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Database: PDB
Entry: 3QKJ
LinkDB: 3QKJ
Original site: 3QKJ 
HEADER    TRANSFERASE                             01-FEB-11   3QKJ              
TITLE     THE PWWP DOMAIN OF HUMAN DNA (CYTOSINE-5-)-METHYLTRANSFERASE 3 BETA IN
TITLE    2 COMPLEX WITH A BIS-TRIS MOLECULE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA CYTOSINE-5 METHYLTRANSFERASE 3 BETA ISOFORM 6 VARIANT; 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 293-442;                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
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: PET28-MHL                                 
KEYWDS    DNMT3B, PWWP DOMAIN, METHYLTRANSFERASE 3 BETA, SGC, S-ADENOSYL-L-     
KEYWDS   2 METHIONINE, TRANSFERASE, ZINC-FINGER, STRUCTURAL GENOMICS,           
KEYWDS   3 STRUCTURAL GENOMICS CONSORTIUM                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.ZENG,M.F.AMAYA,F.MACKENZIE,J.WEIGELT,M.SUNDSTROM,C.H.ARROWSMITH,    
AUTHOR   2 A.M.EDWARDS,A.BOTCHKAREV,J.MIN,H.WU,STRUCTURAL GENOMICS CONSORTIUM   
AUTHOR   3 (SGC)                                                                
REVDAT   3   20-JUL-11 3QKJ    1       JRNL                                     
REVDAT   2   16-MAR-11 3QKJ    1       REMARK                                   
REVDAT   1   09-MAR-11 3QKJ    0                                                
JRNL        AUTH   H.WU,H.ZENG,R.LAM,W.TEMPEL,M.F.AMAYA,C.XU,L.DOMBROVSKI,      
JRNL        AUTH 2 W.QIU,Y.WANG,J.MIN                                           
JRNL        TITL   STRUCTURAL AND HISTONE BINDING ABILITY CHARACTERIZATIONS OF  
JRNL        TITL 2 HUMAN PWWP DOMAINS.                                          
JRNL        REF    PLOS ONE                      V.   6 E1891 2011              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   21720545                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0018919                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 62267                          
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)  : 0.210                          
REMARK   3   R VALUE            (WORKING SET)  : 0.209                          
REMARK   3   FREE R VALUE                      : 0.228                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.080                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3163                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.04                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.09                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4120                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2530                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3907                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2530                   
REMARK   3   BIN FREE R VALUE                        : 0.2530                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.17                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 213                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4106                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 263                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.63550                                              
REMARK   3    B22 (A**2) : 0.63550                                              
REMARK   3    B33 (A**2) : -1.27100                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.39                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4330   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5842   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1405   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 71     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 634    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4278   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : NULL   ; NULL   ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.97                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   36.7010   54.1438   34.2364           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0927 T22:   -0.0298                                    
REMARK   3     T33:   -0.0860 T12:   -0.0572                                    
REMARK   3     T13:   -0.0528 T23:   -0.0003                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.0892 L22:    2.4553                                    
REMARK   3     L33:    1.6888 L12:    2.5632                                    
REMARK   3     L13:   -0.7524 L23:   -0.4226                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0455 S12:   -0.2184 S13:    0.0698                     
REMARK   3     S21:   -0.0313 S22:   -0.1308 S23:    0.0293                     
