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Database: PDB
Entry: 6EHK
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Original site: 6EHK 
HEADER    TRANSFERASE                             13-SEP-17   6EHK              
TITLE     THE CRYSTAL STRUCTURE OF CK2ALPHA IN COMPLEX WITH CAM4712 AND COMPOUND
TITLE    2 37                                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 2-329;                                            
COMPND   5 SYNONYM: CK II ALPHA;                                                
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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: PHAT2                                     
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,J.IEGRE,M.YOSHIDA,S.MITCHELL,M.ROSSMANN,L.CARRO,   
AUTHOR   2 H.SORE,M.HYVONEN,D.SPRING                                            
REVDAT   2   16-MAY-18 6EHK    1       JRNL                                     
REVDAT   1   28-FEB-18 6EHK    0                                                
JRNL        AUTH   J.IEGRE,P.BREAR,C.DE FUSCO,M.YOSHIDA,S.L.MITCHELL,           
JRNL        AUTH 2 M.ROSSMANN,L.CARRO,H.F.SORE,M.HYVONEN,D.R.SPRING             
JRNL        TITL   SECOND-GENERATION CK2 ALPHA INHIBITORS TARGETING THE ALPHA D 
JRNL        TITL 2 POCKET.                                                      
JRNL        REF    CHEM SCI                      V.   9  3041 2018              
JRNL        REFN                   ISSN 2041-6520                               
JRNL        PMID   29732088                                                     
JRNL        DOI    10.1039/C7SC05122K                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.1                                        
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) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 61080                          
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)  : 0.179                          
REMARK   3   R VALUE            (WORKING SET)  : 0.178                          
REMARK   3   FREE R VALUE                      : 0.194                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.030                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3074                           
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) : 1.40                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.44                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.21                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4487                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2211                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4272                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2202                   
REMARK   3   BIN FREE R VALUE                        : 0.2377                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.79                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 215                      
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            : 2748                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 206                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12530                                              
REMARK   3    B22 (A**2) : 2.04360                                              
REMARK   3    B33 (A**2) : -2.16890                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.56110                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.154               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.062               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.060               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.062               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.061               
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      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2928   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3975   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1026   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 73     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 465    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2928   ; 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   : 351    ; 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   : 3500   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.97                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.51                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.20                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6EHK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006628.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-17                          
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) : 0.97625                            
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 0.5.31, XDS                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61116                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.85100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5CVH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
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: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       23.14500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 440 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 15680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL                         
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 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     SER A     2                                                      
REMARK 465     ARG A   330                                                      
REMARK 465     GLU A   331                                                      
REMARK 465     ALA A   332                                                      
REMARK 465     MET A   333                                                      
REMARK 465     GLU A   334                                                      
REMARK 465     HIS A   335                                                      
REMARK 465     PRO A   336                                                      
REMARK 465     TYR A   337                                                      
REMARK 465     PHE A   338                                                      
REMARK 465     TYR A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     VAL A   341                                                      
REMARK 465     VAL A   342                                                      
REMARK 465     LYS A   343                                                      
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   NH2  ARG A   107     O    HOH A   501              0.57            
REMARK 500   CZ   ARG A   107     O    HOH A   501              0.75            
REMARK 500   NH1  ARG A   107     O    HOH A   501              1.81            
REMARK 500   NE   ARG A   107     O    HOH A   501              1.83            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD1  ASP A   259     NH2  ARG A   283    26415     1.86            
REMARK 500   OD2  ASP A   130     NH2  ARG A   316    26516     2.00            
REMARK 500   OE2  GLU A   264     NE   ARG A   280    26415     2.09            
REMARK 500   OH   TYR A    12     CG2  THR A   326    26416     2.10            
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    LYS A  77       37.95    -97.92                                   
REMARK 500    ASP A 156       44.89   -148.32                                   
REMARK 500    ASP A 175       78.33     49.41                                   
REMARK 500    ALA A 193      156.66     57.78                                   
REMARK 500    ALA A 193      158.32     57.78                                   
REMARK 500    HIS A 234       69.93   -100.22                                   
