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Database: PDB
Entry: 4MSG
LinkDB: 4MSG
Original site: 4MSG 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       18-SEP-13   4MSG              
TITLE     CRYSTAL STRUCTURE OF TANKYRASE 1 WITH COMPOUND 22                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TANKYRASE-1;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1104-1314;                                    
COMPND   5 SYNONYM: TANK1, ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 5,      
COMPND   6 ARTD5, POLY [ADP-RIBOSE] POLYMERASE 5A, TNKS-1, TRF1-INTERACTING     
COMPND   7 ANKYRIN-RELATED ADP-RIBOSE POLYMERASE, TANKYRASE I;                  
COMPND   8 EC: 2.4.2.30;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TNKS, PARP5A, PARPL, TIN1, TINF1, TNKS1;                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TANKYRASE, PARP, INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.HUANG                                                               
REVDAT   2   05-FEB-14 4MSG    1       JRNL                                     
REVDAT   1   25-DEC-13 4MSG    0                                                
JRNL        AUTH   Z.HUA,H.BREGMAN,J.L.BUCHANAN,N.CHAKKA,A.GUZMAN-PEREZ,        
JRNL        AUTH 2 H.GUNAYDIN,X.HUANG,Y.GU,V.BERRY,J.LIU,Y.TEFFERA,L.HUANG,     
JRNL        AUTH 3 B.EGGE,R.EMKEY,E.L.MULLADY,S.SCHNEIDER,P.S.ANDREWS,          
JRNL        AUTH 4 L.ACQUAVIVA,J.DOVEY,A.MISHRA,J.NEWCOMB,D.SAFFRAN,R.SERAFINO, 
JRNL        AUTH 5 C.A.STRATHDEE,S.M.TURCI,M.STANTON,C.WILSON,E.F.DIMAURO       
JRNL        TITL   DEVELOPMENT OF NOVEL DUAL BINDERS AS POTENT, SELECTIVE, AND  
JRNL        TITL 2 ORALLY BIOAVAILABLE TANKYRASE INHIBITORS.                    
JRNL        REF    J.MED.CHEM.                   V.  56 10003 2013              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   24294969                                                     
JRNL        DOI    10.1021/JM401317Z                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 45304                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2287                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 3307                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 465                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4MSG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB082309.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0-6.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46193                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2/0.4 M DI AMMONIUM TARTARTE, 12.5-    
REMARK 280  25% PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, PH    
REMARK 280  5.0                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       20.76450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.07600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.78400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.07600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.76450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.78400            
REMARK 290   SMTRY3   4  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 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     GLN A  1104                                                      
REMARK 465     HIS A  1316                                                      
REMARK 465     HIS A  1317                                                      
REMARK 465     HIS A  1318                                                      
REMARK 465     HIS A  1319                                                      
REMARK 465     HIS A  1320                                                      
REMARK 465     GLN B  1104                                                      
REMARK 465     ARG B  1281                                                      
REMARK 465     PRO B  1282                                                      
REMARK 465     SER B  1283                                                      
REMARK 465     VAL B  1284                                                      
REMARK 465     ASN B  1285                                                      
REMARK 465     GLY B  1286                                                      
REMARK 465     LEU B  1287                                                      
REMARK 465     ALA B  1288                                                      
REMARK 465     HIS B  1315                                                      
REMARK 465     HIS B  1316                                                      
REMARK 465     HIS B  1317                                                      