REMARK   3     S31:   -0.0791 S32:    0.0172 S33:    0.0853                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    9.2937   38.2421   30.9742           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0955 T22:   -0.0314                                    
REMARK   3     T33:   -0.0848 T12:   -0.0591                                    
REMARK   3     T13:   -0.0211 T23:   -0.0441                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.4446 L22:    2.0917                                    
REMARK   3     L33:    1.7439 L12:    2.4279                                    
REMARK   3     L13:   -0.7148 L23:   -0.2626                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2003 S12:    0.1002 S13:    0.0979                     
REMARK   3     S21:   -0.0642 S22:    0.1201 S23:    0.0449                     
REMARK   3     S31:   -0.0255 S32:   -0.0787 S33:    0.0801                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   41.1942   76.6684   14.7812           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0549 T22:   -0.2727                                    
REMARK   3     T33:   -0.1341 T12:   -0.0255                                    
REMARK   3     T13:   -0.0474 T23:    0.0110                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6835 L22:    3.6464                                    
REMARK   3     L33:    8.2121 L12:   -0.6989                                    
REMARK   3     L13:    0.1582 L23:    0.3526                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.3775 S12:   -0.0693 S13:   -0.1255                     
REMARK   3     S21:   -0.6515 S22:   -0.0982 S23:    0.2552                     
REMARK   3     S31:    0.4524 S32:    0.2191 S33:   -0.2793                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   62.0665   45.6541   50.5457           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2014 T22:   -0.0031                                    
REMARK   3     T33:   -0.1260 T12:    0.1304                                    
REMARK   3     T13:   -0.0188 T23:   -0.0440                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3219 L22:    2.6658                                    
REMARK   3     L33:    7.7142 L12:   -1.0124                                    
REMARK   3     L13:    0.1041 L23:    0.1421                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2953 S12:   -0.2856 S13:    0.1509                     
REMARK   3     S21:    0.3408 S22:    0.5898 S23:   -0.2175                     
REMARK   3     S31:    0.4443 S32:    0.2854 S33:   -0.2945                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3QKJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063760.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
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                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62267                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6, VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 300K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      106.84400            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       53.42200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLY A   205                                                      
REMARK 465     GLU A   206                                                      
REMARK 465     ALA A   207                                                      
REMARK 465     ASP A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     GLY A   210                                                      
REMARK 465     ASP A   211                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     ASP A   213                                                      
REMARK 465     SER A   214                                                      
REMARK 465     SER A   319                                                      
REMARK 465     SER A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     GLY A   322                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     SER A   324                                                      
REMARK 465     LEU A   325                                                      
REMARK 465     ASN A   352                                                      
REMARK 465     THR A   353                                                      
REMARK 465     GLN A   354                                                      
REMARK 465     PRO A   355                                                      
REMARK 465     GLY B   205                                                      
REMARK 465     GLU B   206                                                      
REMARK 465     ALA B   207                                                      
REMARK 465     ASP B   208                                                      
REMARK 465     SER B   209                                                      
