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Database: PDB
Entry: 2DFK
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Original site: 2DFK 
HEADER    CELL CYCLE                              02-MAR-06   2DFK              
TITLE     CRYSTAL STRUCTURE OF THE CDC42-COLLYBISTIN II COMPLEX                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COLLYBISTIN II;                                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 10-411;                                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CELL DIVISION CYCLE 42 ISOFORM 1;                          
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 SYNONYM: GTP-BINDING PROTEIN, 25KD; CDC42;                           
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTYB12;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    DH DOMAIN, PH DOMAIN, CELL CYCLE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XIANG,E.Y.KIM,J.J.CONNELLY,N.NASSAR,J.KIRSCH,J.WINKING,G.SCHWARZ,   
AUTHOR   2 H.SCHINDELIN                                                         
REVDAT   4   13-JUL-11 2DFK    1       VERSN                                    
REVDAT   3   24-FEB-09 2DFK    1       VERSN                                    
REVDAT   2   23-MAY-06 2DFK    1       JRNL                                     
REVDAT   1   02-MAY-06 2DFK    0                                                
JRNL        AUTH   S.XIANG,E.Y.KIM,J.J.CONNELLY,N.NASSAR,J.KIRSCH,J.WINKING,    
JRNL        AUTH 2 G.SCHWARZ,H.SCHINDELIN                                       
JRNL        TITL   THE CRYSTAL STRUCTURE OF CDC42 IN COMPLEX WITH COLLYBISTIN   
JRNL        TITL 2 II, A GEPHYRIN-INTERACTING GUANINE NUCLEOTIDE EXCHANGE       
JRNL        TITL 3 FACTOR.                                                      
JRNL        REF    J.MOL.BIOL.                   V. 359    35 2006              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16616186                                                     
JRNL        DOI    10.1016/J.JMB.2006.03.019                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 72076                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3782                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4417                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 224                          
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9002                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 581                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.10000                                             
REMARK   3    B22 (A**2) : 0.44000                                              
REMARK   3    B33 (A**2) : -0.34000                                             
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): 0.213         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.184         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.120         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.593         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9247 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  8336 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12448 ; 1.833 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 19465 ; 0.981 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 6.631 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1338 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10114 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1897 ; 0.012 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2029 ; 0.231 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  9566 ; 0.240 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5644 ; 0.090 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   440 ; 0.212 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    22 ; 0.278 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    86 ; 0.275 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.137 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5460 ; 1.070 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8850 ; 2.049 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3787 ; 3.326 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3598 ; 5.520 ; 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  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    43        A   246                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8202  11.5297  20.8668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2039 T22:   0.2419                                     
REMARK   3      T33:   0.2639 T12:   0.0110                                     
REMARK   3      T13:  -0.0118 T23:  -0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6897 L22:   1.6748                                     
REMARK   3      L33:   1.3454 L12:  -0.0185                                     
REMARK   3      L13:   0.1867 L23:   0.5639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0667 S12:   0.0205 S13:  -0.0700                       
REMARK   3      S21:  -0.0065 S22:  -0.0598 S23:   0.0363                       
