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Database: PDB
Entry: 5D5K
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Original site: 5D5K 
HEADER    PROTON TRANSPORT                        10-AUG-15   5D5K              
TITLE     CRYSTAL STRUCTURE NLS FROM HUMAN PARP-2 COMPLEXED WITH IMPORTIN ALPHA 
TITLE    2 DELTA IBB                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IMPORTIN SUBUNIT ALPHA-1;                                  
COMPND   3 CHAIN: C;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 70-529;                                       
COMPND   5 SYNONYM: IMPORTIN ALPHA P1,KARYOPHERIN SUBUNIT ALPHA-2,PENDULIN,PORE 
COMPND   6 TARGETING COMPLEX 58 KDA SUBUNIT,PTAC58,RAG COHORT PROTEIN 1,SRP1-   
COMPND   7 ALPHA;                                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 2;                            
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 1-78;                                         
COMPND  13 SYNONYM: HPARP-2,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 2,     
COMPND  14 ARTD2,NAD(+) ADP-RIBOSYLTRANSFERASE 2,ADPRT-2,POLY[ADP-RIBOSE]       
COMPND  15 SYNTHASE 2,PADPRT-2;                                                 
COMPND  16 EC: 2.4.2.30;                                                        
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: KPNA2, RCH1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PARP2, ADPRT2, ADPRTL2;                                        
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PARP-2 NLS, PARP-2, POLY(ADP-RIBOSE)POLYMERASE-2, IMPORTIN ALPHA,     
KEYWDS   2 PROTON TRANSPORT                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.RICCIO,G.CINGOLANI,J.M.PASCAL                                     
REVDAT   2   04-OCT-17 5D5K    1       JRNL   REMARK                            
REVDAT   1   22-JUN-16 5D5K    0                                                
JRNL        AUTH   A.A.RICCIO,G.CINGOLANI,J.M.PASCAL                            
JRNL        TITL   PARP-2 DOMAIN REQUIREMENTS FOR DNA DAMAGE-DEPENDENT          
JRNL        TITL 2 ACTIVATION AND LOCALIZATION TO SITES OF DNA DAMAGE.          
JRNL        REF    NUCLEIC ACIDS RES.            V.  44  1691 2016              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   26704974                                                     
JRNL        DOI    10.1093/NAR/GKV1376                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.34                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 56607                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.151                           
REMARK   3   R VALUE            (WORKING SET) : 0.150                           
REMARK   3   FREE R VALUE                     : 0.171                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2873                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.3541 -  5.2390    0.95     2610   156  0.1861 0.2140        
REMARK   3     2  5.2390 -  4.1595    1.00     2665   119  0.1370 0.1569        
REMARK   3     3  4.1595 -  3.6340    1.00     2596   136  0.1332 0.1429        
REMARK   3     4  3.6340 -  3.3019    1.00     2601   142  0.1486 0.1524        
REMARK   3     5  3.3019 -  3.0653    1.00     2559   135  0.1491 0.1665        
REMARK   3     6  3.0653 -  2.8846    1.00     2577   148  0.1434 0.1686        
REMARK   3     7  2.8846 -  2.7402    1.00     2572   132  0.1412 0.1496        
REMARK   3     8  2.7402 -  2.6209    1.00     2569   131  0.1381 0.1439        
REMARK   3     9  2.6209 -  2.5201    1.00     2559   131  0.1343 0.1556        
REMARK   3    10  2.5201 -  2.4331    1.00     2564   138  0.1306 0.1642        
REMARK   3    11  2.4331 -  2.3570    1.00     2548   136  0.1371 0.1679        
REMARK   3    12  2.3570 -  2.2897    1.00     2524   156  0.1296 0.1514        
REMARK   3    13  2.2897 -  2.2294    1.00     2564   109  0.1297 0.1752        
REMARK   3    14  2.2294 -  2.1750    1.00     2560   137  0.1439 0.1690        
REMARK   3    15  2.1750 -  2.1256    1.00     2510   144  0.1498 0.1531        
REMARK   3    16  2.1256 -  2.0803    1.00     2547   136  0.1589 0.1842        
REMARK   3    17  2.0803 -  2.0387    1.00     2573   117  0.1704 0.2008        
REMARK   3    18  2.0387 -  2.0002    1.00     2512   136  0.1851 0.2054        
REMARK   3    19  2.0002 -  1.9645    1.00     2531   122  0.2101 0.2327        
REMARK   3    20  1.9645 -  1.9312    1.00     2522   157  0.2270 0.2691        
REMARK   3    21  1.9312 -  1.9001    0.99     2471   155  0.2662 0.2858        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.380           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           3433                                  
