GenomeNet

Database: PDB
Entry: 3V3V
LinkDB: 3V3V
Original site: 3V3V 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       14-DEC-11   3V3V              
TITLE     STRUCTURAL AND FUNCTIONAL ANALYSIS OF QUERCETAGETIN, A NATURAL JNK1   
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-363;                                        
COMPND   5 SYNONYM: MAP KINASE 8, MAPK 8, JNK-46, STRESS-ACTIVATED PROTEIN      
COMPND   6 KINASE 1C, SAPK1C, STRESS-ACTIVATED PROTEIN KINASE JNK1, C-JUN N-    
COMPND   7 TERMINAL KINASE 1;                                                   
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 1;         
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: UNP RESIDUES 153-163;                                      
COMPND  14 SYNONYM: JIP-1, JNK-INTERACTING PROTEIN 1, ISLET-BRAIN-1, IB-1, JNK  
COMPND  15 MAP KINASE SCAFFOLD PROTEIN 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, SAPK1, SAPK1C;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-21B;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 OTHER_DETAILS: FMOC SYNTHESIS                                        
KEYWDS    TRANSFERASE, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE INHIBITOR       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BAEK,N.J.KANG,G.M.POPOWICZ,M.ARCINIEGA,S.K.JUNG,S.BYUN,N.R.SONG,    
AUTHOR   2 Y.S.HEO,B.Y.KIM,H.J.LEE,T.A.HOLAK,M.AUGUSTIN,A.M.BODE,R.HUBER,       
AUTHOR   3 Z.DONG,K.W.LEE                                                       
REVDAT   2   30-JAN-13 3V3V    1       JRNL                                     
REVDAT   1   05-DEC-12 3V3V    0                                                
JRNL        AUTH   S.BAEK,N.J.KANG,G.M.POPOWICZ,M.ARCINIEGA,S.K.JUNG,S.BYUN,    
JRNL        AUTH 2 N.R.SONG,Y.S.HEO,B.Y.KIM,H.J.LEE,T.A.HOLAK,M.AUGUSTIN,       
JRNL        AUTH 3 A.M.BODE,R.HUBER,Z.DONG,K.W.LEE                              
JRNL        TITL   STRUCTURAL AND FUNCTIONAL ANALYSIS OF THE NATURAL JNK1       
JRNL        TITL 2 INHIBITOR QUERCETAGETIN.                                     
JRNL        REF    J.MOL.BIOL.                   V. 425   411 2013              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   23142567                                                     
JRNL        DOI    10.1016/J.JMB.2012.10.019                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 77.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 13278                          
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) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 611                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 521                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 42.44                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5040                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 26                           
REMARK   3   BIN FREE R VALUE                    : 0.5050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2866                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 27                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.71000                                             
REMARK   3    B22 (A**2) : -0.71000                                             
REMARK   3    B33 (A**2) : 1.42000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.961         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.374         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.318         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.648        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2981 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4044 ; 1.456 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   357 ; 6.653 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   129 ;38.697 ;24.496       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   520 ;21.683 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;21.871 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   444 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2209 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1804 ; 0.606 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2923 ; 1.144 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1177 ; 1.261 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1121 ; 2.169 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3V3V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB069561.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MONOCHROMATOR AND MIRROR           
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13950                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.0                               
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) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 43.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.980                              
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: 1UKH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1M AMMONIUM SULFATE  0.1M BIS-TRIS,    
REMARK 280  PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       86.18500            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       86.18500            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       43.02000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       86.18500            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       86.18500            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       43.02000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       86.18500            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       86.18500            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       43.02000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       86.18500            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       86.18500            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       43.02000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       86.18500            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       86.18500            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       43.02000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       86.18500            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       86.18500            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       43.02000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       86.18500            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       86.18500            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       43.02000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       86.18500            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       86.18500            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       43.02000            
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: 3080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -226.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC              