REMARK   3      S31:  -0.1129 S32:  -0.0004 S33:  -0.0069                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   247        A   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.7753  22.6372 -13.4878              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2738 T22:   0.2451                                     
REMARK   3      T33:   0.1201 T12:   0.1474                                     
REMARK   3      T13:   0.0214 T23:   0.1473                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0656 L22:   3.8265                                     
REMARK   3      L33:   5.4229 L12:  -0.5002                                     
REMARK   3      L13:   1.5046 L23:  -0.9889                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0060 S12:  -0.4153 S13:  -0.2685                       
REMARK   3      S21:   0.1084 S22:   0.1904 S23:   0.3077                       
REMARK   3      S31:   0.2125 S32:  -0.4546 S33:  -0.1844                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   191                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.0935  -0.1561   6.3448              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2089 T22:   0.2882                                     
REMARK   3      T33:   0.2910 T12:   0.0361                                     
REMARK   3      T13:   0.0662 T23:   0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6118 L22:   2.3947                                     
REMARK   3      L33:   1.5895 L12:  -0.0618                                     
REMARK   3      L13:   0.1071 L23:   0.4732                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0414 S12:   0.0909 S13:  -0.0537                       
REMARK   3      S21:  -0.2885 S22:  -0.0391 S23:  -0.3384                       
REMARK   3      S31:  -0.0120 S32:   0.2851 S33:  -0.0023                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    51        C   246                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.7864 -33.6330  36.9794              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2220 T22:   0.2544                                     
REMARK   3      T33:   0.2778 T12:  -0.0257                                     
REMARK   3      T13:  -0.0069 T23:   0.0423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8634 L22:   1.3443                                     
REMARK   3      L33:   0.8136 L12:  -0.5237                                     
REMARK   3      L13:   0.4092 L23:  -0.5183                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0268 S12:  -0.0516 S13:   0.0152                       
REMARK   3      S21:   0.0177 S22:   0.0746 S23:  -0.0451                       
REMARK   3      S31:  -0.0222 S32:   0.0392 S33:  -0.0478                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   247        C   397                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.3390 -37.7865  -2.6298              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2633 T22:   0.2459                                     
REMARK   3      T33:   0.2255 T12:  -0.0058                                     
REMARK   3      T13:   0.0169 T23:  -0.0408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1471 L22:   1.7504                                     
REMARK   3      L33:   5.5846 L12:  -0.0751                                     
REMARK   3      L13:  -0.1765 L23:  -1.2230                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0257 S12:   0.1462 S13:  -0.1767                       
REMARK   3      S21:  -0.1826 S22:   0.0022 S23:  -0.0812                       
REMARK   3      S31:   0.5534 S32:  -0.0768 S33:  -0.0280                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    -2        D   191                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.5993 -38.6721  40.5404              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2305 T22:   0.2220                                     
REMARK   3      T33:   0.2672 T12:  -0.0152                                     
REMARK   3      T13:   0.0132 T23:   0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6139 L22:   0.9730                                     
REMARK   3      L33:   1.6739 L12:   0.2304                                     
REMARK   3      L13:  -0.0380 L23:   0.1007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0221 S12:   0.0264 S13:   0.0455                       
REMARK   3      S21:   0.0174 S22:  -0.0611 S23:   0.1028                       
REMARK   3      S31:  -0.0453 S32:  -0.1364 S33:   0.0390                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 2DFK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-MAR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB025359.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-AUG-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X26C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72590                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