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 AUW 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                 
DBREF  6EHK A    2   329  UNP    P68400   CSK21_HUMAN      2    329             
SEQADV 6EHK SER A   21  UNP  P68400    ARG    21 ENGINEERED MUTATION            
SEQADV 6EHK ALA A   74  UNP  P68400    LYS    74 ENGINEERED MUTATION            
SEQADV 6EHK ALA A   75  UNP  P68400    LYS    75 ENGINEERED MUTATION            
SEQADV 6EHK ALA A   76  UNP  P68400    LYS    76 ENGINEERED MUTATION            
SEQADV 6EHK ARG A  330  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK GLU A  331  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK ALA A  332  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK MET A  333  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK GLU A  334  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK HIS A  335  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK PRO A  336  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK TYR A  337  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK PHE A  338  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK TYR A  339  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK THR A  340  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK VAL A  341  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK VAL A  342  UNP  P68400              EXPRESSION TAG                 
SEQADV 6EHK LYS A  343  UNP  P68400              EXPRESSION TAG                 
SEQRES   1 A  342  SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR ASP          
SEQRES   2 A  342  VAL ASN THR HIS ARG PRO SER GLU TYR TRP ASP TYR GLU          
SEQRES   3 A  342  SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR GLN          
SEQRES   4 A  342  LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU VAL          
SEQRES   5 A  342  PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL VAL          
SEQRES   6 A  342  VAL LYS ILE LEU LYS PRO VAL ALA ALA ALA LYS ILE LYS          
SEQRES   7 A  342  ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY PRO          
SEQRES   8 A  342  ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO VAL          
SEQRES   9 A  342  SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN ASN          
SEQRES  10 A  342  THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP TYR          
SEQRES  11 A  342  ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA LEU          
SEQRES  12 A  342  ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP VAL          
SEQRES  13 A  342  LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG LYS          
SEQRES  14 A  342  LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR HIS          
SEQRES  15 A  342  PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG TYR          
SEQRES  16 A  342  PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET TYR          
SEQRES  17 A  342  ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET LEU          
SEQRES  18 A  342  ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS GLY          
SEQRES  19 A  342  HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS VAL          
SEQRES  20 A  342  LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS TYR          
SEQRES  21 A  342  ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU GLY          
SEQRES  22 A  342  ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS SER          
SEQRES  23 A  342  GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP PHE          
SEQRES  24 A  342  LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG LEU          
SEQRES  25 A  342  THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR THR          
SEQRES  26 A  342  VAL VAL LYS ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  27 A  342  THR VAL VAL LYS                                              
HET    ACT  A 401       4                                                       
HET    ACT  A 402       4                                                       
HET    AUW  A 403      29                                                       
HET    54G  A 404      11                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM     AUW 2-(1~{H}-BENZIMIDAZOL-2-YL)-~{N}-[[3,5-BIS(CHLORANYL)-           
HETNAM   2 AUW  4-(2-ETHYLPHENYL)PHENYL]METHYL]ETHANAMINE                       
HETNAM     54G 2-HYDROXY-5-METHYLBENZOIC ACID                                   
FORMUL   2  ACT    2(C2 H3 O2 1-)                                               
FORMUL   4  AUW    C24 H23 CL2 N3                                               
FORMUL   5  54G    C8 H8 O3                                                     
FORMUL   6  HOH   *206(H2 O)                                                    
HELIX    1 AA1 ASP A   14  ARG A   19  1                                   6    
HELIX    2 AA2 PRO A   20  ASP A   25  1                                   6    
HELIX    3 AA3 TYR A   26  HIS A   29  5                                   4    
HELIX    4 AA4 ASN A   35  ASP A   37  5                                   3    
HELIX    5 AA5 ALA A   74  ALA A   76  5                                   3    
HELIX    6 AA6 LYS A   77  ARG A   89  1                                  13    
HELIX    7 AA7 ASP A  120  LEU A  128  1                                   9    
HELIX    8 AA8 THR A  129  MET A  150  1                                  22    
HELIX    9 AA9 LYS A  158  HIS A  160  5                                   3    
HELIX   10 AB1 HIS A  166  ARG A  169  5                                   4    
HELIX   11 AB2 ASP A  175  ALA A  179  5                                   5    
HELIX   12 AB3 SER A  194  LYS A  198  5                                   5    
HELIX   13 AB4 GLY A  199  VAL A  204  1                                   6    
HELIX   14 AB5 TYR A  211  ARG A  228  1                                  18    
HELIX   15 AB6 ASP A  237  GLY A  250  1                                  14    
HELIX   16 AB7 GLY A  250  TYR A  261  1                                  12    
HELIX   17 AB8 ASP A  266  ILE A  272  5                                   7    
HELIX   18 AB9 ARG A  280  VAL A  285  5                                   6    
HELIX   19 AC1 ASN A  289  VAL A  293  5                                   5    
HELIX   20 AC2 SER A  294  LEU A  305  1                                  12    
HELIX   21 AC3 ASP A  308  ARG A  312  5                                   5    
HELIX   22 AC4 THR A  314  GLU A  320  1                                   7    
HELIX   23 AC5 HIS A  321  TYR A  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  GLY A  46           
SHEET    3 AA1 5 LYS A  64  LEU A  70 -1  O  ILE A  69   N  GLU A  52           
SHEET    4 AA1 5 PRO A 109  GLU A 114 -1  O  PHE A 113   N  VAL A  66           
SHEET    5 AA1 5 LEU A  97  LYS A 102 -1  N  ASP A  99   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  ARG A 172   N  MET A 163           
CISPEP   1 GLU A  230    PRO A  231          0        -5.79                     
SITE     1 AC1  3 ASP A 103  ARG A 280  HOH A 537                               
SITE     1 AC2  3 ARG A  80  ARG A 155  HOH A 642                               
SITE     1 AC3 10 TYR A 125  MET A 137  PRO A 159  HIS A 160                    
SITE     2 AC3 10 VAL A 162  MET A 163  MET A 221  MET A 225                    
SITE     3 AC3 10 HOH A 571  HOH A 673                                          
SITE     1 AC4  9 VAL A  53  VAL A  66  LYS A  68  PHE A 113                    
SITE     2 AC4  9 MET A 163  ILE A 174  ASP A 175  HOH A 547                    
SITE     3 AC4  9 HOH A 565                                                     
CRYST1   58.290   46.290   63.050  90.00 111.93  90.00 P 1 21 1      2          
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      0.017156  0.000000  0.006907        0.00000                         
SCALE2      0.000000  0.021603  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017098        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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