REMARK 465     GLY B   210                                                      
REMARK 465     ASP B   211                                                      
REMARK 465     GLY B   212                                                      
REMARK 465     ASP B   213                                                      
REMARK 465     SER B   214                                                      
REMARK 465     SER B   319                                                      
REMARK 465     SER B   320                                                      
REMARK 465     PRO B   321                                                      
REMARK 465     GLY B   322                                                      
REMARK 465     ASP B   323                                                      
REMARK 465     SER B   324                                                      
REMARK 465     THR B   353                                                      
REMARK 465     GLN B   354                                                      
REMARK 465     PRO B   355                                                      
REMARK 465     GLY C   205                                                      
REMARK 465     GLU C   206                                                      
REMARK 465     ALA C   207                                                      
REMARK 465     ASP C   208                                                      
REMARK 465     SER C   209                                                      
REMARK 465     GLY C   210                                                      
REMARK 465     ASP C   211                                                      
REMARK 465     GLY C   212                                                      
REMARK 465     ASP C   213                                                      
REMARK 465     SER C   214                                                      
REMARK 465     SER C   215                                                      
REMARK 465     PRO C   318                                                      
REMARK 465     SER C   319                                                      
REMARK 465     SER C   320                                                      
REMARK 465     PRO C   321                                                      
REMARK 465     GLY C   322                                                      
REMARK 465     ASN C   352                                                      
REMARK 465     THR C   353                                                      
REMARK 465     GLN C   354                                                      
REMARK 465     PRO C   355                                                      
REMARK 465     GLY D   205                                                      
REMARK 465     GLU D   206                                                      
REMARK 465     ALA D   207                                                      
REMARK 465     ASP D   208                                                      
REMARK 465     SER D   209                                                      
REMARK 465     GLY D   210                                                      
REMARK 465     ASP D   211                                                      
REMARK 465     GLY D   212                                                      
REMARK 465     ASP D   213                                                      
REMARK 465     SER D   214                                                      
REMARK 465     SER D   215                                                      
REMARK 465     SER D   319                                                      
REMARK 465     SER D   320                                                      
REMARK 465     PRO D   321                                                      
REMARK 465     GLY D   322                                                      
REMARK 465     ASN D   351                                                      
REMARK 465     ASN D   352                                                      
REMARK 465     THR D   353                                                      
REMARK 465     GLN D   354                                                      
REMARK 465     PRO D   355                                                      
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     SER A 215    OG                                                  
REMARK 470     LYS A 221    CD   CE   NZ                                        
REMARK 470     GLU A 222    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 234    CG   CD   CE   NZ                                   
REMARK 470     LYS A 294    CE   NZ                                             
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     GLU A 326    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 351    CG   OD1                                            