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     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.52000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: PDB ENTRY 1FOE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, POTASSIUM DIHYDROGEN           
REMARK 280  PHOSPHATE, NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K,   
REMARK 280  PH 8.00                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.97850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       83.61000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       73.74950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       83.61000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.97850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       73.74950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: 4010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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: 10920 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 53250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     TRP A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     ASN A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     GLU A    16                                                      
REMARK 465     ASP A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     VAL A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     ASP A    25                                                      
REMARK 465     VAL A    26                                                      
REMARK 465     GLN A    27                                                      
REMARK 465     ASN A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     HIS A    30                                                      
REMARK 465     LEU A    31                                                      
REMARK 465     ASP A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     ASN A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     GLN A   402                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     VAL A   404                                                      
REMARK 465     THR A   405                                                      
REMARK 465     GLN A   406                                                      
REMARK 465     ARG A   407                                                      
REMARK 465     LYS A   408                                                      
REMARK 465     TRP A   409                                                      
REMARK 465     HIS A   410                                                      
REMARK 465     TYR A   411                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     PRO B   180                                                      
REMARK 465     GLU B   181                                                      
REMARK 465     PRO B   182                                                      
REMARK 465     LYS B   183                                                      
REMARK 465     MET C    10                                                      
REMARK 465     LEU C    11                                                      
REMARK 465     TRP C    12                                                      
REMARK 465     VAL C    13                                                      
REMARK 465     ASN C    14                                                      
REMARK 465     GLN C    15                                                      
REMARK 465     GLU C    16                                                      
REMARK 465     ASP C    17                                                      
REMARK 465     GLY C    18                                                      
REMARK 465     VAL C    19                                                      
REMARK 465     GLU C    20                                                      
REMARK 465     GLU C    21                                                      
REMARK 465     GLY C    22                                                      
REMARK 465     PRO C    23                                                      
REMARK 465     SER C    24                                                      
REMARK 465     ASP C    25                                                      
REMARK 465     VAL C    26                                                      
REMARK 465     GLN C    27                                                      
REMARK 465     ASN C    28                                                      
REMARK 465     GLY C    29                                                      
REMARK 465     HIS C    30                                                      
REMARK 465     LEU C    31                                                      
REMARK 465     ASP C    32                                                      
REMARK 465     PRO C    33                                                      
REMARK 465     ASN C    34                                                      
REMARK 465     SER C    35                                                      
REMARK 465     ASP C    36                                                      
