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Database: PDB
Entry: 4PJV
LinkDB: 4PJV
Original site: 4PJV 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       12-MAY-14   4PJV              
TITLE     STRUCTURE OF PARP2 CATALYTIC DOMAIN BOUND TO INHIBITOR BMN 673        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 2;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PARP2 HELICAL AND CATALYTIC DOMAINS (UNP RESIDUES 235-579);
COMPND   5 SYNONYM: HPARP-2,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 2,     
COMPND   6 ARTD2,NAD(+) ADP-RIBOSYLTRANSFERASE 2,ADPRT-2,POLY[ADP-RIBOSE]       
COMPND   7 SYNTHASE 2,PADPRT-2;                                                 
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: PARP2, ADPRT2, ADPRTL2;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: NEB T7 EXPRESS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    PARP2, INHIBITOR, COMPLEX                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.AOYAGI-SCHARBER,A.S.GARDBERG,T.L.EDWARDS                            
REVDAT   1   24-SEP-14 4PJV    0                                                
JRNL        AUTH   M.AOYAGI-SCHARBER,A.S.GARDBERG,B.K.YIP,B.WANG,Y.SHEN,        
JRNL        AUTH 2 P.A.FITZPATRICK                                              
JRNL        TITL   STRUCTURAL BASIS FOR THE INHIBITION OF POLY(ADP-RIBOSE)      
JRNL        TITL 2 POLYMERASES 1 AND 2 BY BMN 673, A POTENT INHIBITOR DERIVED   
JRNL        TITL 3 FROM DIHYDROPYRIDOPHTHALAZINONE.                             
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  70  1143 2014              
JRNL        REFN                   ESSN 2053-230X                               
JRNL        PMID   25195882                                                     
JRNL        DOI    10.1107/S2053230X14015088                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22773                          
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) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1150                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1614                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 70                           
REMARK   3   BIN FREE R VALUE                    : 0.4090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5114                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 143                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.67                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.70000                                              
REMARK   3    B22 (A**2) : 0.43000                                              
REMARK   3    B33 (A**2) : -0.76000                                             
REMARK   3    B12 (A**2) : -0.62000                                             
REMARK   3    B13 (A**2) : 0.07000                                              
REMARK   3    B23 (A**2) : 0.35000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 2.366         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.372         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.258         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.703        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.910                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.848                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5299 ; 0.011 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  3474 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7185 ; 1.462 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8503 ; 0.931 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   662 ; 6.619 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   219 ;38.753 ;24.338       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   864 ;17.391 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;16.222 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   807 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5887 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1039 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    234       A     579      4                      
REMARK   3           1     B    234       B     579      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   4213 ; 0.300 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   4213 ; 3.260 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   234        A   292                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4260   7.1030  -5.0530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1410 T22:   0.1668                                     
REMARK   3      T33:   0.0968 T12:  -0.0507                                     
REMARK   3      T13:  -0.0064 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6812 L22:   3.0606                                     
REMARK   3      L33:   1.6274 L12:  -1.3619                                     
REMARK   3      L13:  -0.0391 L23:  -0.3163                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0429 S12:  -0.0917 S13:  -0.1425                       