REMARK 470     SER B 215    OG                                                  
REMARK 470     LYS B 221    CD   CE   NZ                                        
REMARK 470     GLU B 222    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 234    CG   CD   CE   NZ                                   
REMARK 470     LYS B 251    CE   NZ                                             
REMARK 470     LEU B 325    CG   CD1  CD2                                       
REMARK 470     GLU B 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 330    CE   NZ                                             
REMARK 470     ASN B 351    OD1                                                 
REMARK 470     ASN B 352    CG   OD1                                            
REMARK 470     GLN C 218    CD   OE1  NE2                                       
REMARK 470     LYS C 221    CE   NZ                                             
REMARK 470     LYS C 234    CG   CD   CE   NZ                                   
REMARK 470     LYS C 251    CE   NZ                                             
REMARK 470     LYS C 276    CG   CD   CE   NZ                                   
REMARK 470     LYS C 294    CE   NZ                                             
REMARK 470     LYS C 300    CG   CD   CE   NZ                                   
REMARK 470     LYS C 341    CD   CE   NZ                                        
REMARK 470     ASN C 351    CG   OD1                                            
REMARK 470     GLN D 218    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 221    NZ                                                  
REMARK 470     LYS D 234    CE   NZ                                             
REMARK 470     LYS D 276    CG   CD   CE   NZ                                   
REMARK 470     LYS D 294    CE   NZ                                             
REMARK 470     LYS D 300    CG   CD   CE   NZ                                   
REMARK 470     ASP D 323    CG   OD1  OD2                                       
REMARK 470     LYS D 341    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 223      123.70     79.74                                   
REMARK 500    LYS A 251     -106.02   -111.17                                   
REMARK 500    PHE B 223      125.77     77.76                                   
REMARK 500    LYS B 251     -106.48   -112.34                                   
REMARK 500    PHE C 223      124.53     76.92                                   
REMARK 500    LYS C 251     -106.02   -113.95                                   
REMARK 500    PHE D 223      120.66     82.31                                   
REMARK 500    LYS D 251     -105.08   -111.07                                   
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 359        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH B 104        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH C 362        DISTANCE =  6.56 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB A 356                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB B 356                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB C 356                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB D 356                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2                   
DBREF  3QKJ A  206   355  UNP    Q59H79   Q59H79_HUMAN   293    442             
DBREF  3QKJ B  206   355  UNP    Q59H79   Q59H79_HUMAN   293    442             
DBREF  3QKJ C  206   355  UNP    Q59H79   Q59H79_HUMAN   293    442             
DBREF  3QKJ D  206   355  UNP    Q59H79   Q59H79_HUMAN   293    442             
SEQADV 3QKJ GLY A  205  UNP  Q59H79              EXPRESSION TAG                 
SEQADV 3QKJ GLY B  205  UNP  Q59H79              EXPRESSION TAG                 
SEQADV 3QKJ GLY C  205  UNP  Q59H79              EXPRESSION TAG                 
SEQADV 3QKJ GLY D  205  UNP  Q59H79              EXPRESSION TAG                 
SEQRES   1 A  151  GLY GLU ALA ASP SER GLY ASP GLY ASP SER SER GLU TYR          
SEQRES   2 A  151  GLN ASP GLY LYS GLU PHE GLY ILE GLY ASP LEU VAL TRP          
SEQRES   3 A  151  GLY LYS ILE LYS GLY PHE SER TRP TRP PRO ALA MET VAL          
SEQRES   4 A  151  VAL SER TRP LYS ALA THR SER LYS ARG GLN ALA MET SER          
SEQRES   5 A  151  GLY MET ARG TRP VAL GLN TRP PHE GLY ASP GLY LYS PHE          
SEQRES   6 A  151  SER GLU VAL SER ALA ASP LYS LEU VAL ALA LEU GLY LEU          
SEQRES   7 A  151  PHE SER GLN HIS PHE ASN LEU ALA THR PHE ASN LYS LEU          
SEQRES   8 A  151  VAL SER TYR ARG LYS ALA MET TYR HIS ALA LEU GLU LYS          
SEQRES   9 A  151  ALA ARG VAL ARG ALA GLY LYS THR PHE PRO SER SER PRO          
SEQRES  10 A  151  GLY ASP SER LEU GLU ASP GLN LEU LYS PRO MET LEU GLU          