REMARK 465     CYS C    37                                                      
REMARK 465     LEU C    38                                                      
REMARK 465     CYS C    39                                                      
REMARK 465     LEU C    40                                                      
REMARK 465     GLY C    41                                                      
REMARK 465     ARG C    42                                                      
REMARK 465     PRO C    43                                                      
REMARK 465     LEU C    44                                                      
REMARK 465     LYS C   398                                                      
REMARK 465     ALA C   399                                                      
REMARK 465     SER C   400                                                      
REMARK 465     LYS C   401                                                      
REMARK 465     GLN C   402                                                      
REMARK 465     LYS C   403                                                      
REMARK 465     VAL C   404                                                      
REMARK 465     THR C   405                                                      
REMARK 465     GLN C   406                                                      
REMARK 465     ARG C   407                                                      
REMARK 465     LYS C   408                                                      
REMARK 465     TRP C   409                                                      
REMARK 465     HIS C   410                                                      
REMARK 465     TYR C   411                                                      
REMARK 465     PRO D   180                                                      
REMARK 465     GLU D   181                                                      
REMARK 465     PRO D   182                                                      
REMARK 465     LYS D   183                                                      
REMARK 465     LYS D   184                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLN C   106     O    HOH C   603              1.73            
REMARK 500   O    HOH C   429     O    HOH C   578              1.79            
REMARK 500   NZ   LYS C   195     O    HOH C   472              1.83            
REMARK 500   NE2  GLN C   106     O    HOH C   605              2.01            
REMARK 500   OE2  GLU C   133     O    HOH C   594              2.09            
REMARK 500   NZ   LYS C   235     OE1  GLU C   239              2.11            
REMARK 500   O    HOH A   656     O    HOH A   729              2.14            
REMARK 500   O    HOH C   479     O    HOH C   567              2.15            
REMARK 500   OE2  GLU C    62     O    HOH C   605              2.18            
REMARK 500   NZ   LYS C   235     O    HOH C   518              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 202   CD    GLU A 202   OE2     0.072                       
REMARK 500    GLU C 233   CD    GLU C 233   OE2     0.086                       
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    ARG A  51   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  51   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG A 104   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG A 104   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ASP A 112   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 121   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP A 210   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    LEU A 296   CA  -  CB  -  CG  ANGL. DEV. =  18.3 DEGREES          
REMARK 500    ASP A 314   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP A 316   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    PHE A 331   N   -  CA  -  C   ANGL. DEV. =  18.4 DEGREES          
REMARK 500    ARG C  63   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP C 112   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG C 237   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP C 242   CB  -  CG  -  OD2 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ASP C 261   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG C 262   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG C 262   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP C 314   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP C 329   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG C 368   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG C 368   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASP D  11   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    LEU D  19   CB  -  CG  -  CD1 ANGL. DEV. = -11.4 DEGREES          
REMARK 500    ASP D  38   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP D  76   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP D 118   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP D 122   CB  -  CG  -  OD2 ANGL. DEV. =   8.4 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  98       30.38    -99.10                                   