REMARK   3      S21:   0.2995 S22:   0.0991 S23:   0.2494                       
REMARK   3      S31:  -0.2330 S32:  -0.1533 S33:  -0.0562                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   296        A   369                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.4460  10.8060  -6.6200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1565 T22:   0.1813                                     
REMARK   3      T33:   0.0554 T12:  -0.0128                                     
REMARK   3      T13:  -0.0463 T23:   0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3321 L22:   4.1415                                     
REMARK   3      L33:   0.7934 L12:  -0.7469                                     
REMARK   3      L13:  -0.4365 L23:   0.8883                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1356 S12:  -0.0331 S13:  -0.0172                       
REMARK   3      S21:   0.0874 S22:  -0.1540 S23:  -0.1368                       
REMARK   3      S31:  -0.1215 S32:  -0.0141 S33:   0.0184                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   370        A   579                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6110  -2.8120  -5.0160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1127 T22:   0.0788                                     
REMARK   3      T33:   0.0107 T12:   0.0222                                     
REMARK   3      T13:   0.0132 T23:  -0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6306 L22:   1.3293                                     
REMARK   3      L33:   1.8185 L12:  -0.1729                                     
REMARK   3      L13:  -0.1300 L23:  -0.4609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0246 S12:  -0.0508 S13:   0.0046                       
REMARK   3      S21:  -0.0555 S22:   0.0029 S23:  -0.0686                       
REMARK   3      S31:   0.0949 S32:   0.0721 S33:   0.0217                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   234        B   289                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4390  33.7520 -41.1290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2990 T22:   0.2661                                     
REMARK   3      T33:   0.1229 T12:  -0.0465                                     
REMARK   3      T13:  -0.0436 T23:   0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4469 L22:   3.8176                                     
REMARK   3      L33:   1.4417 L12:  -3.0394                                     
REMARK   3      L13:   1.0488 L23:  -1.2791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0109 S12:   0.1008 S13:   0.3777                       
REMARK   3      S21:   0.0474 S22:  -0.0131 S23:  -0.4773                       
REMARK   3      S31:  -0.1563 S32:  -0.0643 S33:   0.0240                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   296        B   369                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2690  35.0600 -39.0890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3047 T22:   0.1918                                     
REMARK   3      T33:   0.0219 T12:  -0.0174                                     
REMARK   3      T13:  -0.0134 T23:   0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5469 L22:   2.9159                                     
REMARK   3      L33:   1.0122 L12:  -2.6140                                     
REMARK   3      L13:   1.0360 L23:  -1.1579                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0365 S12:  -0.0926 S13:  -0.1167                       
REMARK   3      S21:   0.1760 S22:   0.0510 S23:   0.0749                       
REMARK   3      S31:  -0.3250 S32:  -0.0282 S33:  -0.0875                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   370        B   579                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9630  12.4130 -40.3640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0925 T22:   0.0493                                     
REMARK   3      T33:   0.0021 T12:   0.0498                                     
REMARK   3      T13:   0.0027 T23:   0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1978 L22:   1.5090                                     
REMARK   3      L33:   3.0658 L12:  -0.1803                                     
REMARK   3      L13:  -0.0656 L23:  -0.2013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0404 S12:  -0.0117 S13:   0.0432                       
REMARK   3      S21:  -0.0737 S22:   0.0414 S23:   0.0114                       
REMARK   3      S31:   0.1713 S32:   0.0226 S33:  -0.0011                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED                 
REMARK   3   HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                  
REMARK   4                                                                      
REMARK   4 4PJV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201524.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.097                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22773                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.330                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.12300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0200                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
