GenomeNet

Database: PDB
Entry: 5MMF
LinkDB: 5MMF
Original site: 5MMF 
HEADER    TRANSFERASE                             09-DEC-16   5MMF              
TITLE     CRYSTAL STRUCTURE OF CK2ALPHA WITH COMPOUND 7 BOUND                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 2-329 AND N-TERMINAL EXTENSION                    
COMPND   5 GSMDIEFDDDADDDGSGSGSGSGS;                                            
COMPND   6 SYNONYM: CK II ALPHA;                                                
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CSNK2A1, CK2A1;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHAT4                                     
KEYWDS    CK2ALPHA, CK2A, FRAGMENT BASED DRUG DISCOVERY, HIGH CONCENTRATION     
KEYWDS   2 SCREENING, SELECTIVE ATP COMPETITIVE INHIBITORS, SURFACE ENTROPHY    
KEYWDS   3 REDUCTION, TRANSFERASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.BREAR,C.DE FUSCO,K.H.GEORGIOU,D.SPRING,M.HYVONEN                    
REVDAT   3   23-AUG-17 5MMF    1       REMARK                                   
REVDAT   2   07-JUN-17 5MMF    1       JRNL                                     
REVDAT   1   24-MAY-17 5MMF    0                                                
JRNL        AUTH   C.DE FUSCO,P.BREAR,J.IEGRE,K.H.GEORGIOU,H.F.SORE,M.HYVONEN,  
JRNL        AUTH 2 D.R.SPRING                                                   
JRNL        TITL   A FRAGMENT-BASED APPROACH LEADING TO THE DISCOVERY OF A      
JRNL        TITL 2 NOVEL BINDING SITE AND THE SELECTIVE CK2 INHIBITOR CAM4066.  
JRNL        REF    BIOORG. MED. CHEM.            V.  25  3471 2017              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   28495381                                                     
JRNL        DOI    10.1016/J.BMC.2017.04.037                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER                                               
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) : 1.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 167.29                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 51569                          
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)  : 0.203                          
REMARK   3   R VALUE            (WORKING SET)  : 0.202                          
REMARK   3   FREE R VALUE                      : 0.219                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.080                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2619                           
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) : 1.99                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.04                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.30                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3491                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2308                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3321                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2298                   
REMARK   3   BIN FREE R VALUE                        : 0.2519                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.87                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 170                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5495                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 235                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.85                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.70110                                              
REMARK   3    B22 (A**2) : -11.30230                                            
REMARK   3    B33 (A**2) : 9.60120                                              
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) : 0.276               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.185               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.146               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.183               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.146               
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      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5760   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7793   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2042   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 144    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 864    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5760   ; 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   : 689    ; 5.000  ; SEMIHARMONIC        
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   : 6588   ; 0.000  ; SEMIHARMONIC        
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) : 2.85                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.94                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   15.6680  144.1307  356.0817           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0916 T22:   -0.0281                                    
REMARK   3     T33:   -0.0488 T12:   -0.0234                                    
REMARK   3     T13:    0.0075 T23:   -0.0120                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2375 L22:    0.3494                                    
REMARK   3     L33:    0.6598 L12:   -0.0130                                    
REMARK   3     L13:    0.0605 L23:   -0.1429                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0260 S12:   -0.0371 S13:   -0.0043                     
REMARK   3     S21:    0.0185 S22:   -0.0228 S23:    0.0127                     
REMARK   3     S31:   -0.0168 S32:    0.0062 S33:   -0.0032                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.2022  155.4107  396.8015           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1051 T22:    0.1670                                    
REMARK   3     T33:   -0.1637 T12:   -0.0125                                    
REMARK   3     T13:    0.0413 T23:    0.0193                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0702 L22:    0.4090                                    
REMARK   3     L33:    1.8332 L12:   -0.0097                                    
REMARK   3     L13:    1.2587 L23:   -0.3260                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0618 S12:   -0.4763 S13:    0.0342                     
REMARK   3     S21:   -0.1867 S22:    0.1045 S23:   -0.1009                     
REMARK   3     S31:    0.0920 S32:   -0.5442 S33:   -0.0427                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5MMF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200002673.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9600                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS (VERSION JANUARY 10,           
REMARK 200                                   AUTOPROC                           
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.2.14, CCP4 6.4           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51653                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.989                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 167.290                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.14400                            
REMARK 200  R SYM                      (I) : 0.14400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.31600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, PHASER                                        
REMARK 200 STARTING MODEL: 5CVH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 112.5MM MES PH 6.5, 35% GLYCEROL         
REMARK 280  ETHOXYLATE, 180 MM AMMONIUM ACETATE, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 298K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      167.28600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      167.28600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       32.20400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       34.31550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       32.20400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       34.31550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      167.28600            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       32.20400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       34.31550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      167.28600            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       32.20400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       34.31550            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 662  LIES ON A SPECIAL POSITION.                          