REMARK   3   ANGLE     :  1.269           4674                                  
REMARK   3   CHIRALITY :  0.074            564                                  
REMARK   3   PLANARITY :  0.007            597                                  
REMARK   3   DIHEDRAL  : 13.849           1270                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 73 THROUGH 202 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.8284  -2.6133 116.3494              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3122 T22:   0.2799                                     
REMARK   3      T33:   0.2307 T12:   0.0085                                     
REMARK   3      T13:  -0.0454 T23:   0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4161 L22:   3.6533                                     
REMARK   3      L33:   1.5019 L12:  -0.2031                                     
REMARK   3      L13:   0.4049 L23:  -1.4914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1043 S12:   0.0183 S13:  -0.1635                       
REMARK   3      S21:  -0.1141 S22:  -0.0298 S23:  -0.0547                       
REMARK   3      S31:   0.2370 S32:   0.1232 S33:  -0.0686                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 203 THROUGH 322 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5967  23.5805 112.2733              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2077 T22:   0.1978                                     
REMARK   3      T33:   0.2520 T12:   0.0166                                     
REMARK   3      T13:  -0.0024 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6471 L22:   2.2814                                     
REMARK   3      L33:   2.0711 L12:   1.0551                                     
REMARK   3      L13:  -0.7043 L23:  -0.5627                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1115 S12:   0.1009 S13:   0.2349                       
REMARK   3      S21:   0.0805 S22:  -0.0201 S23:  -0.0377                       
REMARK   3      S31:  -0.0591 S32:   0.0351 S33:  -0.0777                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 323 THROUGH 496 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8345  37.4475  82.0369              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3129 T22:   0.5364                                     
REMARK   3      T33:   0.3526 T12:   0.0070                                     
REMARK   3      T13:  -0.0550 T23:   0.1686                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3178 L22:   2.8173                                     
REMARK   3      L33:   1.7393 L12:   0.2777                                     
REMARK   3      L13:  -0.9064 L23:  -0.5474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0338 S12:   0.8447 S13:   0.3217                       
REMARK   3      S21:  -0.5272 S22:   0.1796 S23:   0.4282                       
REMARK   3      S31:  -0.0051 S32:  -0.5050 S33:   0.3851                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 23 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0641  32.5854  91.4959              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5608 T22:   0.6955                                     
REMARK   3      T33:   0.7274 T12:  -0.1070                                     
REMARK   3      T13:  -0.0252 T23:   0.2475                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6212 L22:   2.7240                                     
REMARK   3      L33:   5.8827 L12:   2.1929                                     
REMARK   3      L13:  -0.8067 L23:   1.6745                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0582 S12:   0.3354 S13:   0.2267                       
REMARK   3      S21:  -0.2088 S22:   0.0921 S23:   0.3340                       
REMARK   3      S31:   1.0186 S32:  -1.0437 S33:  -0.2437                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 34 THROUGH 40 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7610   4.6665 109.5644              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2191 T22:   0.3339                                     
REMARK   3      T33:   0.2573 T12:   0.0162                                     
REMARK   3      T13:   0.0540 T23:   0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4398 L22:   8.4242                                     
REMARK   3      L33:   6.6398 L12:  -1.9475                                     
REMARK   3      L13:   2.9738 L23:  -3.1459                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0486 S12:   0.0688 S13:   0.2051                       
