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Database: PDB
Entry: 5CU2
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HEADER    TRANSFERASE                             24-JUL-15   5CU2              
TITLE     CRYSTAL STRUCTURE OF CK2ALPHA WITH 2-HYDROXY-5-METHYLBENZOIC ACID AND 
TITLE    2 (METHYL 4-((3-(3-CHLORO-4-(PHENYL)BENZYLAMINO)PROPYL)AMINO)-4-       
TITLE    3 OXOBUTANOAT 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_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   07-JUN-17 5CU2    1       JRNL                                     
REVDAT   2   24-MAY-17 5CU2    1       JRNL                                     
REVDAT   1   30-NOV-16 5CU2    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.    1.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT                                           
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 167.18                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 73933                          
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)  : 0.184                          
REMARK   3   R VALUE            (WORKING SET)  : 0.183                          
REMARK   3   FREE R VALUE                      : 0.204                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.020                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3709                           
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) : 1.70                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.74                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 90.06                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2807                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2570                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2678                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2556                   
REMARK   3   BIN FREE R VALUE                        : 0.2874                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.60                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 129                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5510                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 144                                     
REMARK   3   SOLVENT ATOMS            : 330                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.15                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.09530                                              
REMARK   3    B22 (A**2) : -8.00950                                             
REMARK   3    B33 (A**2) : 6.91420                                              
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) : 0.230               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.112               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.102               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.112               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.102               
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      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5872   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7954   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2072   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 146    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 936    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5872   ; 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   : 693    ; 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   : 6867   ; 0.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.011                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.98                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.18                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.68                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   15.7149  143.2790  355.8380           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0679 T22:   -0.0832                                    
REMARK   3     T33:   -0.0281 T12:   -0.0175                                    
REMARK   3     T13:    0.0072 T23:   -0.0059                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3112 L22:    0.4041                                    
REMARK   3     L33:    0.7509 L12:    0.0252                                    
REMARK   3     L13:   -0.0098 L23:   -0.0960                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0247 S12:   -0.0342 S13:   -0.0031                     
REMARK   3     S21:    0.0079 S22:   -0.0175 S23:    0.0044                     
REMARK   3     S31:   -0.0292 S32:    0.0140 S33:   -0.0072                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.2333  154.4700  396.6490           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0836 T22:    0.0644                                    
REMARK   3     T33:   -0.1432 T12:   -0.0254                                    
REMARK   3     T13:    0.0158 T23:    0.0183                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9614 L22:    0.4347                                    
REMARK   3     L33:    1.8705 L12:    0.1305                                    
REMARK   3     L13:    0.9349 L23:   -0.2734                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0013 S12:   -0.4911 S13:    0.0219                     
REMARK   3     S21:   -0.1540 S22:    0.0695 S23:   -0.0955                     
REMARK   3     S31:    0.1109 S32:   -0.5390 S33:   -0.0708                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   11.3834  145.2760  375.3050           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0414 T22:   -0.1188                                    
REMARK   3     T33:    0.0011 T12:   -0.1023                                    
REMARK   3     T13:    0.0435 T23:    0.0120                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0937 L22:    0.1944                                    
REMARK   3     L33:    1.1976 L12:   -0.6742                                    
REMARK   3     L13:   -0.3006 L23:    0.4196                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0171 S12:   -0.1885 S13:    0.0052                     
REMARK   3     S21:   -0.0712 S22:   -0.0869 S23:    0.1702                     
REMARK   3     S31:    0.0780 S32:   -0.1431 S33:    0.0698                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5CU2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212188.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-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                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.2.14                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73934                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.705                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 167.180                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 52.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.75900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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: 3WAR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 107MM MES PH 6.5, 29% GLYCEROL           