SEQRES  11 A  151  TRP ALA HIS GLY GLY PHE LYS PRO THR GLY ILE GLU GLY          
SEQRES  12 A  151  LEU LYS PRO ASN ASN THR GLN PRO                              
SEQRES   1 B  151  GLY GLU ALA ASP SER GLY ASP GLY ASP SER SER GLU TYR          
SEQRES   2 B  151  GLN ASP GLY LYS GLU PHE GLY ILE GLY ASP LEU VAL TRP          
SEQRES   3 B  151  GLY LYS ILE LYS GLY PHE SER TRP TRP PRO ALA MET VAL          
SEQRES   4 B  151  VAL SER TRP LYS ALA THR SER LYS ARG GLN ALA MET SER          
SEQRES   5 B  151  GLY MET ARG TRP VAL GLN TRP PHE GLY ASP GLY LYS PHE          
SEQRES   6 B  151  SER GLU VAL SER ALA ASP LYS LEU VAL ALA LEU GLY LEU          
SEQRES   7 B  151  PHE SER GLN HIS PHE ASN LEU ALA THR PHE ASN LYS LEU          
SEQRES   8 B  151  VAL SER TYR ARG LYS ALA MET TYR HIS ALA LEU GLU LYS          
SEQRES   9 B  151  ALA ARG VAL ARG ALA GLY LYS THR PHE PRO SER SER PRO          
SEQRES  10 B  151  GLY ASP SER LEU GLU ASP GLN LEU LYS PRO MET LEU GLU          
SEQRES  11 B  151  TRP ALA HIS GLY GLY PHE LYS PRO THR GLY ILE GLU GLY          
SEQRES  12 B  151  LEU LYS PRO ASN ASN THR GLN PRO                              
SEQRES   1 C  151  GLY GLU ALA ASP SER GLY ASP GLY ASP SER SER GLU TYR          
SEQRES   2 C  151  GLN ASP GLY LYS GLU PHE GLY ILE GLY ASP LEU VAL TRP          
SEQRES   3 C  151  GLY LYS ILE LYS GLY PHE SER TRP TRP PRO ALA MET VAL          
SEQRES   4 C  151  VAL SER TRP LYS ALA THR SER LYS ARG GLN ALA MET SER          
SEQRES   5 C  151  GLY MET ARG TRP VAL GLN TRP PHE GLY ASP GLY LYS PHE          
SEQRES   6 C  151  SER GLU VAL SER ALA ASP LYS LEU VAL ALA LEU GLY LEU          
SEQRES   7 C  151  PHE SER GLN HIS PHE ASN LEU ALA THR PHE ASN LYS LEU          
SEQRES   8 C  151  VAL SER TYR ARG LYS ALA MET TYR HIS ALA LEU GLU LYS          
SEQRES   9 C  151  ALA ARG VAL ARG ALA GLY LYS THR PHE PRO SER SER PRO          
SEQRES  10 C  151  GLY ASP SER LEU GLU ASP GLN LEU LYS PRO MET LEU GLU          
SEQRES  11 C  151  TRP ALA HIS GLY GLY PHE LYS PRO THR GLY ILE GLU GLY          
SEQRES  12 C  151  LEU LYS PRO ASN ASN THR GLN PRO                              
SEQRES   1 D  151  GLY GLU ALA ASP SER GLY ASP GLY ASP SER SER GLU TYR          
SEQRES   2 D  151  GLN ASP GLY LYS GLU PHE GLY ILE GLY ASP LEU VAL TRP          
SEQRES   3 D  151  GLY LYS ILE LYS GLY PHE SER TRP TRP PRO ALA MET VAL          
SEQRES   4 D  151  VAL SER TRP LYS ALA THR SER LYS ARG GLN ALA MET SER          
SEQRES   5 D  151  GLY MET ARG TRP VAL GLN TRP PHE GLY ASP GLY LYS PHE          
SEQRES   6 D  151  SER GLU VAL SER ALA ASP LYS LEU VAL ALA LEU GLY LEU          
SEQRES   7 D  151  PHE SER GLN HIS PHE ASN LEU ALA THR PHE ASN LYS LEU          
SEQRES   8 D  151  VAL SER TYR ARG LYS ALA MET TYR HIS ALA LEU GLU LYS          
SEQRES   9 D  151  ALA ARG VAL ARG ALA GLY LYS THR PHE PRO SER SER PRO          
SEQRES  10 D  151  GLY ASP SER LEU GLU ASP GLN LEU LYS PRO MET LEU GLU          
SEQRES  11 D  151  TRP ALA HIS GLY GLY PHE LYS PRO THR GLY ILE GLU GLY          
SEQRES  12 D  151  LEU LYS PRO ASN ASN THR GLN PRO                              
HET    BTB  A 356      14                                                       
HET    SO4  A   3       5                                                       
HET    SO4  A   4       5                                                       
HET    BTB  B 356      14                                                       
HET    SO4  B   5       5                                                       
HET    SO4  B   6       5                                                       
HET    BTB  C 356      14                                                       
HET    BTB  D 356      14                                                       
HET    SO4  D   1       5                                                       
HET    SO4  D   2       5                                                       
HETNAM     BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-                 
HETNAM   2 BTB  PROPANE-1,3-DIOL                                                
HETNAM     SO4 SULFATE ION                                                      
HETSYN     BTB BIS-TRIS BUFFER                                                  
FORMUL   5  BTB    4(C8 H19 N O5)                                               
FORMUL   6  SO4    6(O4 S 2-)                                                   
FORMUL  15  HOH   *263(H2 O)                                                    
HELIX    1   1 SER A  245  THR A  249  5                                   5    
HELIX    2   2 ASN A  288  LEU A  295  1                                   8    
HELIX    3   3 LEU A  295  GLY A  314  1                                  20    
HELIX    4   4 GLN A  328  GLY A  338  1                                  11    
HELIX    5   5 THR A  343  LYS A  349  5                                   7    
HELIX    6   6 SER B  245  THR B  249  5                                   5    
