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Database: PDB
Entry: 5MO8
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Original site: 5MO8 
HEADER    TRANSFERASE                             13-DEC-16   5MO8              
TITLE     CRYSTAL STRUCTURE OF CK2ALPHA WITH N-(3-(((2-CHLORO-[1,1'-BIPHENYL]-4-
TITLE    2 YL)METHYL)AMINO)PROPYL)METHANESULFONAMIDE 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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: 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.GEORGIOU,J.IEGRE,H.SORE,M.HYVONEN,D.SPRING       
REVDAT   2   07-JUN-17 5MO8    1       JRNL                                     
REVDAT   1   24-MAY-17 5MO8    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.    1.82 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) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 167.46                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 66669                          
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)  : 0.205                          
REMARK   3   R VALUE            (WORKING SET)  : 0.205                          
REMARK   3   FREE R VALUE                      : 0.219                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3370                           
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               : NULL                     
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.82                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.86                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.79                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4574                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2289                   
REMARK   3   BIN FREE R VALUE                        : 0.2394                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.12                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 247                      
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            : 5487                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 90                                      
REMARK   3   SOLVENT ATOMS            : 211                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.89                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.21990                                              
REMARK   3    B22 (A**2) : -10.54250                                            
REMARK   3    B33 (A**2) : 7.32260                                              
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) : 0.278               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.134               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.115               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.136               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.117               
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      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5781   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7822   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2057   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 144    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 884    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5781   ; 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   : 688    ; 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   : 6648   ; 0.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.95                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.84                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.62                    
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):   15.3514  141.7852  356.5037           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0778 T22:   -0.0116                                    
REMARK   3     T33:   -0.0324 T12:   -0.0417                                    
REMARK   3     T13:    0.0085 T23:   -0.0297                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3015 L22:    0.3672                                    
REMARK   3     L33:    0.6120 L12:    0.1396                                    
REMARK   3     L13:    0.1271 L23:   -0.1869                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0761 S12:   -0.0980 S13:    0.0429                     
REMARK   3     S21:    0.0199 S22:   -0.0870 S23:    0.0384                     
REMARK   3     S31:   -0.0070 S32:    0.0014 S33:    0.0109                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.4364  152.8616  397.1338           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0312 T22:    0.2621                                    
REMARK   3     T33:   -0.2226 T12:   -0.0381                                    
REMARK   3     T13:    0.0515 T23:   -0.0253                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.3763 L22:    0.3327                                    
REMARK   3     L33:    1.7625 L12:    0.0067                                    
REMARK   3     L13:    0.7144 L23:    0.2091                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1395 S12:   -0.5191 S13:    0.0700                     
REMARK   3     S21:   -0.2712 S22:    0.1369 S23:   -0.1049                     
REMARK   3     S31:    0.1588 S32:   -0.5442 S33:    0.0026                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5MO8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200002762.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-SEP-15                          
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) : 0.976250                           
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 NOVEMBER 3,           
REMARK 200                                   AUTOPROC                           
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.4, CCP4 6.5.           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66762                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 167.460                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5CVH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
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      167.46050            
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      167.46050            