REMARK 280  ETHOXYLATE, 1 M AMMONIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  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      167.18000            
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      167.18000            
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       32.39000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       34.12850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       32.39000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       34.12850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      167.18000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       32.39000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       34.12850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      167.18000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       32.39000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       34.12850            
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 575  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     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   CE1  PHE B   121     OE1  GLU B   230              1.95            
REMARK 500   OD2  ASP A   259     O    HOH A   501              2.14            
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    ASP A 156       39.46   -149.49                                   
REMARK 500    ASP A 175       77.73     51.16                                   
REMARK 500    ALA A 193      163.50     61.24                                   
REMARK 500    ALA A 193      164.87     61.24                                   
REMARK 500    MET A 208       53.97    -91.65                                   
REMARK 500    ASP A 210     -159.83   -149.15                                   
REMARK 500    ASP B 156       39.75   -150.15                                   
REMARK 500    ASP B 175       74.97     50.36                                   
REMARK 500    ALA B 193      161.82     62.21                                   
REMARK 500    ASP B 210     -159.86   -146.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     551 A  402                                                       
REMARK 610     551 A  403                                                       
REMARK 610     551 B  402                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 551 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 551 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 551 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 54G 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 ACT A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 551 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 551 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 54G B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 405                 
DBREF  5CU2 A    2   329  UNP    P68400   CSK21_HUMAN      2    329             
DBREF  5CU2 B    2   329  UNP    P68400   CSK21_HUMAN      2    329             
SEQADV 5CU2 GLY A  -22  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER A  -21  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 MET A  -20  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP A  -19  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ILE A  -18  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLU A  -17  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 PHE A  -16  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP A  -15  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP A  -14  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP A  -13  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ALA A  -12  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP A  -11  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP A  -10  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP A   -9  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLY A   -8  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER A   -7  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLY A   -6  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER A   -5  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLY A   -4  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER A   -3  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLY A   -2  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER A   -1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLY A    0  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER A    1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER A   21  UNP  P68400    ARG    21 ENGINEERED MUTATION            
SEQADV 5CU2 GLY B  -22  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER B  -21  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 MET B  -20  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP B  -19  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ILE B  -18  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLU B  -17  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 PHE B  -16  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP B  -15  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP B  -14  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP B  -13  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ALA B  -12  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP B  -11  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP B  -10  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 ASP B   -9  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLY B   -8  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER B   -7  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLY B   -6  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER B   -5  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLY B   -4  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER B   -3  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLY B   -2  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER B   -1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 GLY B    0  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 SER B    1  UNP  P68400              EXPRESSION TAG                 
SEQADV 5CU2 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    551  A 401      26                                                       
HET    551  A 402      18                                                       
HET    551  A 403      15                                                       
HET    54G  A 404      11                                                       
HET    PO4  A 405       5                                                       
HET    ACT  A 406       7                                                       
HET    ACT  A 407       7                                                       
HET    551  B 401      26                                                       
HET    551  B 402      15                                                       
HET    54G  B 403      11                                                       
HET    PO4  B 404       5                                                       
HET    ACT  B 405       7                                                       
HETNAM     551 METHYL 3-[(3-{[(2-CHLOROBIPHENYL-4-YL)                           