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   -22                                                      
REMARK 465     SER A   -21                                                      
REMARK 465     MET A   -20                                                      
REMARK 465     ASP A   -19                                                      
REMARK 465     ILE A   -18                                                      
REMARK 465     GLU A   -17                                                      
REMARK 465     PHE A   -16                                                      
REMARK 465     ASP A   -15                                                      
REMARK 465     ASP A   -14                                                      
REMARK 465     ASP A   -13                                                      
REMARK 465     ALA A   -12                                                      
REMARK 465     ASP A   -11                                                      
REMARK 465     ASP A   -10                                                      
REMARK 465     ASP A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     SER A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     LYS A   329                                                      
REMARK 465     GLY B   -22                                                      
REMARK 465     SER B   -21                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     ASP B   -19                                                      
REMARK 465     ILE B   -18                                                      
REMARK 465     GLU B   -17                                                      
REMARK 465     PHE B   -16                                                      
REMARK 465     ASP B   -15                                                      
REMARK 465     ASP B   -14                                                      
REMARK 465     ASP B   -13                                                      
REMARK 465     ALA B   -12                                                      
REMARK 465     ASP B   -11                                                      
REMARK 465     ASP B   -10                                                      
REMARK 465     ASP B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     SER B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     SER B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     VAL B   328                                                      
REMARK 465     LYS B   329                                                      
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   OXT  ACT A   404     O    HOH A   501              1.04            
REMARK 500   C    ACT A   404     O    HOH A   501              1.29            
REMARK 500   O    ACT A   404     O    HOH A   501              1.74            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CG2  VAL A    73     O    TYR A   325     5545     1.96            
REMARK 500   CG1  VAL B    73     O    TYR B   325     5545     2.13            
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    PRO A  72       76.55    -65.87                                   
REMARK 500    VAL A 105      -82.06    -83.86                                   
REMARK 500    ASP A 156       38.26   -142.43                                   
REMARK 500    ASP A 175       80.05     52.11                                   
REMARK 500    ALA A 193      164.11     63.73                                   
REMARK 500    ALA A 193      163.96     63.73                                   
REMARK 500    ARG A 195      -57.77    -28.33                                   
REMARK 500    ASP A 210     -158.99   -142.65                                   
REMARK 500    HIS A 234       75.13   -101.54                                   
REMARK 500    VAL A 248      -62.02   -101.75                                   
REMARK 500    PRO B  72       94.70    -62.85                                   
REMARK 500    TYR B 125      -55.04   -141.89                                   
REMARK 500    ASP B 156       37.31   -145.76                                   
REMARK 500    ASP B 165       74.23   -109.93                                   
REMARK 500    ASP B 175       81.37     52.02                                   
REMARK 500    ALA B 193      164.26     63.19                                   
REMARK 500    ALA B 193      164.15     63.19                                   
REMARK 500    ARG B 195      -57.62    -27.06                                   
REMARK 500    ARG B 195      -57.62    -29.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  19         0.09    SIDE CHAIN                              
REMARK 500    ARG B  19         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JMB A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 401                 