REMARK 500    ASP A 121       78.83   -154.39                                   
REMARK 500    SER A 264       17.53   -144.39                                   
REMARK 500    TYR A 279       -0.29     74.92                                   
REMARK 500    HIS A 292      -23.84     86.25                                   
REMARK 500    ASP A 325      153.30    -49.75                                   
REMARK 500    ASP A 330       90.20    -24.55                                   
REMARK 500    PHE A 331      -68.49     15.75                                   
REMARK 500    ASN A 337       71.83     65.71                                   
REMARK 500    GLU A 358      -38.52    -36.33                                   
REMARK 500    ALA A 399       56.72    -92.95                                   
REMARK 500    SER A 400      111.03     49.95                                   
REMARK 500    LYS B  96      -62.05   -129.11                                   
REMARK 500    SER B 185      -48.11    139.95                                   
REMARK 500    LEU B 190      110.30     20.38                                   
REMARK 500    ARG C  83       76.16   -112.64                                   
REMARK 500    ASN C  98       33.93    -97.06                                   
REMARK 500    ASP C 121       80.20   -157.89                                   
REMARK 500    SER C 264       -2.78   -142.26                                   
REMARK 500    HIS C 292      -18.73     82.26                                   
REMARK 500    ASP C 305      -50.09    -29.34                                   
REMARK 500    THR C 346     -117.91   -140.35                                   
REMARK 500    GLU C 347      -15.34    177.96                                   
REMARK 500    SER D  -1     -153.96     99.21                                   
REMARK 500    TYR D  32      116.62   -162.82                                   
REMARK 500    ASN D  39      134.65    -38.45                                   
REMARK 500    LYS D  96      -64.46   -105.69                                   
REMARK 500    VAL D 189     -149.60   -122.48                                   
REMARK 500    LEU D 190      170.40     39.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS B  184     SER B  185                 -149.66                    
REMARK 500 THR C  346     GLU C  347                 -142.22                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE A 331        19.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 647        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A 745        DISTANCE =  5.29 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 606                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FOE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1KZ7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1KZG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1LB1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1KI1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1DBH   RELATED DB: PDB                                   
DBREF  2DFK A   10   411  UNP    Q9QX73   ARHG9_RAT       10    411             
DBREF  2DFK C   10   411  UNP    Q9QX73   ARHG9_RAT       10    411             
DBREF  2DFK B    1   191  UNP    P60953   CDC42_HUMAN      1    191             
DBREF  2DFK D    1   191  UNP    P60953   CDC42_HUMAN      1    191             
SEQADV 2DFK GLY B   -2  UNP  P60953              CLONING ARTIFACT               
SEQADV 2DFK SER B   -1  UNP  P60953              CLONING ARTIFACT               
SEQADV 2DFK HIS B    0  UNP  P60953              CLONING ARTIFACT               
SEQADV 2DFK GLY D   -2  UNP  P60953              CLONING ARTIFACT               
SEQADV 2DFK SER D   -1  UNP  P60953              CLONING ARTIFACT               
SEQADV 2DFK HIS D    0  UNP  P60953              CLONING ARTIFACT               
SEQRES   1 A  402  MET LEU TRP VAL ASN GLN GLU ASP GLY VAL GLU GLU GLY          
SEQRES   2 A  402  PRO SER ASP VAL GLN ASN GLY HIS LEU ASP PRO ASN SER          
SEQRES   3 A  402  ASP CYS LEU CYS LEU GLY ARG PRO LEU GLN ASN ARG ASP          
SEQRES   4 A  402  GLN MET ARG ALA ASN VAL ILE ASN GLU ILE MET SER THR          
SEQRES   5 A  402  GLU ARG HIS TYR ILE LYS HIS LEU LYS ASP ILE CYS GLU          
SEQRES   6 A  402  GLY TYR LEU LYS GLN CYS ARG LYS ARG ARG ASP MET PHE          
SEQRES   7 A  402  SER ASP GLU GLN LEU LYS VAL ILE PHE GLY ASN ILE GLU          
SEQRES   8 A  402  ASP ILE TYR ARG PHE GLN MET GLY PHE VAL ARG ASP LEU          
SEQRES   9 A  402  GLU LYS GLN TYR ASN ASN ASP ASP PRO HIS LEU SER GLU          
SEQRES  10 A  402  ILE GLY PRO CYS PHE LEU GLU HIS GLN ASP GLY PHE TRP          
SEQRES  11 A  402  ILE TYR SER GLU TYR CYS ASN ASN HIS LEU ASP ALA CYS          
SEQRES  12 A  402  MET GLU LEU SER LYS LEU MET LYS ASP SER ARG TYR GLN          
SEQRES  13 A  402  HIS PHE PHE GLU ALA CYS ARG LEU LEU GLN GLN MET ILE          
SEQRES  14 A  402  ASP ILE ALA ILE ASP GLY PHE LEU LEU THR PRO VAL GLN          