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: 3KCZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: (W/V) POLYETHYLENE GLYCOL 3350, 333 MM   
REMARK 280  SODIUM CHLORIDE.                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     HIS A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     SER A   220                                                      
REMARK 465     GLY A   221                                                      
REMARK 465     VAL A   222                                                      
REMARK 465     ASP A   223                                                      
REMARK 465     LEU A   224                                                      
REMARK 465     GLY A   225                                                      
REMARK 465     THR A   226                                                      
REMARK 465     GLU A   227                                                      
REMARK 465     ASN A   228                                                      
REMARK 465     LEU A   229                                                      
REMARK 465     TYR A   230                                                      
REMARK 465     PHE A   231                                                      
REMARK 465     GLN A   232                                                      
REMARK 465     SER A   233                                                      
REMARK 465     GLN A   293                                                      
REMARK 465     HIS A   294                                                      
REMARK 465     GLY A   295                                                      
REMARK 465     LEU A   351                                                      
REMARK 465     GLN A   352                                                      
REMARK 465     SER A   353                                                      
REMARK 465     PRO A   354                                                      
REMARK 465     MET B   212                                                      
REMARK 465     HIS B   213                                                      
REMARK 465     HIS B   214                                                      
REMARK 465     HIS B   215                                                      
REMARK 465     HIS B   216                                                      
REMARK 465     HIS B   217                                                      
REMARK 465     HIS B   218                                                      
REMARK 465     SER B   219                                                      
REMARK 465     SER B   220                                                      
REMARK 465     GLY B   221                                                      
REMARK 465     VAL B   222                                                      
REMARK 465     ASP B   223                                                      
REMARK 465     LEU B   224                                                      
REMARK 465     GLY B   225                                                      
REMARK 465     THR B   226                                                      
REMARK 465     GLU B   227                                                      
REMARK 465     ASN B   228                                                      
REMARK 465     LEU B   229                                                      
REMARK 465     TYR B   230                                                      
REMARK 465     PHE B   231                                                      
REMARK 465     GLN B   232                                                      
REMARK 465     SER B   233                                                      
REMARK 465     ARG B   290                                                      
REMARK 465     ALA B   291                                                      
REMARK 465     GLY B   292                                                      
REMARK 465     GLN B   293                                                      
REMARK 465     HIS B   294                                                      
REMARK 465     GLY B   295                                                      
REMARK 465     THR B   349                                                      
REMARK 465     GLU B   350                                                      
REMARK 465     LEU B   351                                                      
REMARK 465     GLN B   352                                                      
REMARK 465     SER B   353                                                      
REMARK 465     PRO B   354                                                      
REMARK 465     GLU B   355                                                      
REMARK 465     ASN B   548                                                      
REMARK 465     PRO B   549                                                      