DBREF  5MMF A    2   329  UNP    P68400   CSK21_HUMAN      2    329             
DBREF  5MMF B    2   329  UNP    P68400   CSK21_HUMAN      2    329             
SEQADV 5MMF GLY A  -22  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER A  -21  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF MET A  -20  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP A  -19  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ILE A  -18  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLU A  -17  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF PHE A  -16  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP A  -15  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP A  -14  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP A  -13  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ALA A  -12  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP A  -11  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP A  -10  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP A   -9  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLY A   -8  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER A   -7  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLY A   -6  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER A   -5  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLY A   -4  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER A   -3  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLY A   -2  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER A   -1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLY A    0  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER A    1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER A   21  UNP  P68400    ARG    21 ENGINEERED MUTATION            
SEQADV 5MMF GLY B  -22  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER B  -21  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF MET B  -20  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP B  -19  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ILE B  -18  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLU B  -17  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF PHE B  -16  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP B  -15  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP B  -14  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP B  -13  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ALA B  -12  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP B  -11  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP B  -10  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF ASP B   -9  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLY B   -8  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER B   -7  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLY B   -6  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER B   -5  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLY B   -4  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER B   -3  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLY B   -2  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER B   -1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF GLY B    0  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER B    1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MMF SER B   21  UNP  P68400    ARG    21 ENGINEERED MUTATION            
SEQRES   1 A  352  GLY SER MET ASP ILE GLU PHE ASP ASP ASP ALA ASP ASP          
SEQRES   2 A  352  ASP GLY SER GLY SER GLY SER GLY SER GLY SER SER GLY          
SEQRES   3 A  352  PRO VAL PRO SER ARG ALA ARG VAL TYR THR ASP VAL ASN          
SEQRES   4 A  352  THR HIS ARG PRO SER GLU TYR TRP ASP TYR GLU SER HIS          
SEQRES   5 A  352  VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR GLN LEU VAL          
SEQRES   6 A  352  ARG LYS LEU GLY ARG GLY LYS TYR SER GLU VAL PHE GLU          
SEQRES   7 A  352  ALA ILE ASN ILE THR ASN ASN GLU LYS VAL VAL VAL LYS          
SEQRES   8 A  352  ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE LYS ARG GLU          
SEQRES   9 A  352  ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY PRO ASN ILE          
SEQRES  10 A  352  ILE THR LEU ALA ASP ILE VAL LYS ASP PRO VAL SER ARG          
SEQRES  11 A  352  THR PRO ALA LEU VAL PHE GLU HIS VAL ASN ASN THR ASP          
SEQRES  12 A  352  PHE LYS GLN LEU TYR GLN THR LEU THR ASP TYR ASP ILE          
SEQRES  13 A  352  ARG PHE TYR MET TYR GLU ILE LEU LYS ALA LEU ASP TYR          
SEQRES  14 A  352  CYS HIS SER MET GLY ILE MET HIS ARG ASP VAL LYS PRO          
SEQRES  15 A  352  HIS ASN VAL MET ILE ASP HIS GLU HIS ARG LYS LEU ARG          
SEQRES  16 A  352  LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR HIS PRO GLY          
SEQRES  17 A  352  GLN GLU TYR ASN VAL ARG VAL ALA SER ARG TYR PHE LYS          