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       32.29800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       33.74750            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       32.29800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       33.74750            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      167.46050            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       32.29800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       33.74750            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      167.46050            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       32.29800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       33.74750            
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 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 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 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     GLY A     3                                                      
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     GLY B     3                                                      
REMARK 465     VAL B   328                                                      
REMARK 465     LYS B   329                                                      
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   OE2  GLU A   264     NH1  ARG A   280     8597     1.75            
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    VAL A  42      -61.22    -98.41                                   
REMARK 500    ASP A 156       41.79   -149.75                                   
REMARK 500    ASP A 175       79.95     52.05                                   
REMARK 500    ALA A 193      172.71     62.06                                   
REMARK 500    ALA A 193      171.98     62.06                                   
REMARK 500    ARG A 195      -59.79    -24.02                                   
REMARK 500    ARG A 195      -59.79    -29.44                                   
REMARK 500    VAL B  42      -61.04    -98.52                                   
REMARK 500    ASP B 156       39.95   -151.95                                   
REMARK 500    ASP B 175       74.62     52.70                                   
REMARK 500    ALA B 193      171.13     63.33                                   
REMARK 500    ALA B 193      170.48     63.33                                   
REMARK 500    ARG B 195      -60.73    -22.76                                   
REMARK 500    ARG B 195      -60.73    -28.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG B  19        -10.04                                           
REMARK 500    ARG B  19        -10.51                                           
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 ACT 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 C98 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C98 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 402                 
DBREF  5MO8 A    2   329  UNP    P68400   CSK21_HUMAN      2    329             
DBREF  5MO8 B    2   329  UNP    P68400   CSK21_HUMAN      2    329             
SEQADV 5MO8 GLY A  -22  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER A  -21  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 MET A  -20  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP A  -19  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ILE A  -18  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLU A  -17  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 PHE A  -16  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP A  -15  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP A  -14  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP A  -13  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ALA A  -12  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP A  -11  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP A  -10  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP A   -9  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLY A   -8  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER A   -7  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLY A   -6  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER A   -5  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLY A   -4  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER A   -3  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLY A   -2  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER A   -1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLY A    0  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER A    1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER A   21  UNP  P68400    ARG    21 ENGINEERED MUTATION            
SEQADV 5MO8 GLY B  -22  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER B  -21  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 MET B  -20  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP B  -19  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ILE B  -18  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLU B  -17  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 PHE B  -16  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP B  -15  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP B  -14  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP B  -13  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ALA B  -12  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP B  -11  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP B  -10  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 ASP B   -9  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLY B   -8  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER B   -7  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLY B   -6  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER B   -5  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLY B   -4  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER B   -3  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLY B   -2  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER B   -1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 GLY B    0  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 SER B    1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5MO8 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    ACT  A 401       4                                                       
HET    ACT  A 402       4                                                       