SEQRES  15 A  402  LYS ILE CYS LYS TYR PRO LEU GLN LEU ALA GLU LEU LEU          
SEQRES  16 A  402  LYS TYR THR ALA GLN ASP HIS SER ASP TYR ARG TYR VAL          
SEQRES  17 A  402  ALA ALA ALA LEU ALA VAL MET ARG ASN VAL THR GLN GLN          
SEQRES  18 A  402  ILE ASN GLU ARG LYS ARG ARG LEU GLU ASN ILE ASP LYS          
SEQRES  19 A  402  ILE ALA GLN TRP GLN ALA SER VAL LEU ASP TRP GLU GLY          
SEQRES  20 A  402  ASP ASP ILE LEU ASP ARG SER SER GLU LEU ILE TYR THR          
SEQRES  21 A  402  GLY GLU MET ALA TRP ILE TYR GLN PRO TYR GLY ARG ASN          
SEQRES  22 A  402  GLN GLN ARG VAL PHE PHE LEU PHE ASP HIS GLN MET VAL          
SEQRES  23 A  402  LEU CYS LYS LYS ASP LEU ILE ARG ARG ASP ILE LEU TYR          
SEQRES  24 A  402  TYR LYS GLY ARG ILE ASP MET ASP LYS TYR GLU VAL ILE          
SEQRES  25 A  402  ASP ILE GLU ASP GLY ARG ASP ASP ASP PHE ASN VAL SER          
SEQRES  26 A  402  MET LYS ASN ALA PHE LYS LEU HIS ASN LYS GLU THR GLU          
SEQRES  27 A  402  GLU VAL HIS LEU PHE PHE ALA LYS LYS LEU GLU GLU LYS          
SEQRES  28 A  402  ILE ARG TRP LEU ARG ALA PHE ARG GLU GLU ARG LYS MET          
SEQRES  29 A  402  VAL GLN GLU ASP GLU LYS ILE GLY PHE GLU ILE SER GLU          
SEQRES  30 A  402  ASN GLN LYS ARG GLN ALA ALA MET THR VAL ARG LYS ALA          
SEQRES  31 A  402  SER LYS GLN LYS VAL THR GLN ARG LYS TRP HIS TYR              
SEQRES   1 B  194  GLY SER HIS MET GLN THR ILE LYS CYS VAL VAL VAL GLY          
SEQRES   2 B  194  ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR          
SEQRES   3 B  194  THR THR ASN LYS PHE PRO SER GLU TYR VAL PRO THR VAL          
SEQRES   4 B  194  PHE ASP ASN TYR ALA VAL THR VAL MET ILE GLY GLY GLU          
SEQRES   5 B  194  PRO TYR THR LEU GLY LEU PHE ASP THR ALA GLY GLN GLU          
SEQRES   6 B  194  ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR          
SEQRES   7 B  194  ASP VAL PHE LEU VAL CYS PHE SER VAL VAL SER PRO SER          
SEQRES   8 B  194  SER PHE GLU ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE          
SEQRES   9 B  194  THR HIS HIS CYS PRO LYS THR PRO PHE LEU LEU VAL GLY          
SEQRES  10 B  194  THR GLN ILE ASP LEU ARG ASP ASP PRO SER THR ILE GLU          
SEQRES  11 B  194  LYS LEU ALA LYS ASN LYS GLN LYS PRO ILE THR PRO GLU          
SEQRES  12 B  194  THR ALA GLU LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS          
SEQRES  13 B  194  TYR VAL GLU CYS SER ALA LEU THR GLN LYS GLY LEU LYS          
SEQRES  14 B  194  ASN VAL PHE ASP GLU ALA ILE LEU ALA ALA LEU GLU PRO          
SEQRES  15 B  194  PRO GLU PRO LYS LYS SER ARG ARG CYS VAL LEU LEU              
SEQRES   1 C  402  MET LEU TRP VAL ASN GLN GLU ASP GLY VAL GLU GLU GLY          
SEQRES   2 C  402  PRO SER ASP VAL GLN ASN GLY HIS LEU ASP PRO ASN SER          
SEQRES   3 C  402  ASP CYS LEU CYS LEU GLY ARG PRO LEU GLN ASN ARG ASP          
SEQRES   4 C  402  GLN MET ARG ALA ASN VAL ILE ASN GLU ILE MET SER THR          
SEQRES   5 C  402  GLU ARG HIS TYR ILE LYS HIS LEU LYS ASP ILE CYS GLU          
SEQRES   6 C  402  GLY TYR LEU LYS GLN CYS ARG LYS ARG ARG ASP MET PHE          
SEQRES   7 C  402  SER ASP GLU GLN LEU LYS VAL ILE PHE GLY ASN ILE GLU          
SEQRES   8 C  402  ASP ILE TYR ARG PHE GLN MET GLY PHE VAL ARG ASP LEU          
SEQRES   9 C  402  GLU LYS GLN TYR ASN ASN ASP ASP PRO HIS LEU SER GLU          
SEQRES  10 C  402  ILE GLY PRO CYS PHE LEU GLU HIS GLN ASP GLY PHE TRP          
SEQRES  11 C  402  ILE TYR SER GLU TYR CYS ASN ASN HIS LEU ASP ALA CYS          
SEQRES  12 C  402  MET GLU LEU SER LYS LEU MET LYS ASP SER ARG TYR GLN          
SEQRES  13 C  402  HIS PHE PHE GLU ALA CYS ARG LEU LEU GLN GLN MET ILE          
SEQRES  14 C  402  ASP ILE ALA ILE ASP GLY PHE LEU LEU THR PRO VAL GLN          
SEQRES  15 C  402  LYS ILE CYS LYS TYR PRO LEU GLN LEU ALA GLU LEU LEU          
SEQRES  16 C  402  LYS TYR THR ALA GLN ASP HIS SER ASP TYR ARG TYR VAL          
SEQRES  17 C  402  ALA ALA ALA LEU ALA VAL MET ARG ASN VAL THR GLN GLN          
SEQRES  18 C  402  ILE ASN GLU ARG LYS ARG ARG LEU GLU ASN ILE ASP LYS          
SEQRES  19 C  402  ILE ALA GLN TRP GLN ALA SER VAL LEU ASP TRP GLU GLY          
SEQRES  20 C  402  ASP ASP ILE LEU ASP ARG SER SER GLU LEU ILE TYR THR          
SEQRES  21 C  402  GLY GLU MET ALA TRP ILE TYR GLN PRO TYR GLY ARG ASN          
SEQRES  22 C  402  GLN GLN ARG VAL PHE PHE LEU PHE ASP HIS GLN MET VAL          
SEQRES  23 C  402  LEU CYS LYS LYS ASP LEU ILE ARG ARG ASP ILE LEU TYR          
SEQRES  24 C  402  TYR LYS GLY ARG ILE ASP MET ASP LYS TYR GLU VAL ILE          
SEQRES  25 C  402  ASP ILE GLU ASP GLY ARG ASP ASP ASP PHE ASN VAL SER          
SEQRES  26 C  402  MET LYS ASN ALA PHE LYS LEU HIS ASN LYS GLU THR GLU          
SEQRES  27 C  402  GLU VAL HIS LEU PHE PHE ALA LYS LYS LEU GLU GLU LYS          
SEQRES  28 C  402  ILE ARG TRP LEU ARG ALA PHE ARG GLU GLU ARG LYS MET          
SEQRES  29 C  402  VAL GLN GLU ASP GLU LYS ILE GLY PHE GLU ILE SER GLU          
SEQRES  30 C  402  ASN GLN LYS ARG GLN ALA ALA MET THR VAL ARG LYS ALA          
SEQRES  31 C  402  SER LYS GLN LYS VAL THR GLN ARG LYS TRP HIS TYR              