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 40190 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 120230 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1094.0 KCAL/MOL                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   8  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     PHE A   180                                                      
REMARK 465     MET A   181                                                      
REMARK 465     MET A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     ASN A   287                                                      
REMARK 465     ALA A   288                                                      
REMARK 465     PRO A   364                                                      
REMARK 465     LYS A   365                                                      
REMARK 465     ARG A   366                                                      
REMARK 465     PRO A   367                                                      
REMARK 465     THR A   368                                                      
REMARK 465     THR A   369                                                      
REMARK 465     LEU A   370                                                      
REMARK 465     ASN A   371                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     PHE A   373                                                      
REMARK 465     HIS A   374                                                      
REMARK 465     HIS A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     HIS A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     HIS A   379                                                      
REMARK 465     ARG B   153                                                      
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     ILE A  15    CD1                                                 
REMARK 470     LYS A  30    CE   NZ                                             
REMARK 470     ALA A  36    CB                                                  
REMARK 470     GLN A  37    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  96    CD   CE   NZ                                        
REMARK 470     HIS A 286    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 336    CD   CE   NZ                                        
REMARK 470     LEU A 342    CG   CD1  CD2                                       
REMARK 470     ASP A 343    CG   OD1  OD2                                       
REMARK 470     GLU A 344    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 345    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 346    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH1  ARG A   189     O1   SO4 A   405     5555     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 319   C   -  N   -  CA  ANGL. DEV. =   9.6 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        4.94    -60.14                                   
REMARK 500    ILE A  32      -56.29   -120.70                                   
REMARK 500    SER A  34      -42.60   -177.08                                   
REMARK 500    ALA A  36       -8.66   -168.60                                   
REMARK 500    ARG A  59       55.41     28.52                                   
REMARK 500    ASN A  90      147.21   -175.69                                   
REMARK 500    LEU A  98      -39.92    -34.06                                   
REMARK 500    GLN A 102      -66.56   -124.72                                   
REMARK 500    GLN A 120        1.77    -66.88                                   
REMARK 500    ARG A 150      -25.09     75.22                                   
REMARK 500    ASP A 151       55.54   -144.78                                   
REMARK 500    ASP A 169       90.19     52.69                                   
REMARK 500    ALA A 176      151.30    -45.54                                   
REMARK 500    LEU A 198     -166.85    -78.44                                   
REMARK 500    ASN A 205       -2.36    -57.59                                   
REMARK 500    PRO A 281      -89.03    -84.26                                   
REMARK 500    SER A 284     -159.52    -64.07                                   
REMARK 500    MET A 301      -61.42    -91.65                                   
REMARK 500    LEU A 302       67.49    -66.96                                   
REMARK 500    PRO A 319      -53.81    -21.69                                   
REMARK 500    GLU A 331       41.73   -102.01                                   
REMARK 500    LYS A 340       50.64     39.05                                   
REMARK 500    ASP A 343       88.27    -18.93                                   
REMARK 500    GLU A 344      100.27    -58.68                                   
REMARK 500    GLU A 346       85.52     57.17                                   
REMARK 500    ILE A 349      -38.42    -33.27                                   
REMARK 500    LYS A 353      -38.99    -39.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER A 179        23.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYU A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 408                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UKH   RELATED DB: PDB                                   
REMARK 900 JNK1 WITH QUERCETIN                                                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE MATCHES TO UNP ENTRY P45983-4(ISOFORM 4).               
DBREF  3V3V A    1   366  UNP    P45983   MK08_HUMAN       1    366             
DBREF  3V3V B  153   163  UNP    Q9WVI9   JIP1_MOUSE     153    163             
SEQADV 3V3V GLU A  185  UNP  P45983    TYR   185 CONFLICT                       
SEQADV 3V3V ALA A  288  UNP  P45983    LYS   288 CONFLICT                       
SEQADV 3V3V PRO A  364  UNP  P45983    GLU   364 CONFLICT                       
SEQADV 3V3V LYS A  365  UNP  P45983    GLU   365 CONFLICT                       
SEQADV 3V3V PRO A  367  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V THR A  368  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V THR A  369  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V LEU A  370  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V ASN A  371  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V LEU A  372  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V PHE A  373  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V HIS A  374  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V HIS A  375  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V HIS A  376  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V HIS A  377  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V HIS A  378  UNP  P45983              EXPRESSION TAG                 
SEQADV 3V3V HIS A  379  UNP  P45983              EXPRESSION TAG                 
SEQRES   1 A  379  MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL          
SEQRES   2 A  379  GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR          
SEQRES   3 A  379  GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE          
SEQRES   4 A  379  VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL          
SEQRES   5 A  379  ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR          