SEQRES  18 A  352  GLY PRO GLU LEU LEU VAL ASP TYR GLN MET TYR ASP TYR          
SEQRES  19 A  352  SER LEU ASP MET TRP SER LEU GLY CYS MET LEU ALA SER          
SEQRES  20 A  352  MET ILE PHE ARG LYS GLU PRO PHE PHE HIS GLY HIS ASP          
SEQRES  21 A  352  ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS VAL LEU GLY          
SEQRES  22 A  352  THR GLU ASP LEU TYR ASP TYR ILE ASP LYS TYR ASN ILE          
SEQRES  23 A  352  GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU GLY ARG HIS          
SEQRES  24 A  352  SER ARG LYS ARG TRP GLU ARG PHE VAL HIS SER GLU ASN          
SEQRES  25 A  352  GLN HIS LEU VAL SER PRO GLU ALA LEU ASP PHE LEU ASP          
SEQRES  26 A  352  LYS LEU LEU ARG TYR ASP HIS GLN SER ARG LEU THR ALA          
SEQRES  27 A  352  ARG GLU ALA MET GLU HIS PRO TYR PHE TYR THR VAL VAL          
SEQRES  28 A  352  LYS                                                          
SEQRES   1 B  352  GLY SER MET ASP ILE GLU PHE ASP ASP ASP ALA ASP ASP          
SEQRES   2 B  352  ASP GLY SER GLY SER GLY SER GLY SER GLY SER SER GLY          
SEQRES   3 B  352  PRO VAL PRO SER ARG ALA ARG VAL TYR THR ASP VAL ASN          
SEQRES   4 B  352  THR HIS ARG PRO SER GLU TYR TRP ASP TYR GLU SER HIS          
SEQRES   5 B  352  VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR GLN LEU VAL          
SEQRES   6 B  352  ARG LYS LEU GLY ARG GLY LYS TYR SER GLU VAL PHE GLU          
SEQRES   7 B  352  ALA ILE ASN ILE THR ASN ASN GLU LYS VAL VAL VAL LYS          
SEQRES   8 B  352  ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE LYS ARG GLU          
SEQRES   9 B  352  ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY PRO ASN ILE          
SEQRES  10 B  352  ILE THR LEU ALA ASP ILE VAL LYS ASP PRO VAL SER ARG          
SEQRES  11 B  352  THR PRO ALA LEU VAL PHE GLU HIS VAL ASN ASN THR ASP          
SEQRES  12 B  352  PHE LYS GLN LEU TYR GLN THR LEU THR ASP TYR ASP ILE          
SEQRES  13 B  352  ARG PHE TYR MET TYR GLU ILE LEU LYS ALA LEU ASP TYR          
SEQRES  14 B  352  CYS HIS SER MET GLY ILE MET HIS ARG ASP VAL LYS PRO          
SEQRES  15 B  352  HIS ASN VAL MET ILE ASP HIS GLU HIS ARG LYS LEU ARG          
SEQRES  16 B  352  LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR HIS PRO GLY          
SEQRES  17 B  352  GLN GLU TYR ASN VAL ARG VAL ALA SER ARG TYR PHE LYS          
SEQRES  18 B  352  GLY PRO GLU LEU LEU VAL ASP TYR GLN MET TYR ASP TYR          
SEQRES  19 B  352  SER LEU ASP MET TRP SER LEU GLY CYS MET LEU ALA SER          
SEQRES  20 B  352  MET ILE PHE ARG LYS GLU PRO PHE PHE HIS GLY HIS ASP          
SEQRES  21 B  352  ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS VAL LEU GLY          
SEQRES  22 B  352  THR GLU ASP LEU TYR ASP TYR ILE ASP LYS TYR ASN ILE          
SEQRES  23 B  352  GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU GLY ARG HIS          
SEQRES  24 B  352  SER ARG LYS ARG TRP GLU ARG PHE VAL HIS SER GLU ASN          
SEQRES  25 B  352  GLN HIS LEU VAL SER PRO GLU ALA LEU ASP PHE LEU ASP          
SEQRES  26 B  352  LYS LEU LEU ARG TYR ASP HIS GLN SER ARG LEU THR ALA          
SEQRES  27 B  352  ARG GLU ALA MET GLU HIS PRO TYR PHE TYR THR VAL VAL          
SEQRES  28 B  352  LYS                                                          
HET    JMB  A 401      36                                                       
HET    ACT  A 402       4                                                       
HET    ACT  A 403       4                                                       
HET    ACT  A 404       4                                                       
HET    ACT  A 405       4                                                       
HET    ACT  B 401       4                                                       
HETNAM     JMB (3-CHLORANYL-4-PHENYL-PHENYL)METHYL-PROPYL-AZANIUM               
HETNAM     ACT ACETATE ION                                                      
FORMUL   3  JMB    C16 H19 CL N 1+                                              
FORMUL   4  ACT    5(C2 H3 O2 1-)                                               
FORMUL   9  HOH   *235(H2 O)                                                    
HELIX    1 AA1 PRO A   20  ASP A   25  1                                   6    
HELIX    2 AA2 LYS A   74  ARG A   89  1                                  16    
HELIX    3 AA3 ASP A  120  LEU A  128  1                                   9    
HELIX    4 AA4 THR A  129  MET A  150  1                                  22    
HELIX    5 AA5 LYS A  158  HIS A  160  5                                   3    
HELIX    6 AA6 SER A  194  LYS A  198  5                                   5    
HELIX    7 AA7 GLY A  199  VAL A  204  1                                   6    
HELIX    8 AA8 TYR A  211  ARG A  228  1                                  18    