REMARK 465     HIS B  1318                                                      
REMARK 465     HIS B  1319                                                      
REMARK 465     HIS B  1320                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A1133    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A1285    CG   OD1  ND2                                       
REMARK 470     HIS A1315    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET B1207    CG   SD   CE                                        
REMARK 470     THR B1265    OG1  CG2                                            
REMARK 470     MET B1266    CG   SD   CE                                        
REMARK 470     TYR B1289    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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   O    HOH B  1550     O    HOH B  1671              1.88            
REMARK 500   O    HOH A  1656     O    HOH A  1705              1.89            
REMARK 500   O    ALA B  1290     O    HOH B  1621              1.91            
REMARK 500   O    HOH A  1624     O    HOH A  1759              1.91            
REMARK 500   O    HOH A  1622     O    HOH A  1768              1.93            
REMARK 500   O    HOH A  1633     O    HOH A  1759              1.94            
REMARK 500   OE2  GLU A  1291     O    HOH A  1588              2.00            
REMARK 500   O    HOH B  1615     O    HOH B  1628              2.00            
REMARK 500   O    HOH A  1675     O    HOH B  1653              2.01            
REMARK 500   O    HOH B  1606     O    HOH B  1624              2.03            
REMARK 500   OE2  GLU B  1114     O    HOH B  1526              2.05            
REMARK 500   O    HOH A  1560     O    HOH A  1578              2.06            
REMARK 500   N    TYR B  1289     O    HOH B  1665              2.08            
REMARK 500   O    HOH B  1533     O    HOH B  1548              2.08            
REMARK 500   O    HOH A  1618     O    HOH A  1687              2.09            
REMARK 500   O    HOH A  1565     O    HOH A  1638              2.10            
REMARK 500   O    HOH A  1636     O    HOH A  1652              2.11            
REMARK 500   O    HOH B  1673     O    HOH B  1674              2.14            
REMARK 500   O    HOH A  1621     O    HOH A  1706              2.15            
REMARK 500   OD1  ASN B  1175     O    HOH B  1602              2.15            
REMARK 500   O    HOH A  1737     O    HOH A  1756              2.15            
REMARK 500   O    HOH B  1686     O    HOH B  1690              2.17            
REMARK 500   O    HOH A  1656     O    HOH A  1737              2.17            
REMARK 500   O    HOH A  1725     O    HOH A  1759              2.18            
REMARK 500   O    HOH A  1685     O    HOH A  1700              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B1160   CG    GLU B1160   CD      0.096                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A1168   CB  -  CG  -  CD  ANGL. DEV. = -17.0 DEGREES          
REMARK 500    ARG A1180   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A1180   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A1253   CG  -  CD  -  NE  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ARG A1253   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    GLU A1314   CB  -  CG  -  CD  ANGL. DEV. =  21.5 DEGREES          
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    GLU A1298        0.59    -67.87                                   
REMARK 500    ASP B1134        9.15    -69.77                                   
REMARK 500    ARG B1149      134.83   -173.31                                   
REMARK 500    PHE B1263      -64.49    -99.21                                   
REMARK 500    THR B1265       56.66    -52.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR B1265        24.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A1237   ND1                                                    
REMARK 620 2 CYS A1234   SG  107.9                                              
REMARK 620 3 CYS A1242   SG  107.3 110.6                                        
REMARK 620 4 CYS A1245   SG  103.1 115.4 111.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B1237   ND1                                                    
REMARK 620 2 CYS B1242   SG  118.5                                              
REMARK 620 3 CYS B1245   SG   94.5 112.4                                        
REMARK 620 4 CYS B1234   SG  102.0 109.6 119.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2C6 A 1402                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2C6 B 1402                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4I9I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4MSK   RELATED DB: PDB                                   