REMARK   3      S21:  -0.6303 S22:  -0.0465 S23:  -0.8498                       
REMARK   3      S31:  -0.2214 S32:   0.1129 S33:   0.0048                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5D5K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210827.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56607                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: 1Y2A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6-0.7M SODIUM CITRATE, 0.1M SODIUM     
REMARK 280  CITRATE BUFFER PH 5.6, AND 7-10MM DTT, VAPOR DIFFUSION, SITTING     
REMARK 280  DROP, TEMPERATURE 295K                                              
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       39.32000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.99000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.32000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.99000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 C    64                                                      
REMARK 465     ALA C    65                                                      
REMARK 465     ASP C    66                                                      
REMARK 465     ILE C    67                                                      
REMARK 465     GLY C    68                                                      
REMARK 465     SER C    69                                                      
REMARK 465     ASN C    70                                                      
REMARK 465     GLN C    71                                                      
REMARK 465     GLY C    72                                                      
REMARK 465     SER C   497                                                      
REMARK 465     VAL C   498                                                      
REMARK 465     GLU C   499                                                      
REMARK 465     GLU C   500                                                      
REMARK 465     GLU C   501                                                      
REMARK 465     GLU C   502                                                      
REMARK 465     ASP C   503                                                      
REMARK 465     GLN C   504                                                      
REMARK 465     ASN C   505                                                      
REMARK 465     VAL C   506                                                      
REMARK 465     VAL C   507                                                      
REMARK 465     PRO C   508                                                      
REMARK 465     GLU C   509                                                      
REMARK 465     THR C   510                                                      
REMARK 465     THR C   511                                                      
REMARK 465     SER C   512                                                      
REMARK 465     GLU C   513                                                      
REMARK 465     GLY C   514                                                      
REMARK 465     PHE C   515                                                      
REMARK 465     ALA C   516                                                      
REMARK 465     PHE C   517                                                      
REMARK 465     GLN C   518                                                      
REMARK 465     VAL C   519                                                      
REMARK 465     GLN C   520                                                      
REMARK 465     ASP C   521                                                      
REMARK 465     GLY C   522                                                      
REMARK 465     ALA C   523                                                      
REMARK 465     PRO C   524                                                      
REMARK 465     GLY C   525                                                      
REMARK 465     THR C   526                                                      
REMARK 465     PHE C   527                                                      
REMARK 465     ASN C   528                                                      
REMARK 465     PHE C   529                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     GLY B   -19                                                      
REMARK 465     SER B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     VAL B    -6                                                      
REMARK 465     PRO B    -5                                                      