HETNAM   2 551  METHYL]AMINO}PROPYL)AMINO]-3-OXOPROPANOATE                      
HETNAM     54G 2-HYDROXY-5-METHYLBENZOIC ACID                                   
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ACT ACETATE ION                                                      
FORMUL   3  551    5(C20 H23 CL N2 O3)                                          
FORMUL   6  54G    2(C8 H8 O3)                                                  
FORMUL   7  PO4    2(O4 P 3-)                                                   
FORMUL   8  ACT    3(C2 H3 O2 1-)                                               
FORMUL  15  HOH   *330(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 ASN A   35  ASP A   37  5                                   3    
HELIX    4 AA4 LYS A   74  ARG A   89  1                                  16    
HELIX    5 AA5 ASP A  120  LEU A  128  1                                   9    
HELIX    6 AA6 THR A  129  MET A  150  1                                  22    
HELIX    7 AA7 LYS A  158  HIS A  160  5                                   3    
HELIX    8 AA8 HIS A  166  ARG A  169  5                                   4    
HELIX    9 AA9 ASP A  175  ALA A  179  5                                   5    
HELIX   10 AB1 SER A  194  LYS A  198  5                                   5    
HELIX   11 AB2 GLY A  199  VAL A  204  1                                   6    
HELIX   12 AB3 TYR A  211  ARG A  228  1                                  18    
HELIX   13 AB4 ASP A  237  GLY A  250  1                                  14    
HELIX   14 AB5 GLY A  250  TYR A  261  1                                  12    
HELIX   15 AB6 ASP A  266  ASN A  270  5                                   5    
HELIX   16 AB7 ARG A  280  VAL A  285  5                                   6    
HELIX   17 AB8 ASN A  289  VAL A  293  5                                   5    
HELIX   18 AB9 SER A  294  LEU A  305  1                                  12    
HELIX   19 AC1 ASP A  308  ARG A  312  5                                   5    
HELIX   20 AC2 THR A  314  GLU A  320  1                                   7    
HELIX   21 AC3 HIS A  321  TYR A  325  5                                   5    
HELIX   22 AC4 PRO B   20  ASP B   25  1                                   6    
HELIX   23 AC5 TYR B   26  HIS B   29  5                                   4    
HELIX   24 AC6 ASN B   35  ASP B   37  5                                   3    
HELIX   25 AC7 LYS B   74  ARG B   89  1                                  16    
HELIX   26 AC8 ASP B  120  LEU B  128  1                                   9    
HELIX   27 AC9 THR B  129  MET B  150  1                                  22    
HELIX   28 AD1 LYS B  158  HIS B  160  5                                   3    
HELIX   29 AD2 HIS B  166  ARG B  169  5                                   4    
HELIX   30 AD3 ASP B  175  ALA B  179  5                                   5    
HELIX   31 AD4 SER B  194  LYS B  198  5                                   5    
HELIX   32 AD5 GLY B  199  VAL B  204  1                                   6    
HELIX   33 AD6 TYR B  211  ARG B  228  1                                  18    
HELIX   34 AD7 ASP B  237  GLY B  250  1                                  14    
HELIX   35 AD8 GLY B  250  TYR B  261  1                                  12    
HELIX   36 AD9 ASP B  266  ASN B  270  5                                   5    
HELIX   37 AE1 ARG B  280  VAL B  285  5                                   6    
HELIX   38 AE2 ASN B  289  VAL B  293  5                                   5    
HELIX   39 AE3 SER B  294  LEU B  305  1                                  12    
HELIX   40 AE4 ASP B  308  ARG B  312  5                                   5    
HELIX   41 AE5 THR B  314  GLU B  320  1                                   7    
HELIX   42 AE6 HIS B  321  TYR B  325  5                                   5    
SHEET    1 AA1 5 TYR A  39  ARG A  47  0                                        
SHEET    2 AA1 5 SER A  51  ASN A  58 -1  O  VAL A  53   N  LEU A  45           
SHEET    3 AA1 5 GLU A  63  LEU A  70 -1  O  GLU A  63   N  ASN A  58           
SHEET    4 AA1 5 THR A 108  GLU A 114 -1  O  PHE A 113   N  VAL A  66           
SHEET    5 AA1 5 LEU A  97  ASP A 103 -1  N  ALA A  98   O  VAL A 112           
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  LYS A 170   N  ASP A 165           
SHEET    1 AA4 5 TYR B  39  ARG B  47  0                                        
SHEET    2 AA4 5 SER B  51  ASN B  58 -1  O  GLU B  55   N  VAL B  42           
SHEET    3 AA4 5 GLU B  63  LEU B  70 -1  O  ILE B  69   N  GLU B  52           
SHEET    4 AA4 5 THR B 108  GLU B 114 -1  O  PHE B 113   N  VAL B  66           
SHEET    5 AA4 5 LEU B  97  ASP B 103 -1  N  ASP B  99   O  VAL B 112           
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        -5.95                     
CISPEP   2 GLU B  230    PRO B  231          0        -5.89                     
SITE     1 AC1 14 LEU A  45  GLY A  46  ASN A 118  ILE A 133                    
SITE     2 AC1 14 TYR A 136  PRO A 159  HIS A 160  VAL A 162                    
SITE     3 AC1 14 ILE A 164  ILE A 174  MET A 221  MET A 225                    
SITE     4 AC1 14 54G A 404  HOH A 563                                          
SITE     1 AC2  6 GLN A  36  ASP A  37  TYR A  39  ASP A 103                    
SITE     2 AC2  6 THR A 108  ALA A 110                                          
SITE     1 AC3  6 TRP A  24  GLN A  40  VAL A  42  HIS A 183                    
SITE     2 AC3  6 GLN A 186  HOH A 518                                          
SITE     1 AC4  9 VAL A  53  LYS A  68  ILE A  95  PHE A 113                    
SITE     2 AC4  9 ILE A 174  ASP A 175  551 A 401  HOH A 523                    
SITE     3 AC4  9 HOH A 567                                                     
SITE     1 AC5  5 ARG A 195  TYR A 196  HIS A 234  GLY A 235                    
SITE     2 AC5  5 HOH A 510                                                     
SITE     1 AC6  3 ARG A  80  ARG A 155  HOH A 648                               
SITE     1 AC7  3 HIS A 276  SER A 277  LYS A 279                               
SITE     1 AC8 10 ASN B 118  PHE B 121  TYR B 136  PRO B 159                    
SITE     2 AC8 10 HIS B 160  VAL B 162  ILE B 164  ILE B 174                    
SITE     3 AC8 10 MET B 225  HOH B 502                                          
SITE     1 AC9  6 TYR B  39  GLN B  40  LEU B  41  ASP B 103                    
SITE     2 AC9  6 THR B 108  ALA B 110                                          
SITE     1 AD1  7 LYS B  68  ILE B  95  PHE B 113  ILE B 174                    
SITE     2 AD1  7 ASP B 175  HOH B 529  HOH B 547                               
SITE     1 AD2  6 ARG B 195  TYR B 196  HIS B 234  GLY B 235                    
SITE     2 AD2  6 ARG B 244  LYS B 247                                          
SITE     1 AD3  3 ARG B  80  ARG B 155  HOH B 550                               
CRYST1   64.780   68.257  334.360  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      0.015437  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014651  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002991        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system