DBREF  4MSG A 1104  1314  UNP    O95271   TNKS1_HUMAN   1104   1314             
DBREF  4MSG B 1104  1314  UNP    O95271   TNKS1_HUMAN   1104   1314             
SEQADV 4MSG HIS A 1315  UNP  O95271              EXPRESSION TAG                 
SEQADV 4MSG HIS A 1316  UNP  O95271              EXPRESSION TAG                 
SEQADV 4MSG HIS A 1317  UNP  O95271              EXPRESSION TAG                 
SEQADV 4MSG HIS A 1318  UNP  O95271              EXPRESSION TAG                 
SEQADV 4MSG HIS A 1319  UNP  O95271              EXPRESSION TAG                 
SEQADV 4MSG HIS A 1320  UNP  O95271              EXPRESSION TAG                 
SEQADV 4MSG HIS B 1315  UNP  O95271              EXPRESSION TAG                 
SEQADV 4MSG HIS B 1316  UNP  O95271              EXPRESSION TAG                 
SEQADV 4MSG HIS B 1317  UNP  O95271              EXPRESSION TAG                 
SEQADV 4MSG HIS B 1318  UNP  O95271              EXPRESSION TAG                 
SEQADV 4MSG HIS B 1319  UNP  O95271              EXPRESSION TAG                 
SEQADV 4MSG HIS B 1320  UNP  O95271              EXPRESSION TAG                 
SEQRES   1 A  217  GLN GLY THR ILE LEU LEU ASP LEU ALA PRO GLU ASP LYS          
SEQRES   2 A  217  GLU TYR GLN SER VAL GLU GLU GLU MET GLN SER THR ILE          
SEQRES   3 A  217  ARG GLU HIS ARG ASP GLY GLY ASN ALA GLY GLY ILE PHE          
SEQRES   4 A  217  ASN ARG TYR ASN VAL ILE ARG ILE GLN LYS VAL VAL ASN          
SEQRES   5 A  217  LYS LYS LEU ARG GLU ARG PHE CYS HIS ARG GLN LYS GLU          
SEQRES   6 A  217  VAL SER GLU GLU ASN HIS ASN HIS HIS ASN GLU ARG MET          
SEQRES   7 A  217  LEU PHE HIS GLY SER PRO PHE ILE ASN ALA ILE ILE HIS          
SEQRES   8 A  217  LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY GLY MET          
SEQRES   9 A  217  PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER SER LYS          
SEQRES  10 A  217  SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY THR GLY          
SEQRES  11 A  217  CYS PRO THR HIS LYS ASP ARG SER CYS TYR ILE CYS HIS          
SEQRES  12 A  217  ARG GLN MET LEU PHE CYS ARG VAL THR LEU GLY LYS SER          
SEQRES  13 A  217  PHE LEU GLN PHE SER THR MET LYS MET ALA HIS ALA PRO          
SEQRES  14 A  217  PRO GLY HIS HIS SER VAL ILE GLY ARG PRO SER VAL ASN          
SEQRES  15 A  217  GLY LEU ALA TYR ALA GLU TYR VAL ILE TYR ARG GLY GLU          
SEQRES  16 A  217  GLN ALA TYR PRO GLU TYR LEU ILE THR TYR GLN ILE MET          
SEQRES  17 A  217  LYS PRO GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  217  GLN GLY THR ILE LEU LEU ASP LEU ALA PRO GLU ASP LYS          
SEQRES   2 B  217  GLU TYR GLN SER VAL GLU GLU GLU MET GLN SER THR ILE          
SEQRES   3 B  217  ARG GLU HIS ARG ASP GLY GLY ASN ALA GLY GLY ILE PHE          
SEQRES   4 B  217  ASN ARG TYR ASN VAL ILE ARG ILE GLN LYS VAL VAL ASN          
SEQRES   5 B  217  LYS LYS LEU ARG GLU ARG PHE CYS HIS ARG GLN LYS GLU          
SEQRES   6 B  217  VAL SER GLU GLU ASN HIS ASN HIS HIS ASN GLU ARG MET          
SEQRES   7 B  217  LEU PHE HIS GLY SER PRO PHE ILE ASN ALA ILE ILE HIS          
SEQRES   8 B  217  LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY GLY MET          
SEQRES   9 B  217  PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER SER LYS          
SEQRES  10 B  217  SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY THR GLY          
SEQRES  11 B  217  CYS PRO THR HIS LYS ASP ARG SER CYS TYR ILE CYS HIS          
SEQRES  12 B  217  ARG GLN MET LEU PHE CYS ARG VAL THR LEU GLY LYS SER          
SEQRES  13 B  217  PHE LEU GLN PHE SER THR MET LYS MET ALA HIS ALA PRO          
SEQRES  14 B  217  PRO GLY HIS HIS SER VAL ILE GLY ARG PRO SER VAL ASN          
SEQRES  15 B  217  GLY LEU ALA TYR ALA GLU TYR VAL ILE TYR ARG GLY GLU          
SEQRES  16 B  217  GLN ALA TYR PRO GLU TYR LEU ILE THR TYR GLN ILE MET          
SEQRES  17 B  217  LYS PRO GLU HIS HIS HIS HIS HIS HIS                          
HET     ZN  A1401       1                                                       
HET    2C6  A1402      34                                                       
HET     ZN  B1401       1                                                       
HET    2C6  B1402      34                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     2C6 3-[(4-OXO-3,4-DIHYDROQUINAZOLIN-2-YL)SULFANYL]-N-                
HETNAM   2 2C6  [TRANS-4-(5-PHENYL-1,3,4-OXADIAZOL-2-YL)                        
HETNAM   3 2C6  CYCLOHEXYL]PROPANAMIDE                                          
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  2C6    2(C25 H25 N5 O3 S)                                           