REMARK 465     ARG B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     ARG B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     ARG B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     ASN B    17                                                      
REMARK 465     ASN B    24                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     ASN B    26                                                      
REMARK 465     THR B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     CYS B    41                                                      
REMARK 465     GLN B    42                                                      
REMARK 465     ARG B    43                                                      
REMARK 465     GLN B    44                                                      
REMARK 465     GLU B    45                                                      
REMARK 465     SER B    46                                                      
REMARK 465     LYS B    47                                                      
REMARK 465     LYS B    48                                                      
REMARK 465     MET B    49                                                      
REMARK 465     PRO B    50                                                      
REMARK 465     VAL B    51                                                      
REMARK 465     ALA B    52                                                      
REMARK 465     GLY B    53                                                      
REMARK 465     GLY B    54                                                      
REMARK 465     LYS B    55                                                      
REMARK 465     ALA B    56                                                      
REMARK 465     ASN B    57                                                      
REMARK 465     LYS B    58                                                      
REMARK 465     ASP B    59                                                      
REMARK 465     ARG B    60                                                      
REMARK 465     THR B    61                                                      
REMARK 465     GLU B    62                                                      
REMARK 465     ASP B    63                                                      
REMARK 465     LYS B    64                                                      
REMARK 465     GLN B    65                                                      
REMARK 465     ASP B    66                                                      
REMARK 465     GLU B    67                                                      
REMARK 465     SER B    68                                                      
REMARK 465     VAL B    69                                                      
REMARK 465     LYS B    70                                                      
REMARK 465     ALA B    71                                                      
REMARK 465     LEU B    72                                                      
REMARK 465     LEU B    73                                                      
REMARK 465     LEU B    74                                                      
REMARK 465     LYS B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 465     LYS B    77                                                      
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     GLU B  18    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  31    CG   OD1  OD2                                       
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   HZ1  LYS B    37     O    HOH B   101              1.37            
REMARK 500   HZ2  LYS C   292     O    HOH C   605              1.47            
REMARK 500  HH12  ARG C   315     O    HOH C   601              1.49            
REMARK 500   O    HOH C   846     O    HOH C   871              1.94            
REMARK 500   O    HOH C   805     O    HOH C   834              1.95            
REMARK 500   O    HOH C   835     O    HOH C   867              1.98            
REMARK 500   O    HOH C   815     O    HOH C   819              2.01            
REMARK 500   O    HOH C   629     O    HOH C   835              2.02            
REMARK 500   O    HOH C   699     O    HOH C   826              2.02            
REMARK 500   O    HOH C   601     O    HOH B   109              2.03            
REMARK 500   O    HOH C   848     O    HOH C   855              2.08            
REMARK 500   O    HOH C   774     O    HOH C   871              2.11            
REMARK 500   O    HOH C   715     O    HOH B   101              2.14            