REMARK 465     ASP B   550                                                      
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     LEU A 236    CG   CD1  CD2                                       
REMARK 470     GLN A 249    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 259    CG   CD   CE   NZ                                   
REMARK 470     LYS A 263    CG   CD   CE   NZ                                   
REMARK 470     LYS A 264    CG   CD   CE   NZ                                   
REMARK 470     LYS A 269    CG   CD   CE   NZ                                   
REMARK 470     LYS A 284    CG   CD   CE   NZ                                   
REMARK 470     ARG A 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 296    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 299    CG   SD   CE                                        
REMARK 470     GLU A 300    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 322    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 324    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 325    CG   CD   CE   NZ                                   
REMARK 470     SER A 328    OG                                                  
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 470     GLU A 350    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 355    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 363    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 410    CG   OD1  OD2                                       
REMARK 470     LEU A 479    CG   CD1  CD2                                       
REMARK 470     GLN A 494    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 543    CG   OD1  OD2                                       
REMARK 470     ASP A 550    CG   OD1  OD2                                       
REMARK 470     TYR A 552    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU B 236    CG   CD1  CD2                                       
REMARK 470     LYS B 259    CG   CD   CE   NZ                                   
REMARK 470     LYS B 263    CG   CD   CE   NZ                                   
REMARK 470     LYS B 264    CG   CD   CE   NZ                                   
REMARK 470     LYS B 269    CG   CD   CE   NZ                                   
REMARK 470     LEU B 270    CG   CD1  CD2                                       
REMARK 470     LYS B 276    CG   CD   CE   NZ                                   
REMARK 470     LYS B 284    CG   CD   CE   NZ                                   
REMARK 470     ASP B 287    CG   OD1  OD2                                       
REMARK 470     ARG B 296    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 299    CG   SD   CE                                        
REMARK 470     GLU B 300    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 304    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 320    CG   CD1  CD2                                       
REMARK 470     ARG B 322    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 324    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 325    CG   CD   CE   NZ                                   
REMARK 470     GLU B 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 345    CG   CD   CE   NZ                                   
REMARK 470     VAL B 347    CG1  CG2                                            
REMARK 470     LYS B 348    CG   CD   CE   NZ                                   
REMARK 470     GLN B 360    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 449    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 479    CG   CD1  CD2                                       
REMARK 470     SER B 525    OG                                                  
REMARK 470     ASP B 543    CG   OD1  OD2                                       
REMARK 470     LEU B 547    CG   CD1  CD2                                       
REMARK 470     TYR B 552    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR B 553    OG1  CG2                                            
REMARK 470     ARG B 570    CG   CD   NE   CZ   NH1  NH2                        
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   NZ   LYS A   283     OD2  ASP A   287              2.11            
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   O    LEU B   315     NZ   LYS B   380     1465     2.12            
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    HIS A 421   CG    HIS A 421   CD2     0.056                       
REMARK 500    HIS B 527   CG    HIS B 527   CD2     0.058                       
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    HIS A 394       54.76   -109.85                                   
REMARK 500    ARG A 570      -47.72   -139.94                                   
REMARK 500    ASN B 502      102.85   -165.23                                   
REMARK 500    ASN B 557      150.98    -42.55                                   
REMARK 500    ARG B 570      -33.64   -130.10                                   