FORMUL   7  HOH   *465(H2 O)                                                    
HELIX    1   1 ASP A 1115  SER A 1127  1                                  13    
HELIX    2   2 ASN A 1155  GLU A 1172  1                                  18    
HELIX    3   3 PHE A 1188  GLY A 1196  1                                   9    
HELIX    4   4 ASP A 1198  ALA A 1202  5                                   5    
HELIX    5   5 ASN A 1217  GLN A 1223  1                                   7    
HELIX    6   6 GLY A 1227  GLY A 1231  5                                   5    
HELIX    7   7 ARG A 1296  GLU A 1298  5                                   3    
HELIX    8   8 ASP B 1115  THR B 1128  1                                  14    
HELIX    9   9 ASN B 1155  ASN B 1173  1                                  19    
HELIX   10  10 PHE B 1188  GLY B 1196  1                                   9    
HELIX   11  11 ASP B 1198  ALA B 1202  5                                   5    
HELIX   12  12 ASN B 1217  GLN B 1223  1                                   7    
HELIX   13  13 GLY B 1227  GLY B 1231  5                                   5    
HELIX   14  14 ARG B 1296  GLU B 1298  5                                   3    
SHEET    1   A 5 ILE A1107  ASP A1110  0                                        
SHEET    2   A 5 ARG A1144  VAL A1154 -1  O  LYS A1152   N  LEU A1109           
SHEET    3   A 5 ALA A1300  MET A1311 -1  O  GLN A1309   N  ASN A1146           
SHEET    4   A 5 ARG A1247  THR A1255 -1  N  ARG A1247   O  TYR A1308           
SHEET    5   A 5 GLU A1179  HIS A1184 -1  N  ARG A1180   O  VAL A1254           
SHEET    1   B 4 ILE A1212  PHE A1214  0                                        
SHEET    2   B 4 GLU A1291  ILE A1294 -1  O  ILE A1294   N  ILE A1212           
SHEET    3   B 4 SER A1277  GLY A1280 -1  N  GLY A1280   O  GLU A1291           
SHEET    4   B 4 SER A1259  GLN A1262  1  N  PHE A1260   O  SER A1277           
SHEET    1   C 5 ILE B1107  ASP B1110  0                                        
SHEET    2   C 5 ARG B1144  VAL B1154 -1  O  LYS B1152   N  LEU B1109           
SHEET    3   C 5 ALA B1300  MET B1311 -1  O  THR B1307   N  ARG B1149           
SHEET    4   C 5 ARG B1247  THR B1255 -1  N  ARG B1247   O  TYR B1308           
SHEET    5   C 5 GLU B1179  HIS B1184 -1  N  LEU B1182   O  CYS B1252           
SHEET    1   D 4 ILE B1212  ALA B1215  0                                        
SHEET    2   D 4 GLU B1291  ILE B1294 -1  O  ILE B1294   N  ILE B1212           
SHEET    3   D 4 SER B1277  GLY B1280 -1  N  GLY B1280   O  GLU B1291           
SHEET    4   D 4 SER B1259  LEU B1261  1  N  PHE B1260   O  SER B1277           
LINK         ND1 HIS A1237                ZN    ZN A1401     1555   1555  2.22  
LINK         ND1 HIS B1237                ZN    ZN B1401     1555   1555  2.31  
LINK         SG  CYS B1242                ZN    ZN B1401     1555   1555  2.32  
LINK         SG  CYS A1234                ZN    ZN A1401     1555   1555  2.35  
LINK         SG  CYS A1242                ZN    ZN A1401     1555   1555  2.36  
LINK         SG  CYS B1245                ZN    ZN B1401     1555   1555  2.38  
LINK         SG  CYS B1234                ZN    ZN B1401     1555   1555  2.40  
LINK         SG  CYS A1245                ZN    ZN A1401     1555   1555  2.42  
SITE     1 AC1  4 CYS A1234  HIS A1237  CYS A1242  CYS A1245                    
SITE     1 AC2 18 HIS A1184  GLY A1185  SER A1186  PHE A1188                    
SITE     2 AC2 18 ALA A1191  ILE A1192  GLY A1196  PHE A1197                    
SITE     3 AC2 18 ASP A1198  HIS A1201  TYR A1213  PHE A1214                    
SITE     4 AC2 18 ALA A1215  LYS A1220  SER A1221  TYR A1224                    
SITE     5 AC2 18 GLU A1291  HOH A1553                                          
SITE     1 AC3  4 CYS B1234  HIS B1237  CYS B1242  CYS B1245                    
SITE     1 AC4 20 HIS B1184  GLY B1185  SER B1186  PHE B1188                    
SITE     2 AC4 20 ALA B1191  ILE B1192  LYS B1195  GLY B1196                    
SITE     3 AC4 20 PHE B1197  ASP B1198  HIS B1201  ILE B1212                    
SITE     4 AC4 20 TYR B1213  PHE B1214  ALA B1215  LYS B1220                    
SITE     5 AC4 20 SER B1221  TYR B1224  ILE B1228  GLU B1291                    
CRYST1   41.529   77.568  148.152  90.00  90.00  90.00 P 21 21 21    8          
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      0.024080  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012892  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006750        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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