REMARK 500   O    HOH C   723     O    HOH B   107              2.16            
REMARK 500   NH1  ARG C   315     O    HOH C   601              2.17            
REMARK 500   OD1  ASN C   114     O    HOH C   602              2.19            
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    HOH C   823     O    HOH C   839     3557     1.91            
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    ASN C  88       41.52    -93.32                                   
REMARK 500    ASN C 239      158.44     82.66                                   
REMARK 500    LYS C 432       49.17    -88.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5D5K C   70   529  UNP    P52293   IMA1_MOUSE      70    529             
DBREF  5D5K B    0    77  UNP    Q9UGN5   PARP2_HUMAN      1     78             
SEQADV 5D5K MET C   64  UNP  P52293              INITIATING METHIONINE          
SEQADV 5D5K ALA C   65  UNP  P52293              EXPRESSION TAG                 
SEQADV 5D5K ASP C   66  UNP  P52293              EXPRESSION TAG                 
SEQADV 5D5K ILE C   67  UNP  P52293              EXPRESSION TAG                 
SEQADV 5D5K GLY C   68  UNP  P52293              EXPRESSION TAG                 
SEQADV 5D5K SER C   69  UNP  P52293              EXPRESSION TAG                 
SEQADV 5D5K MET B  -20  UNP  Q9UGN5              INITIATING METHIONINE          
SEQADV 5D5K GLY B  -19  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K SER B  -18  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K SER B  -17  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K HIS B  -16  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K HIS B  -15  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K HIS B  -14  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K HIS B  -13  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K HIS B  -12  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K HIS B  -11  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K SER B  -10  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K SER B   -9  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K GLY B   -8  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K LEU B   -7  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K VAL B   -6  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K PRO B   -5  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K ARG B   -4  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K GLY B   -3  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K SER B   -2  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 5D5K HIS B   -1  UNP  Q9UGN5              EXPRESSION TAG                 
SEQRES   1 C  466  MET ALA ASP ILE GLY SER ASN GLN GLY THR VAL ASN TRP          
SEQRES   2 C  466  SER VAL GLU ASP ILE VAL LYS GLY ILE ASN SER ASN ASN          
SEQRES   3 C  466  LEU GLU SER GLN LEU GLN ALA THR GLN ALA ALA ARG LYS          
SEQRES   4 C  466  LEU LEU SER ARG GLU LYS GLN PRO PRO ILE ASP ASN ILE          
SEQRES   5 C  466  ILE ARG ALA GLY LEU ILE PRO LYS PHE VAL SER PHE LEU          
SEQRES   6 C  466  GLY LYS THR ASP CYS SER PRO ILE GLN PHE GLU SER ALA          
SEQRES   7 C  466  TRP ALA LEU THR ASN ILE ALA SER GLY THR SER GLU GLN          
SEQRES   8 C  466  THR LYS ALA VAL VAL ASP GLY GLY ALA ILE PRO ALA PHE          
SEQRES   9 C  466  ILE SER LEU LEU ALA SER PRO HIS ALA HIS ILE SER GLU          
SEQRES  10 C  466  GLN ALA VAL TRP ALA LEU GLY ASN ILE ALA GLY ASP GLY          
SEQRES  11 C  466  SER ALA PHE ARG ASP LEU VAL ILE LYS HIS GLY ALA ILE          
SEQRES  12 C  466  ASP PRO LEU LEU ALA LEU LEU ALA VAL PRO ASP LEU SER          
SEQRES  13 C  466  THR LEU ALA CYS GLY TYR LEU ARG ASN LEU THR TRP THR          
SEQRES  14 C  466  LEU SER ASN LEU CYS ARG ASN LYS ASN PRO ALA PRO PRO          
SEQRES  15 C  466  LEU ASP ALA VAL GLU GLN ILE LEU PRO THR LEU VAL ARG          
SEQRES  16 C  466  LEU LEU HIS HIS ASN ASP PRO GLU VAL LEU ALA ASP SER          
SEQRES  17 C  466  CYS TRP ALA ILE SER TYR LEU THR ASP GLY PRO ASN GLU          
SEQRES  18 C  466  ARG ILE GLU MET VAL VAL LYS LYS GLY VAL VAL PRO GLN          
SEQRES  19 C  466  LEU VAL LYS LEU LEU GLY ALA THR GLU LEU PRO ILE VAL          
SEQRES  20 C  466  THR PRO ALA LEU ARG ALA ILE GLY ASN ILE VAL THR GLY          
SEQRES  21 C  466  THR ASP GLU GLN THR GLN LYS VAL ILE ASP ALA GLY ALA          
SEQRES  22 C  466  LEU ALA VAL PHE PRO SER LEU LEU THR ASN PRO LYS THR          
SEQRES  23 C  466  ASN ILE GLN LYS GLU ALA THR TRP THR MET SER ASN ILE          
SEQRES  24 C  466  THR ALA GLY ARG GLN ASP GLN ILE GLN GLN VAL VAL ASN          
SEQRES  25 C  466  HIS GLY LEU VAL PRO PHE LEU VAL GLY VAL LEU SER LYS          