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 2YQ A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2YQ B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4PJT   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 PRO TO HIS CONFLICT IN UNP ENTRY Q9UGN5                              
DBREF  4PJV A  235   579  UNP    Q9UGN5   PARP2_HUMAN    235    579             
DBREF  4PJV B  235   579  UNP    Q9UGN5   PARP2_HUMAN    235    579             
SEQADV 4PJV MET A  212  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS A  213  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS A  214  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS A  215  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS A  216  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS A  217  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS A  218  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV SER A  219  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV SER A  220  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV GLY A  221  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV VAL A  222  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV ASP A  223  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV LEU A  224  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV GLY A  225  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV THR A  226  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV GLU A  227  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV ASN A  228  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV LEU A  229  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV TYR A  230  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV PHE A  231  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV GLN A  232  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV SER A  233  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV MET A  234  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS A  447  UNP  Q9UGN5    PRO   447 SEE REMARK 999                 
SEQADV 4PJV MET B  212  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS B  213  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS B  214  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS B  215  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS B  216  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS B  217  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS B  218  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV SER B  219  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV SER B  220  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV GLY B  221  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV VAL B  222  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV ASP B  223  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV LEU B  224  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV GLY B  225  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV THR B  226  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV GLU B  227  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV ASN B  228  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV LEU B  229  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV TYR B  230  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV PHE B  231  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV GLN B  232  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV SER B  233  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV MET B  234  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4PJV HIS B  447  UNP  Q9UGN5    PRO   447 SEE REMARK 999                 
SEQRES   1 A  368  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  368  GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP LEU ARG          
SEQRES   3 A  368  VAL GLN GLU LEU ILE LYS LEU ILE CYS ASN VAL GLN ALA          
SEQRES   4 A  368  MET GLU GLU MET MET MET GLU MET LYS TYR ASN THR LYS          
SEQRES   5 A  368  LYS ALA PRO LEU GLY LYS LEU THR VAL ALA GLN ILE LYS          
SEQRES   6 A  368  ALA GLY TYR GLN SER LEU LYS LYS ILE GLU ASP CYS ILE          
SEQRES   7 A  368  ARG ALA GLY GLN HIS GLY ARG ALA LEU MET GLU ALA CYS          
SEQRES   8 A  368  ASN GLU PHE TYR THR ARG ILE PRO HIS ASP PHE GLY LEU          
SEQRES   9 A  368  ARG THR PRO PRO LEU ILE ARG THR GLN LYS GLU LEU SER          
SEQRES  10 A  368  GLU LYS ILE GLN LEU LEU GLU ALA LEU GLY ASP ILE GLU          
SEQRES  11 A  368  ILE ALA ILE LYS LEU VAL LYS THR GLU LEU GLN SER PRO          
SEQRES  12 A  368  GLU HIS PRO LEU ASP GLN HIS TYR ARG ASN LEU HIS CYS          
SEQRES  13 A  368  ALA LEU ARG PRO LEU ASP HIS GLU SER TYR GLU PHE LYS          
SEQRES  14 A  368  VAL ILE SER GLN TYR LEU GLN SER THR HIS ALA PRO THR          
SEQRES  15 A  368  HIS SER ASP TYR THR MET THR LEU LEU ASP LEU PHE GLU          
SEQRES  16 A  368  VAL GLU LYS ASP GLY GLU LYS GLU ALA PHE ARG GLU ASP          
SEQRES  17 A  368  LEU HIS ASN ARG MET LEU LEU TRP HIS GLY SER ARG MET          
SEQRES  18 A  368  SER ASN TRP VAL GLY ILE LEU SER HIS GLY LEU ARG ILE          
SEQRES  19 A  368  ALA HIS PRO GLU ALA PRO ILE THR GLY TYR MET PHE GLY          
SEQRES  20 A  368  LYS GLY ILE TYR PHE ALA ASP MET SER SER LYS SER ALA          
SEQRES  21 A  368  ASN TYR CYS PHE ALA SER ARG LEU LYS ASN THR GLY LEU          