HELIX    7   7 LEU B  282  PHE B  287  1                                   6    
HELIX    8   8 ASN B  288  LEU B  295  1                                   8    
HELIX    9   9 LEU B  295  GLY B  314  1                                  20    
HELIX   10  10 LEU B  325  GLY B  338  1                                  14    
HELIX   11  11 THR B  343  LYS B  349  5                                   7    
HELIX   12  12 SER C  245  THR C  249  5                                   5    
HELIX   13  13 LEU C  282  PHE C  287  1                                   6    
HELIX   14  14 ASN C  288  LEU C  295  1                                   8    
HELIX   15  15 LEU C  295  GLY C  314  1                                  20    
HELIX   16  16 SER C  324  GLY C  338  1                                  15    
HELIX   17  17 THR C  343  LYS C  349  5                                   7    
HELIX   18  18 SER D  245  THR D  249  5                                   5    
HELIX   19  19 LEU D  282  PHE D  287  1                                   6    
HELIX   20  20 ASN D  288  LEU D  295  1                                   8    
HELIX   21  21 LEU D  295  GLY D  314  1                                  20    
HELIX   22  22 SER D  324  GLY D  338  1                                  15    
HELIX   23  23 THR D  343  LYS D  349  5                                   7    
SHEET    1   A 5 PHE A 269  SER A 273  0                                        
SHEET    2   A 5 MET A 258  TRP A 263 -1  N  ARG A 259   O  VAL A 272           
SHEET    3   A 5 TRP A 239  VAL A 244 -1  N  MET A 242   O  GLN A 262           
SHEET    4   A 5 LEU A 228  GLY A 231 -1  N  GLY A 231   O  TRP A 239           
SHEET    5   A 5 LEU A 277  ALA A 279 -1  O  VAL A 278   N  TRP A 230           
SHEET    1   B 5 PHE B 269  SER B 273  0                                        
SHEET    2   B 5 MET B 258  TRP B 263 -1  N  ARG B 259   O  VAL B 272           
SHEET    3   B 5 TRP B 239  VAL B 244 -1  N  MET B 242   O  GLN B 262           
SHEET    4   B 5 LEU B 228  GLY B 231 -1  N  GLY B 231   O  TRP B 239           
SHEET    5   B 5 LEU B 277  ALA B 279 -1  O  VAL B 278   N  TRP B 230           
SHEET    1   C 5 PHE C 269  SER C 273  0                                        
SHEET    2   C 5 MET C 258  TRP C 263 -1  N  ARG C 259   O  VAL C 272           
SHEET    3   C 5 TRP C 239  VAL C 244 -1  N  MET C 242   O  GLN C 262           
SHEET    4   C 5 LEU C 228  GLY C 231 -1  N  GLY C 231   O  TRP C 239           
SHEET    5   C 5 LEU C 277  ALA C 279 -1  O  VAL C 278   N  TRP C 230           
SHEET    1   D 5 PHE D 269  SER D 273  0                                        
SHEET    2   D 5 MET D 258  TRP D 263 -1  N  ARG D 259   O  VAL D 272           
SHEET    3   D 5 TRP D 239  VAL D 244 -1  N  MET D 242   O  GLN D 262           
SHEET    4   D 5 LEU D 228  GLY D 231 -1  N  GLY D 231   O  TRP D 239           
SHEET    5   D 5 LEU D 277  ALA D 279 -1  O  VAL D 278   N  TRP D 230           
CISPEP   1 LYS A  341    PRO A  342          0         6.82                     
CISPEP   2 LYS B  341    PRO B  342          0         7.94                     
CISPEP   3 LYS C  341    PRO C  342          0         7.33                     
CISPEP   4 LYS D  341    PRO D  342          0         7.30                     
SITE     1 AC1  7 ILE A 233  PHE A 236  TRP A 239  TRP A 263                    
SITE     2 AC1  7 ASP A 266  LYS A 268  HOH A 362                               
SITE     1 AC2  3 LYS A 308  ARG A 312  ASN A 351                               
SITE     1 AC3  3 ARG A 310  THR A 316  LYS D 234                               
SITE     1 AC4  5 HOH B   3  ILE B 233  PHE B 236  TRP B 263                    
SITE     2 AC4  5 ASP B 266                                                     
SITE     1 AC5  2 LYS B 300  ARG C 252                                          
SITE     1 AC6  1 ARG B 252                                                     
SITE     1 AC7  6 ILE C 233  TRP C 239  TRP C 263  ASP C 266                    
SITE     2 AC7  6 LYS C 268  HOH C 367                                          
SITE     1 AC8  7 HOH D 134  ILE D 233  PHE D 236  TRP D 239                    
SITE     2 AC8  7 TRP D 263  ASP D 266  LYS D 268                               
SITE     1 AC9  6 LYS C 232  TRP C 238  HOH C 361  HOH C 364                    
SITE     2 AC9  6 LYS D 232  TRP D 238                                          
SITE     1 BC1  3 LYS D 251  ARG D 252  HOH D 360                               
CRYST1   74.544   74.544  160.266  90.00  90.00 120.00 P 32         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013415  0.007745  0.000000        0.00000                         
SCALE2      0.000000  0.015490  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006240        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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