SEQRES   1 D  194  GLY SER HIS MET GLN THR ILE LYS CYS VAL VAL VAL GLY          
SEQRES   2 D  194  ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR          
SEQRES   3 D  194  THR THR ASN LYS PHE PRO SER GLU TYR VAL PRO THR VAL          
SEQRES   4 D  194  PHE ASP ASN TYR ALA VAL THR VAL MET ILE GLY GLY GLU          
SEQRES   5 D  194  PRO TYR THR LEU GLY LEU PHE ASP THR ALA GLY GLN GLU          
SEQRES   6 D  194  ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR          
SEQRES   7 D  194  ASP VAL PHE LEU VAL CYS PHE SER VAL VAL SER PRO SER          
SEQRES   8 D  194  SER PHE GLU ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE          
SEQRES   9 D  194  THR HIS HIS CYS PRO LYS THR PRO PHE LEU LEU VAL GLY          
SEQRES  10 D  194  THR GLN ILE ASP LEU ARG ASP ASP PRO SER THR ILE GLU          
SEQRES  11 D  194  LYS LEU ALA LYS ASN LYS GLN LYS PRO ILE THR PRO GLU          
SEQRES  12 D  194  THR ALA GLU LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS          
SEQRES  13 D  194  TYR VAL GLU CYS SER ALA LEU THR GLN LYS GLY LEU LYS          
SEQRES  14 D  194  ASN VAL PHE ASP GLU ALA ILE LEU ALA ALA LEU GLU PRO          
SEQRES  15 D  194  PRO GLU PRO LYS LYS SER ARG ARG CYS VAL LEU LEU              
HET    SO4  D 701       5                                                       
HET    SO4  B 702       5                                                       
HET    GOL  A 601       6                                                       
HET    GOL  A 602       6                                                       
HET    GOL  B 603       6                                                       
HET    GOL  D 604       6                                                       
HET    GOL  D 605       6                                                       
HET    GOL  A 606       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   7  GOL    6(C3 H8 O3)                                                  
FORMUL  13  HOH   *581(H2 O)                                                    
HELIX    1   1 ASN A   46  TYR A   76  1                                  31    
HELIX    2   2 TYR A   76  ARG A   83  1                                   8    
HELIX    3   3 SER A   88  GLY A   97  1                                  10    
HELIX    4   4 ASN A   98  TYR A  117  1                                  20    
HELIX    5   5 ASP A  121  SER A  125  5                                   5    
HELIX    6   6 ILE A  127  HIS A  134  1                                   8    
HELIX    7   7 ASP A  136  PHE A  138  5                                   3    
HELIX    8   8 TRP A  139  MET A  159  1                                  21    
HELIX    9   9 ASP A  161  GLN A  175  1                                  15    
HELIX   10  10 ALA A  181  LEU A  187  1                                   7    
HELIX   11  11 LEU A  187  TYR A  206  1                                  20    
HELIX   12  12 ASP A  213  ASN A  240  1                                  28    
HELIX   13  13 ASN A  240  VAL A  251  1                                  12    
HELIX   14  14 ASP A  258  ARG A  262  5                                   5    
HELIX   15  15 LYS A  356  GLY A  381  1                                  26    
HELIX   16  16 SER A  385  ALA A  399  1                                  15    
HELIX   17  17 GLY B   15  THR B   25  1                                  11    
HELIX   18  18 LEU B   67  TYR B   72  5                                   6    
HELIX   19  19 SER B   86  LYS B   96  1                                  11    
HELIX   20  20 LYS B   96  CYS B  105  1                                  10    
HELIX   21  21 GLN B  116  ASP B  121  5                                   6    
HELIX   22  22 ASP B  122  ASN B  132  1                                  11    
HELIX   23  23 THR B  138  LEU B  149  1                                  12    
HELIX   24  24 GLY B  164  GLU B  178  1                                  15    
HELIX   25  25 ASN C   46  GLY C   75  1                                  30    
HELIX   26  26 GLY C   75  LYS C   82  1                                   8    
HELIX   27  27 SER C   88  GLY C   97  1                                  10    
HELIX   28  28 ASN C   98  TYR C  117  1                                  20    
HELIX   29  29 ASP C  121  SER C  125  5                                   5    
HELIX   30  30 ILE C  127  HIS C  134  1                                   8    
HELIX   31  31 GLN C  135  PHE C  138  5                                   4    
HELIX   32  32 TRP C  139  MET C  159  1                                  21    
HELIX   33  33 ASP C  161  GLN C  175  1                                  15    
HELIX   34  34 ALA C  181  LEU C  187  1                                   7    
HELIX   35  35 LEU C  187  TYR C  206  1                                  20    
HELIX   36  36 ASP C  213  ASN C  240  1                                  28    
HELIX   37  37 ASN C  240  VAL C  251  1                                  12    
HELIX   38  38 ASP C  258  ARG C  262  5                                   5    