HELIX    9 AA9 ASP A  237  GLY A  250  1                                  14    
HELIX   10 AB1 GLY A  250  TYR A  261  1                                  12    
HELIX   11 AB2 ASP A  266  ASN A  270  5                                   5    
HELIX   12 AB3 ARG A  280  VAL A  285  5                                   6    
HELIX   13 AB4 ASN A  289  VAL A  293  5                                   5    
HELIX   14 AB5 SER A  294  LEU A  305  1                                  12    
HELIX   15 AB6 ASP A  308  ARG A  312  5                                   5    
HELIX   16 AB7 THR A  314  GLU A  320  1                                   7    
HELIX   17 AB8 HIS A  321  TYR A  325  5                                   5    
HELIX   18 AB9 PRO B   20  ASP B   25  1                                   6    
HELIX   19 AC1 TYR B   26  HIS B   29  5                                   4    
HELIX   20 AC2 LYS B   74  ARG B   89  1                                  16    
HELIX   21 AC3 LYS B  122  THR B  127  1                                   6    
HELIX   22 AC4 THR B  129  MET B  150  1                                  22    
HELIX   23 AC5 LYS B  158  HIS B  160  5                                   3    
HELIX   24 AC6 SER B  194  LYS B  198  5                                   5    
HELIX   25 AC7 GLY B  199  VAL B  204  1                                   6    
HELIX   26 AC8 TYR B  211  PHE B  227  1                                  17    
HELIX   27 AC9 ASP B  237  GLY B  250  1                                  14    
HELIX   28 AD1 GLY B  250  TYR B  261  1                                  12    
HELIX   29 AD2 ASP B  266  ASN B  270  5                                   5    
HELIX   30 AD3 ARG B  280  VAL B  285  5                                   6    
HELIX   31 AD4 ASN B  289  VAL B  293  5                                   5    
HELIX   32 AD5 SER B  294  LEU B  305  1                                  12    
HELIX   33 AD6 ASP B  308  ARG B  312  5                                   5    
HELIX   34 AD7 THR B  314  HIS B  321  1                                   8    
HELIX   35 AD8 PRO B  322  TYR B  325  5                                   4    
SHEET    1 AA1 6 GLY A  34  ASN A  35  0                                        
SHEET    2 AA1 6 LEU A  97  LYS A 102  1  O  ILE A 100   N  GLY A  34           
SHEET    3 AA1 6 PRO A 109  GLU A 114 -1  O  VAL A 112   N  ASP A  99           
SHEET    4 AA1 6 LYS A  64  LEU A  70 -1  N  VAL A  66   O  PHE A 113           
SHEET    5 AA1 6 SER A  51  ASN A  58 -1  N  ALA A  56   O  VAL A  65           
SHEET    6 AA1 6 TYR A  39  ARG A  47 -1  N  LEU A  45   O  VAL A  53           
SHEET    1 AA2 2 ILE A 152  MET A 153  0                                        
SHEET    2 AA2 2 GLU A 180  PHE A 181 -1  O  GLU A 180   N  MET A 153           
SHEET    1 AA3 2 VAL A 162  ASP A 165  0                                        
SHEET    2 AA3 2 LYS A 170  LEU A 173 -1  O  ARG A 172   N  MET A 163           
SHEET    1 AA4 6 GLY B  34  ASN B  35  0                                        
SHEET    2 AA4 6 LEU B  97  LYS B 102  1  O  ILE B 100   N  GLY B  34           
SHEET    3 AA4 6 PRO B 109  GLU B 114 -1  O  VAL B 112   N  ASP B  99           
SHEET    4 AA4 6 LYS B  64  LEU B  70 -1  N  VAL B  66   O  PHE B 113           
SHEET    5 AA4 6 SER B  51  ASN B  58 -1  N  GLU B  52   O  ILE B  69           
SHEET    6 AA4 6 TYR B  39  ARG B  47 -1  N  LEU B  45   O  VAL B  53           
SHEET    1 AA5 2 ILE B 152  MET B 153  0                                        
SHEET    2 AA5 2 GLU B 180  PHE B 181 -1  O  GLU B 180   N  MET B 153           
SHEET    1 AA6 2 VAL B 162  ASP B 165  0                                        
SHEET    2 AA6 2 LYS B 170  LEU B 173 -1  O  ARG B 172   N  MET B 163           
CISPEP   1 GLU A  230    PRO A  231          0        -4.58                     
CISPEP   2 GLU B  230    PRO B  231          0        -8.28                     
SITE     1 AC1  8 ASN A 118  LEU A 124  MET A 137  PRO A 159                    
SITE     2 AC1  8 VAL A 162  MET A 163  ILE A 164  MET A 225                    
SITE     1 AC2  6 LYS A  68  PHE A 113  ILE A 174  ASP A 175                    
SITE     2 AC2  6 HOH A 509  HOH A 608                                          
SITE     1 AC3  3 HIS A 276  SER A 277  LYS A 279                               
SITE     1 AC4  2 HIS A 234  HOH A 501                                          
SITE     1 AC5  4 ARG A  80  ARG A 155  LEU A 178  HOH A 613                    
SITE     1 AC6  4 ARG B 195  TYR B 196  HIS B 234  ARG B 244                    
CRYST1   64.408   68.631  334.572  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015526  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014571  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002989        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system