SEQRES   6 A  379  HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS          
SEQRES   7 A  379  CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL          
SEQRES   8 A  379  PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL          
SEQRES   9 A  379  TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN          
SEQRES  10 A  379  VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR          
SEQRES  11 A  379  LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS          
SEQRES  12 A  379  SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN          
SEQRES  13 A  379  ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP          
SEQRES  14 A  379  PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET          
SEQRES  15 A  379  THR PRO GLU VAL VAL THR ARG TYR TYR ARG ALA PRO GLU          
SEQRES  16 A  379  VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP ILE          
SEQRES  17 A  379  TRP SER VAL GLY CYS ILE MET GLY GLU MET ILE LYS GLY          
SEQRES  18 A  379  GLY VAL LEU PHE PRO GLY THR ASP HIS ILE ASP GLN TRP          
SEQRES  19 A  379  ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU          
SEQRES  20 A  379  PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR TYR VAL          
SEQRES  21 A  379  GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS          
SEQRES  22 A  379  LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS          
SEQRES  23 A  379  ASN ALA LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER          
SEQRES  24 A  379  LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL          
SEQRES  25 A  379  ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR          
SEQRES  26 A  379  ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO          
SEQRES  27 A  379  ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU          
SEQRES  28 A  379  TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU PRO          
SEQRES  29 A  379  LYS ARG PRO THR THR LEU ASN LEU PHE HIS HIS HIS HIS          
SEQRES  30 A  379  HIS HIS                                                      
SEQRES   1 B   11  ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE                  
HET    MYU  A 401      23                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  A 406       5                                                       
HET    SO4  A 407       5                                                       
HET     CL  A 408       1                                                       
HET    SO4  B 201       5                                                       
HETNAM     MYU 3,5,6,7-TETRAHYDROXY-2-(3,4-DIHYDROXYPHENYL)-4H-                 
HETNAM   2 MYU  CHROMEN-4-ONE                                                   
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETSYN     MYU 2-(3,4-DIHYDROXYPHENYL)-3,5,6,7-TETRAHYDROXY-4H-1-               
HETSYN   2 MYU  BENZOPYRAN-4-ONE; 2-(3,4-DIHYDROXYPHENYL)-4H-CHROMENE-          
HETSYN   3 MYU  3,5,6,7-TETRAOL; QUERCETAGETIN                                  
FORMUL   3  MYU    C15 H10 O8                                                   
FORMUL   4  SO4    7(O4 S 2-)                                                   
FORMUL  10   CL    CL 1-                                                        
FORMUL  12  HOH   *27(H2 O)                                                     
HELIX    1   1 ARG A   59  ASN A   63  5                                   5    
HELIX    2   2 GLN A   64  VAL A   80  1                                  17    
HELIX    3   3 SER A   97  PHE A  101  5                                   5    
HELIX    4   4 LEU A  115  GLN A  120  1                                   6    
HELIX    5   5 ASP A  124  SER A  144  1                                  21    
HELIX    6   6 LYS A  153  SER A  155  5                                   3    
HELIX    7   7 THR A  188  ARG A  192  5                                   5    
HELIX    8   8 ALA A  193  LEU A  198  1                                   6    
HELIX    9   9 ASN A  205  GLY A  221  1                                  17    
HELIX   10  10 ILE A  231  GLY A  242  1                                  12    
HELIX   11  11 CYS A  245  LYS A  251  1                                   7    
HELIX   12  12 THR A  255  ARG A  263  1                                   9    
HELIX   13  13 SER A  270  PHE A  275  1                                   6    
HELIX   14  14 PRO A  276  PHE A  280  5                                   5    
HELIX   15  15 LYS A  290  LEU A  302  1                                  13    
HELIX   16  16 SER A  311  HIS A  318  1                                   8    
HELIX   17  17 HIS A  318  VAL A  323  1                                   6    
HELIX   18  18 ASP A  326  GLU A  331  1                                   6    
HELIX   19  19 THR A  348  MET A  361  1                                  14    
SHEET    1   A 2 PHE A  10  GLU A  14  0                                        
SHEET    2   A 2 THR A  19  LEU A  23 -1  O  PHE A  20   N  VAL A  13           
SHEET    1   B 5 TYR A  26  GLY A  33  0                                        
SHEET    2   B 5 ILE A  39  ASP A  45 -1  O  TYR A  44   N  GLN A  27           
SHEET    3   B 5 ARG A  50  LEU A  57 -1  O  ILE A  54   N  CYS A  41           
SHEET    4   B 5 VAL A 104  GLU A 109 -1  O  ILE A 106   N  LYS A  55           
SHEET    5   B 5 LEU A  88  PHE A  92 -1  N  ASN A  90   O  VAL A 107           
SHEET    1   C 3 ALA A 113  ASN A 114  0                                        
SHEET    2   C 3 ILE A 157  VAL A 159 -1  O  VAL A 159   N  ALA A 113           
SHEET    3   C 3 LEU A 165  ILE A 167 -1  O  LYS A 166   N  VAL A 158           
SITE     1 AC1 13 VAL A  40  LYS A  55  GLU A  73  MET A 108                    
SITE     2 AC1 13 GLU A 109  LEU A 110  MET A 111  ASP A 112                    
SITE     3 AC1 13 ALA A 113  ASN A 114  LEU A 168  ASP A 169                    
SITE     4 AC1 13 HOH A 517                                                     
SITE     1 AC2  3 ASN A  28  ARG A  50  ASN A  51                               
SITE     1 AC3  5 GLN A  37  GLY A  38  LYS A  56  LEU A  57                    
SITE     2 AC3  5 SER A  58                                                     
SITE     1 AC4  3 LYS A  68  ARG A  72  ARG A 150                               
SITE     1 AC5  5 ARG A 189  ARG A 192  HIS A 230  THR A 255                    
SITE     2 AC5  5 HOH A 505                                                     
SITE     1 AC6  3 GLY A  35  LYS A 153  SER A 155                               
SITE     1 AC7  1 ARG A 263                                                     
SITE     1 AC8  1 ARG A 127                                                     
SITE     1 AC9  3 PRO B 154  LYS B 155  ARG B 156                               
CRYST1  172.370  172.370   86.040  90.00  90.00  90.00 I 4 2 2      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005801  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005801  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011623        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system