SEQRES  26 C  466  ALA ASP PHE LYS THR GLN LYS GLU ALA ALA TRP ALA ILE          
SEQRES  27 C  466  THR ASN TYR THR SER GLY GLY THR VAL GLU GLN ILE VAL          
SEQRES  28 C  466  TYR LEU VAL HIS CYS GLY ILE ILE GLU PRO LEU MET ASN          
SEQRES  29 C  466  LEU LEU SER ALA LYS ASP THR LYS ILE ILE GLN VAL ILE          
SEQRES  30 C  466  LEU ASP ALA ILE SER ASN ILE PHE GLN ALA ALA GLU LYS          
SEQRES  31 C  466  LEU GLY GLU THR GLU LYS LEU SER ILE MET ILE GLU GLU          
SEQRES  32 C  466  CYS GLY GLY LEU ASP LYS ILE GLU ALA LEU GLN ARG HIS          
SEQRES  33 C  466  GLU ASN GLU SER VAL TYR LYS ALA SER LEU ASN LEU ILE          
SEQRES  34 C  466  GLU LYS TYR PHE SER VAL GLU GLU GLU GLU ASP GLN ASN          
SEQRES  35 C  466  VAL VAL PRO GLU THR THR SER GLU GLY PHE ALA PHE GLN          
SEQRES  36 C  466  VAL GLN ASP GLY ALA PRO GLY THR PHE ASN PHE                  
SEQRES   1 B   98  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B   98  LEU VAL PRO ARG GLY SER HIS MET ALA ALA ARG ARG ARG          
SEQRES   3 B   98  ARG SER THR GLY GLY GLY ARG ALA ARG ALA LEU ASN GLU          
SEQRES   4 B   98  SER LYS ARG VAL ASN ASN GLY ASN THR ALA PRO GLU ASP          
SEQRES   5 B   98  SER SER PRO ALA LYS LYS THR ARG ARG CYS GLN ARG GLN          
SEQRES   6 B   98  GLU SER LYS LYS MET PRO VAL ALA GLY GLY LYS ALA ASN          
SEQRES   7 B   98  LYS ASP ARG THR GLU ASP LYS GLN ASP GLU SER VAL LYS          
SEQRES   8 B   98  ALA LEU LEU LEU LYS GLY LYS                                  
FORMUL   3  HOH   *324(H2 O)                                                    
HELIX    1 AA1 SER C   77  ASN C   86  1                                  10    
HELIX    2 AA2 ASN C   89  SER C  105  1                                  17    
HELIX    3 AA3 PRO C  111  ALA C  118  1                                   8    
HELIX    4 AA4 GLY C  119  GLY C  129  1                                  11    
HELIX    5 AA5 CYS C  133  SER C  149  1                                  17    
HELIX    6 AA6 THR C  151  GLY C  161  1                                  11    
HELIX    7 AA7 GLY C  162  LEU C  171  1                                  10    
HELIX    8 AA8 HIS C  175  GLY C  191  1                                  17    
HELIX    9 AA9 GLY C  193  HIS C  203  1                                  11    
HELIX   10 AB1 ALA C  205  LEU C  212  1                                   8    
HELIX   11 AB2 ASP C  217  LEU C  221  5                                   5    
HELIX   12 AB3 ALA C  222  CYS C  237  1                                  16    
HELIX   13 AB4 PRO C  245  LEU C  260  1                                  16    
HELIX   14 AB5 ASP C  264  THR C  279  1                                  16    
HELIX   15 AB6 PRO C  282  LYS C  291  1                                  10    
HELIX   16 AB7 VAL C  294  GLY C  303  1                                  10    
HELIX   17 AB8 GLU C  306  VAL C  321  1                                  16    
HELIX   18 AB9 THR C  324  ALA C  334  1                                  11    
HELIX   19 AC1 GLY C  335  ALA C  338  5                                   4    
HELIX   20 AC2 VAL C  339  LEU C  344  1                                   6    
HELIX   21 AC3 LYS C  348  THR C  363  1                                  16    
HELIX   22 AC4 ARG C  366  HIS C  376  1                                  11    
HELIX   23 AC5 LEU C  378  LYS C  388  1                                  11    
HELIX   24 AC6 ASP C  390  GLY C  408  1                                  19    
HELIX   25 AC7 THR C  409  CYS C  419  1                                  11    
HELIX   26 AC8 ILE C  421  LEU C  428  1                                   8    
HELIX   27 AC9 LEU C  429  ALA C  431  5                                   3    
HELIX   28 AD1 ASP C  433  LEU C  454  1                                  22    
HELIX   29 AD2 GLU C  456  CYS C  467  1                                  12    
HELIX   30 AD3 GLY C  468  LEU C  476  1                                   9    
HELIX   31 AD4 GLN C  477  HIS C  479  5                                   3    
HELIX   32 AD5 ASN C  481  PHE C  496  1                                  16    
CISPEP   1 ASN C  241    PRO C  242          0         1.38                     
CRYST1   78.640   89.980  100.500  90.00  90.00  90.00 P 21 21 21    4          
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      0.012716  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011114  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009950        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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