SEQRES  22 A  368  LEU LEU LEU SER GLU VAL ALA LEU GLY GLN CYS ASN GLU          
SEQRES  23 A  368  LEU LEU GLU ALA ASN PRO LYS ALA GLU GLY LEU LEU GLN          
SEQRES  24 A  368  GLY LYS HIS SER THR LYS GLY LEU GLY LYS MET ALA PRO          
SEQRES  25 A  368  SER SER ALA HIS PHE VAL THR LEU ASN GLY SER THR VAL          
SEQRES  26 A  368  PRO LEU GLY PRO ALA SER ASP THR GLY ILE LEU ASN PRO          
SEQRES  27 A  368  ASP GLY TYR THR LEU ASN TYR ASN GLU TYR ILE VAL TYR          
SEQRES  28 A  368  ASN PRO ASN GLN VAL ARG MET ARG TYR LEU LEU LYS VAL          
SEQRES  29 A  368  GLN PHE ASN PHE                                              
SEQRES   1 B  368  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  368  GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP LEU ARG          
SEQRES   3 B  368  VAL GLN GLU LEU ILE LYS LEU ILE CYS ASN VAL GLN ALA          
SEQRES   4 B  368  MET GLU GLU MET MET MET GLU MET LYS TYR ASN THR LYS          
SEQRES   5 B  368  LYS ALA PRO LEU GLY LYS LEU THR VAL ALA GLN ILE LYS          
SEQRES   6 B  368  ALA GLY TYR GLN SER LEU LYS LYS ILE GLU ASP CYS ILE          
SEQRES   7 B  368  ARG ALA GLY GLN HIS GLY ARG ALA LEU MET GLU ALA CYS          
SEQRES   8 B  368  ASN GLU PHE TYR THR ARG ILE PRO HIS ASP PHE GLY LEU          
SEQRES   9 B  368  ARG THR PRO PRO LEU ILE ARG THR GLN LYS GLU LEU SER          
SEQRES  10 B  368  GLU LYS ILE GLN LEU LEU GLU ALA LEU GLY ASP ILE GLU          
SEQRES  11 B  368  ILE ALA ILE LYS LEU VAL LYS THR GLU LEU GLN SER PRO          
SEQRES  12 B  368  GLU HIS PRO LEU ASP GLN HIS TYR ARG ASN LEU HIS CYS          
SEQRES  13 B  368  ALA LEU ARG PRO LEU ASP HIS GLU SER TYR GLU PHE LYS          
SEQRES  14 B  368  VAL ILE SER GLN TYR LEU GLN SER THR HIS ALA PRO THR          
SEQRES  15 B  368  HIS SER ASP TYR THR MET THR LEU LEU ASP LEU PHE GLU          
SEQRES  16 B  368  VAL GLU LYS ASP GLY GLU LYS GLU ALA PHE ARG GLU ASP          
SEQRES  17 B  368  LEU HIS ASN ARG MET LEU LEU TRP HIS GLY SER ARG MET          
SEQRES  18 B  368  SER ASN TRP VAL GLY ILE LEU SER HIS GLY LEU ARG ILE          
SEQRES  19 B  368  ALA HIS PRO GLU ALA PRO ILE THR GLY TYR MET PHE GLY          
SEQRES  20 B  368  LYS GLY ILE TYR PHE ALA ASP MET SER SER LYS SER ALA          
SEQRES  21 B  368  ASN TYR CYS PHE ALA SER ARG LEU LYS ASN THR GLY LEU          
SEQRES  22 B  368  LEU LEU LEU SER GLU VAL ALA LEU GLY GLN CYS ASN GLU          
SEQRES  23 B  368  LEU LEU GLU ALA ASN PRO LYS ALA GLU GLY LEU LEU GLN          
SEQRES  24 B  368  GLY LYS HIS SER THR LYS GLY LEU GLY LYS MET ALA PRO          
SEQRES  25 B  368  SER SER ALA HIS PHE VAL THR LEU ASN GLY SER THR VAL          
SEQRES  26 B  368  PRO LEU GLY PRO ALA SER ASP THR GLY ILE LEU ASN PRO          
SEQRES  27 B  368  ASP GLY TYR THR LEU ASN TYR ASN GLU TYR ILE VAL TYR          
SEQRES  28 B  368  ASN PRO ASN GLN VAL ARG MET ARG TYR LEU LEU LYS VAL          
SEQRES  29 B  368  GLN PHE ASN PHE                                              
HET    2YQ  A 601      28                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603       6                                                       
HET    2YQ  B 601      28                                                       
HET    GOL  B 602       6                                                       
HETNAM     2YQ (8S,9R)-5-FLUORO-8-(4-FLUOROPHENYL)-9-(1-METHYL-1H-1,2,          
HETNAM   2 2YQ  4-TRIAZOL-5-YL)-2,7,8,9-TETRAHYDRO-3H-PYRIDO[4,3,2-             
HETNAM   3 2YQ  DE]PHTHALAZIN-3-ONE                                             
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  2YQ    2(C19 H14 F2 N6 O)                                           
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   8  HOH   *143(H2 O)                                                    
HELIX    1 AA1 ASP A  235  CYS A  246  1                                  12    
HELIX    2 AA2 ASN A  247  MET A  258  1                                  12    
HELIX    3 AA3 PRO A  266  LEU A  270  5                                   5    
HELIX    4 AA4 THR A  271  GLY A  292  1                                  22    
HELIX    5 AA5 ALA A  297  ILE A  309  1                                  13    
HELIX    6 AA6 THR A  323  VAL A  347  1                                  25    
HELIX    7 AA7 HIS A  356  HIS A  366  1                                  11    
HELIX    8 AA8 SER A  376  THR A  389  1                                  14    
HELIX    9 AA9 GLY A  411  PHE A  416  1                                   6    
HELIX   10 AB1 ARG A  431  SER A  433  5                                   3    
HELIX   11 AB2 ASN A  434  GLY A  442  1                                   9    
HELIX   12 AB3 MET A  466  TYR A  473  1                                   8    
HELIX   13 AB4 SER A  477  LYS A  480  5                                   4    
HELIX   14 AB5 SER A  525  PHE A  528  5                                   4    
HELIX   15 AB6 ASN A  563  ASN A  565  5                                   3    
HELIX   16 AB7 ASP B  235  CYS B  246  1                                  12    
