UNP  P45983              EXPRESSION TAG                 
SEQADV 2NO3 HIS B  368  UNP  P45983              EXPRESSION TAG                 
SEQADV 2NO3 HIS B  369  UNP  P45983              EXPRESSION TAG                 
SEQADV 2NO3 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 LEU          
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 GLU          
SEQRES  20 A  370  PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR 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   11  ARG 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 LEU          
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 GLU          
SEQRES  20 B  370  PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR 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   11  ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE                  
HET    SO4  A 701       5                                                       
HET    SO4  A 702       5                                                       
HET    859  A 901      24                                                       
HET    SO4  B 801       5                                                       
HET    SO4  B 802       5                                                       
HET    859  B 902      24                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     859 2-({2-[(3-HYDROXYPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)              
HETNAM   2 859  BENZAMIDE                                                       
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   7  859    2(C17 H15 N5 O2)                                             
HELIX    1   1 ASN A   63  VAL A   80  1                                  18    
HELIX    2   2 LEU A  115  GLN A  120  1                                   6    
HELIX    3   3 ASP A  124  SER A  144  1                                  21    
HELIX    4   4 LYS A  153  SER A  155  5                                   3    
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  251  1                                   7    
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 ASP A  305  ARG A  309  5                                   5    
HELIX   15  15 SER A  311  HIS A  318  1                                   8    
HELIX   16  16 ILE A  321  TYR A  325  5                                   5    
HELIX   17  17 ASP A  326  GLU A  331  1                                   6    
HELIX   18  18 THR A  348  MET A  361  1                                  14    
HELIX   19  19 ASP A  362  GLU A  364  5                                   3    
HELIX   20  20 THR B   65  VAL B   80  1                                  16    
HELIX   21  21 ASN B  114  GLN B  120  1                                   7    
HELIX   22  22 ASP B  124  SER B  144  1                                  21    
HELIX   23  23 LYS B  153  SER B  155  5                                   3    
HELIX   24  24 THR B  188  ARG B  192  5                                   5    
HELIX   25  25 ALA B  193  LEU B  198  1                                   6    
HELIX   26  26 GLU B  204  HIS B  221  1                                  18    
HELIX   27  27 ILE B  231  GLY B  242  1                                  12    
HELIX   28  28 CYS B  245  LYS B  250  1                                   6    
HELIX   29  29 GLN B  253  ARG B  263  1                                  11    
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 SER B  311  GLN B  317  1                                   7    
HELIX   33  33 HIS B  318  VAL B  323  1                                   6    
HELIX   34  34 ILE B  349  VAL B  360  1                                  12    
SHEET    1   A 2 VAL A  13  GLU A  14  0                                        
SHEET    2   A 2 THR A  19  PHE A  20 -1  O  PHE A  20   N  VAL A  13           
SHEET    1   B 3 TYR A  26  GLN A  27  0                                        
SHEET    2   B 3 ILE A  39  ASP A  45 -1  O  TYR A  44   N  GLN A  27           
SHEET    3   B 3 PRO A  31  SER A  34 -1  N  GLY A  33   O  VAL A  40           
SHEET    1   C 5 TYR A  26  GLN A  27  0                                        
SHEET    2   C 5 ILE A  39  ASP A  45 -1  O  TYR A  44   N  GLN A  27           
SHEET    3   C 5 ARG A  50  LEU A  57 -1  O  VAL A  52   N  ALA A  43           
SHEET    4   C 5 VAL A 104  MET A 108 -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 5 TYR B  26  GLY B  33  0                                        
SHEET    2   F 5 ILE B  39  ASP B  45 -1  O  VAL B  40   N  GLY B  33           
SHEET    3   F 5 ARG B  50  LEU B  57 -1  O  ILE B  54   N  CYS B  41           
SHEET    4   F 5 VAL B 104  GLU B 109 -1  O  MET B 108   N  ALA B  53           
SHEET    5   F 5 LEU B  88  PHE B  92 -1  N  ASN B  90   O  VAL B 107           
SHEET    1   G 2 ILE B 157  VAL B 158  0                                        
SHEET    2   G 2 LYS B 166  ILE B 167 -1  O  LYS B 166   N  VAL B 158           
SITE     1 AC1  4 ARG A 189  ARG A 192  TYR A 230  THR B 255                    
SITE     1 AC2  2 ARG A  69  ARG A 150                                          
SITE     1 AC3  4 THR A 255  ARG B 189  ARG B 192  TYR B 230                    
SITE     1 AC4  3 LYS B  68  ARG B 150  MET B 182                               
SITE     1 AC5 11 GLY A  33  VAL A  40  LYS A  55  MET A 108                    
SITE     2 AC5 11 GLU A 109  LEU A 110  MET A 111  ASP A 112                    
SITE     3 AC5 11 ASN A 114  LEU A 168  ASP A 169                               
SITE     1 AC6 14 ARG A  50  ILE B  32  GLY B  33  VAL B  40                    
SITE     2 AC6 14 ILE B  86  MET B 108  GLU B 109  LEU B 110                    
SITE     3 AC6 14 MET B 111  ASP B 112  ALA B 113  ASN B 114                    
SITE     4 AC6 14 VAL B 158  LEU B 168                                          
CRYST1  157.201  157.201  123.362  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      0.006361  0.003673  0.000000        0.00000                         
SCALE2      0.000000  0.007345  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008106        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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