HET    ACT  A 403       4                                                       
HET    C98  A 404      34                                                       
HET    PO4  A 405       5                                                       
HET    C98  B 401      34                                                       
HET    PO4  B 402       5                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM     C98 3-[[3-[3-[(3-CHLORANYL-4-PHENYL-PHENYL)                          
HETNAM   2 C98  METHYLAMINO]PROPYLAMINO]-3-OXIDANYLIDENE-                       
HETNAM   3 C98  PROPANOYL]AMINO]BENZOIC ACID                                    
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   3  ACT    3(C2 H3 O2 1-)                                               
FORMUL   6  C98    2(C26 H26 CL N3 O4)                                          
FORMUL   7  PO4    2(O4 P 3-)                                                   
FORMUL  10  HOH   *211(H2 O)                                                    
HELIX    1 AA1 PRO A   20  ASP A   25  1                                   6    
HELIX    2 AA2 TYR A   26  HIS A   29  5                                   4    
HELIX    3 AA3 LYS A   74  ARG A   89  1                                  16    
HELIX    4 AA4 ASP A  120  LEU A  128  1                                   9    
HELIX    5 AA5 THR A  129  MET A  150  1                                  22    
HELIX    6 AA6 LYS A  158  HIS A  160  5                                   3    
HELIX    7 AA7 HIS A  166  ARG A  169  5                                   4    
HELIX    8 AA8 SER A  194  LYS A  198  5                                   5    
HELIX    9 AA9 GLY A  199  VAL A  204  1                                   6    
HELIX   10 AB1 TYR A  211  ARG A  228  1                                  18    
HELIX   11 AB2 ASP A  237  GLY A  250  1                                  14    
HELIX   12 AB3 GLY A  250  TYR A  261  1                                  12    
HELIX   13 AB4 ASP A  266  ASN A  270  5                                   5    
HELIX   14 AB5 ARG A  280  VAL A  285  5                                   6    
HELIX   15 AB6 ASN A  289  VAL A  293  5                                   5    
HELIX   16 AB7 SER A  294  LEU A  305  1                                  12    
HELIX   17 AB8 ASP A  308  ARG A  312  5                                   5    
HELIX   18 AB9 THR A  314  GLU A  320  1                                   7    
HELIX   19 AC1 HIS A  321  TYR A  325  5                                   5    
HELIX   20 AC2 PRO B   20  ASP B   25  1                                   6    
HELIX   21 AC3 TYR B   26  HIS B   29  5                                   4    
HELIX   22 AC4 LYS B   74  ARG B   89  1                                  16    
HELIX   23 AC5 ASP B  120  LEU B  128  1                                   9    
HELIX   24 AC6 THR B  129  MET B  150  1                                  22    
HELIX   25 AC7 LYS B  158  HIS B  160  5                                   3    
HELIX   26 AC8 ASP B  175  ALA B  179  5                                   5    
HELIX   27 AC9 SER B  194  LYS B  198  5                                   5    
HELIX   28 AD1 GLY B  199  VAL B  204  1                                   6    
HELIX   29 AD2 TYR B  211  ARG B  228  1                                  18    
HELIX   30 AD3 ASP B  237  GLY B  250  1                                  14    
HELIX   31 AD4 GLY B  250  TYR B  261  1                                  12    
HELIX   32 AD5 ASP B  266  ASN B  270  5                                   5    
HELIX   33 AD6 ARG B  280  VAL B  285  5                                   6    
HELIX   34 AD7 ASN B  289  VAL B  293  5                                   5    
HELIX   35 AD8 SER B  294  LEU B  305  1                                  12    
HELIX   36 AD9 ASP B  308  ARG B  312  5                                   5    
HELIX   37 AE1 THR B  314  GLU B  320  1                                   7    
HELIX   38 AE2 HIS B  321  TYR B  325  5                                   5    
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  ALA A  98           
SHEET    4 AA1 6 GLU A  63  LEU A  70 -1  N  LYS A  68   O  LEU A 111           
SHEET    5 AA1 6 SER A  51  ASN A  58 -1  N  ASN A  58   O  GLU A  63           
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  ALA B  98           
SHEET    4 AA4 6 GLU B  63  LEU B  70 -1  N  LYS B  68   O  LEU B 111           
SHEET    5 AA4 6 SER B  51  ASN B  58 -1  N  ASN B  58   O  GLU B  63           
SHEET    6 AA4 6 TYR B  39  ARG B  47 -1  N  ARG B  43   O  GLU B  55           
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  LYS B 170   N  ASP B 165           
CISPEP   1 GLU A  230    PRO A  231          0        -4.37                     
CISPEP   2 GLU B  230    PRO B  231          0        -5.42                     
SITE     1 AC1  2 ARG A  80  ARG A 155                                          
SITE     1 AC2  3 HIS A 276  SER A 277  LYS A 279                               
SITE     1 AC3  4 LEU A 203  ASN A 238  TYR A 239  HOH A 577                    
SITE     1 AC4 18 VAL A  66  LYS A  68  PHE A 113  ASN A 118                    
SITE     2 AC4 18 PHE A 121  TYR A 136  PRO A 159  HIS A 160                    
SITE     3 AC4 18 VAL A 162  MET A 163  ILE A 164  ILE A 174                    
SITE     4 AC4 18 ASP A 175  MET A 221  MET A 225  HOH A 534                    
SITE     5 AC4 18 HOH A 555  HOH A 556                                          
SITE     1 AC5  3 ARG A 244  LYS A 247  HOH A 501                               
SITE     1 AC6 15 LYS B  68  PHE B 113  ASN B 118  PHE B 121                    
SITE     2 AC6 15 PRO B 159  HIS B 160  VAL B 162  MET B 163                    
SITE     3 AC6 15 ILE B 164  ILE B 174  ASP B 175  MET B 221                    
SITE     4 AC6 15 MET B 225  HOH B 510  HOH B 529                               
SITE     1 AC7  6 ARG B 195  TYR B 196  HIS B 234  GLY B 235                    
SITE     2 AC7  6 ARG B 244  LYS B 247                                          
CRYST1   64.596   67.495  334.921  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      0.015481  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014816  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002986        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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