HELIX   17 AB8 ASN B  247  MET B  258  1                                  12    
HELIX   18 AB9 PRO B  266  LEU B  270  5                                   5    
HELIX   19 AC1 THR B  271  ILE B  289  1                                  19    
HELIX   20 AC2 ALA B  297  ILE B  309  1                                  13    
HELIX   21 AC3 THR B  323  VAL B  347  1                                  25    
HELIX   22 AC4 PRO B  357  ASN B  364  1                                   8    
HELIX   23 AC5 SER B  376  THR B  389  1                                  14    
HELIX   24 AC6 GLY B  411  PHE B  416  1                                   6    
HELIX   25 AC7 ARG B  431  SER B  433  5                                   3    
HELIX   26 AC8 ASN B  434  GLY B  442  1                                   9    
HELIX   27 AC9 PRO B  451  TYR B  455  5                                   5    
HELIX   28 AD1 MET B  466  ASN B  472  1                                   7    
HELIX   29 AD2 SER B  525  PHE B  528  5                                   4    
HELIX   30 AD3 ASN B  563  ASN B  565  5                                   3    
SHEET    1 AA1 5 CYS A 367  PRO A 371  0                                        
SHEET    2 AA1 5 THR A 398  LYS A 409 -1  O  GLU A 406   N  ARG A 370           
SHEET    3 AA1 5 VAL A 567  ASN A 578 -1  O  ASN A 578   N  THR A 398           
SHEET    4 AA1 5 THR A 482  ALA A 491 -1  N  GLU A 489   O  ARG A 568           
SHEET    5 AA1 5 ARG A 423  GLY A 429 -1  N  MET A 424   O  VAL A 490           
SHEET    1 AA2 4 ILE A 461  PHE A 463  0                                        
SHEET    2 AA2 4 GLU A 558  VAL A 561 -1  O  VAL A 561   N  ILE A 461           
SHEET    3 AA2 4 SER A 514  GLY A 517 -1  N  THR A 515   O  ILE A 560           
SHEET    4 AA2 4 CYS A 495  LEU A 498  1  N  LEU A 498   O  LYS A 516           
SHEET    1 AA3 3 ALA A 541  ASP A 543  0                                        
SHEET    2 AA3 3 GLY A 519  PRO A 523 -1  N  ALA A 522   O  SER A 542           
SHEET    3 AA3 3 LEU A 554  TYR A 556  1  O  ASN A 555   N  MET A 521           
SHEET    1 AA4 2 VAL A 529  LEU A 531  0                                        
SHEET    2 AA4 2 SER A 534  VAL A 536 -1  O  VAL A 536   N  VAL A 529           
SHEET    1 AA5 5 CYS B 367  PRO B 371  0                                        
SHEET    2 AA5 5 THR B 398  LYS B 409 -1  O  GLU B 406   N  ARG B 370           
SHEET    3 AA5 5 VAL B 567  ASN B 578 -1  O  LEU B 572   N  PHE B 405           
SHEET    4 AA5 5 THR B 482  ALA B 491 -1  N  GLU B 489   O  ARG B 568           
SHEET    5 AA5 5 ARG B 423  GLY B 429 -1  N  HIS B 428   O  LEU B 486           
SHEET    1 AA6 4 ILE B 461  PHE B 463  0                                        
SHEET    2 AA6 4 GLU B 558  VAL B 561 -1  O  VAL B 561   N  ILE B 461           
SHEET    3 AA6 4 SER B 514  GLY B 517 -1  N  GLY B 517   O  GLU B 558           
SHEET    4 AA6 4 CYS B 495  LEU B 498  1  N  LEU B 498   O  LYS B 516           
SHEET    1 AA7 3 ALA B 541  ASP B 543  0                                        
SHEET    2 AA7 3 GLY B 519  PRO B 523 -1  N  ALA B 522   O  SER B 542           
SHEET    3 AA7 3 LEU B 554  TYR B 556  1  O  ASN B 555   N  MET B 521           
SHEET    1 AA8 2 VAL B 529  LEU B 531  0                                        
SHEET    2 AA8 2 SER B 534  VAL B 536 -1  O  VAL B 536   N  VAL B 529           
CISPEP   1 GLY A  539    PRO A  540          0        -3.12                     
CISPEP   2 GLY B  539    PRO B  540          0         2.44                     
SITE     1 AC1 17 SER A 328  GLN A 332  GLU A 335  HIS A 428                    
SITE     2 AC1 17 GLY A 429  GLY A 454  TYR A 455  TYR A 462                    
SITE     3 AC1 17 PHE A 463  LYS A 469  SER A 470  TYR A 473                    
SITE     4 AC1 17 GLU A 558  GOL A 602  HOH A 729  HOH A 756                    
SITE     5 AC1 17 HOH A 765                                                     
SITE     1 AC2  8 GLU A 335  ASP A 339  HIS A 428  SER A 430                    
SITE     2 AC2  8 LEU A 443  ARG A 444  2YQ A 601  HOH A 765                    
SITE     1 AC3  6 ASP A 396  TYR A 397  ALA A 471  ASN A 472                    
SITE     2 AC3  6 PHE A 475  ALA A 476                                          
SITE     1 AC4 16 SER B 328  GLN B 332  GLU B 335  HIS B 428                    
SITE     2 AC4 16 GLY B 429  GLY B 454  TYR B 462  PHE B 463                    
SITE     3 AC4 16 ALA B 464  LYS B 469  SER B 470  TYR B 473                    
SITE     4 AC4 16 GLU B 558  HOH B 723  HOH B 726  HOH B 741                    
SITE     1 AC5  5 ASP B 396  ALA B 471  ASN B 472  PHE B 475                    
SITE     2 AC5  5 ALA B 476                                                     
CRYST1   52.860   57.740   69.290  77.28  79.99  63.88 P 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      0.018918 -0.009274 -0.001857        0.00000                         
SCALE2      0.000000  0.019288 -0.003176        0.00000                         
SCALE3      0.000000  0.000000  0.014852        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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