HELIX   39  39 LYS C  356  GLY C  381  1                                  26    
HELIX   40  40 SER C  385  MET C  394  1                                  10    
HELIX   41  41 GLY D   15  ASN D   26  1                                  12    
HELIX   42  42 LEU D   67  TYR D   72  5                                   6    
HELIX   43  43 SER D   86  LYS D   96  1                                  11    
HELIX   44  44 LYS D   96  CYS D  105  1                                  10    
HELIX   45  45 GLN D  116  ASP D  121  5                                   6    
HELIX   46  46 ASP D  122  ASN D  132  1                                  11    
HELIX   47  47 THR D  138  LYS D  150  1                                  13    
HELIX   48  48 GLY D  164  LEU D  177  1                                  14    
SHEET    1   A 7 LEU A 307  ASP A 314  0                                        
SHEET    2   A 7 GLN A 293  LYS A 299 -1  N  MET A 294   O  ILE A 313           
SHEET    3   A 7 GLN A 283  PHE A 290 -1  N  VAL A 286   O  CYS A 297           
SHEET    4   A 7 LEU A 266  ILE A 275 -1  N  ILE A 267   O  LEU A 289           
SHEET    5   A 7 VAL A 349  PHE A 353 -1  O  LEU A 351   N  ILE A 275           
SHEET    6   A 7 ALA A 338  ASN A 343 -1  N  PHE A 339   O  PHE A 352           
SHEET    7   A 7 TYR A 318  ASP A 322 -1  N  ILE A 321   O  LYS A 340           
SHEET    1   B 2 GLY A 326  ARG A 327  0                                        
SHEET    2   B 2 SER A 334  MET A 335 -1  O  MET A 335   N  GLY A 326           
SHEET    1   C 6 TYR B  40  ILE B  46  0                                        
SHEET    2   C 6 GLU B  49  PHE B  56 -1  O  LEU B  53   N  VAL B  42           
SHEET    3   C 6 THR B   3  GLY B  10  1  N  ILE B   4   O  GLY B  54           
SHEET    4   C 6 VAL B  77  SER B  83  1  O  CYS B  81   N  VAL B   9           
SHEET    5   C 6 PHE B 110  THR B 115  1  O  LEU B 111   N  VAL B  80           
SHEET    6   C 6 TYR B 154  GLU B 156  1  O  VAL B 155   N  GLY B 114           
SHEET    1   D 7 LEU C 307  ASP C 314  0                                        
SHEET    2   D 7 GLN C 293  LYS C 299 -1  N  LEU C 296   O  GLY C 311           
SHEET    3   D 7 GLN C 283  PHE C 290 -1  N  PHE C 290   O  GLN C 293           
SHEET    4   D 7 LEU C 266  ILE C 275 -1  N  GLY C 270   O  PHE C 287           
SHEET    5   D 7 VAL C 349  PHE C 353 -1  O  PHE C 353   N  ALA C 273           
SHEET    6   D 7 ALA C 338  ASN C 343 -1  N  PHE C 339   O  PHE C 352           
SHEET    7   D 7 TYR C 318  ASP C 322 -1  N  GLU C 319   O  HIS C 342           
SHEET    1   E 2 GLY C 326  ARG C 327  0                                        
SHEET    2   E 2 SER C 334  MET C 335 -1  O  MET C 335   N  GLY C 326           
SHEET    1   F 6 TYR D  40  ILE D  46  0                                        
SHEET    2   F 6 GLU D  49  PHE D  56 -1  O  LEU D  53   N  VAL D  42           
SHEET    3   F 6 ILE D   4  VAL D   9  1  N  CYS D   6   O  GLY D  54           
SHEET    4   F 6 VAL D  77  SER D  83  1  O  LEU D  79   N  VAL D   9           
SHEET    5   F 6 PHE D 110  THR D 115  1  O  VAL D 113   N  VAL D  80           
SHEET    6   F 6 TYR D 154  GLU D 156  1  O  VAL D 155   N  LEU D 112           
SSBOND   1 CYS B  105    CYS B  188                          1555   1555  2.11  
SSBOND   2 CYS D  105    CYS D  188                          1555   1555  2.11  
CISPEP   1 ASP A  330    PHE A  331          0         3.06                     
SITE     1 AC1 11 ASP D  11  GLY D  12  ALA D  13  VAL D  14                    
SITE     2 AC1 11 GLY D  15  LYS D  16  THR D  17  ALA D  59                    
SITE     3 AC1 11 HOH D 731  HOH D 746  HOH D 777                               
SITE     1 AC2 10 ASP B  11  GLY B  12  ALA B  13  VAL B  14                    
SITE     2 AC2 10 GLY B  15  LYS B  16  THR B  17  GLU B  62                    
SITE     3 AC2 10 HOH B 715  HOH B 733                                          
SITE     1 AC3  4 ARG A 104  LYS D 153  GLU D 171  GLU D 178                    
SITE     1 AC4  5 ARG A 215  TYR A 216  HOH A 769  MET B  45                    
SITE     2 AC4  5 GLY B  48                                                     
SITE     1 AC5  5 SER B  22  TYR B  23  THR B  25  ASN B  26                    
SITE     2 AC5  5 GLN B 162                                                     
SITE     1 AC6  2 THR D  24  THR D  25                                          
SITE     1 AC7  5 THR D  24  PHE D  37  ASP D  38  TYR D  40                    
SITE     2 AC7  5 HOH D 784                                                     
SITE     1 AC8  6 LYS A 115  GLN A 116  TYR A 117  ASN A 118                    
SITE     2 AC8  6 HOH A 655  HOH A 660                                          
CRYST1   57.957  147.499  167.220  90.00  90.00  90.00 P 21 21 21    8          
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      0.017254  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006780  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005980        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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